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Database: PDB
Entry: 3R8F
LinkDB: 3R8F
Original site: 3R8F 
HEADER    REPLICATION ACTIVATOR/DNA               23-MAR-11   3R8F              
TITLE     REPLICATION INITIATOR DNAA BOUND TO AMPPCP AND SINGLE-STRANDED DNA    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA;            
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 76-399;                                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: 5'-D(P*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*A)-3';             
COMPND   8 CHAIN: E;                                                            
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;                               
SOURCE   3 ORGANISM_TAXID: 63363;                                               
SOURCE   4 STRAIN: VF5;                                                         
SOURCE   5 GENE: AQ_322, DNAA;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES                                                       
KEYWDS    AAA+ ATPASE, REPLICATION INITIATOR, DNA BINDING, REPLICATION          
KEYWDS   2 ACTIVATOR-DNA COMPLEX                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.E.DUDERSTADT,K.CHUANG,J.M.BERGER                                    
REVDAT   5   09-SEP-15 3R8F    1       TITLE                                    
REVDAT   4   28-MAR-12 3R8F    1       JRNL                                     
REVDAT   3   22-FEB-12 3R8F    1       HET    HETATM HETNAM HETSYN              
REVDAT   3 2                   1       REMARK                                   
REVDAT   2   19-OCT-11 3R8F    1       JRNL                                     
REVDAT   1   28-SEP-11 3R8F    0                                                
JRNL        AUTH   K.E.DUDERSTADT,K.CHUANG,J.M.BERGER                           
JRNL        TITL   DNA STRETCHING BY BACTERIAL INITIATORS PROMOTES REPLICATION  
JRNL        TITL 2 ORIGIN OPENING.                                              
JRNL        REF    NATURE                        V. 478   209 2011              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   21964332                                                     
JRNL        DOI    10.1038/NATURE10455                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.37 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.37                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.49                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 32803                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.250                           
REMARK   3   R VALUE            (WORKING SET) : 0.249                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1663                            
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 43.4907 -  7.6926    0.96     2704   133  0.2179 0.2132        
REMARK   3     2  7.6926 -  6.1113    0.98     2634   138  0.2785 0.3035        
REMARK   3     3  6.1113 -  5.3403    0.99     2610   150  0.2848 0.3437        
REMARK   3     4  5.3403 -  4.8528    0.99     2605   151  0.2069 0.2459        
REMARK   3     5  4.8528 -  4.5053    0.99     2600   133  0.2035 0.2304        
REMARK   3     6  4.5053 -  4.2399    0.99     2606   145  0.2262 0.2231        
REMARK   3     7  4.2399 -  4.0277    1.00     2596   150  0.2270 0.2507        
REMARK   3     8  4.0277 -  3.8525    1.00     2598   138  0.2719 0.3157        
REMARK   3     9  3.8525 -  3.7043    1.00     2587   125  0.2733 0.2896        
REMARK   3    10  3.7043 -  3.5765    1.00     2589   146  0.2783 0.2847        
REMARK   3    11  3.5765 -  3.4648    1.00     2573   124  0.3293 0.3180        
REMARK   3    12  3.4648 -  3.3660    0.94     2438   130  0.3823 0.4161        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.31                                          
REMARK   3   B_SOL              : 66.67                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.460            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.720           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 85.47                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -6.18040                                             
REMARK   3    B22 (A**2) : 20.58500                                             
REMARK   3    B33 (A**2) : -14.40460                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009          11529                                  
REMARK   3   ANGLE     :  0.864          14840                                  
REMARK   3   CHIRALITY :  0.043           1648                                  
REMARK   3   PLANARITY :  0.003           1812                                  
REMARK   3   DIHEDRAL  : 18.557           4397                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain A and resseq 77:241                              
REMARK   3    ORIGIN FOR THE GROUP (A): -14.6757 -16.3973  19.6790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3701 T22:   0.3710                                     
REMARK   3      T33:   0.3382 T12:   0.0811                                     
REMARK   3      T13:  -0.0096 T23:  -0.0930                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1393 L22:   0.4722                                     
REMARK   3      L33:   3.5563 L12:   0.8747                                     
REMARK   3      L13:  -1.0151 L23:   0.9902                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1180 S12:   0.1314 S13:   0.0687                       
REMARK   3      S21:   0.0426 S22:  -0.1731 S23:   0.1148                       
REMARK   3      S31:   0.0075 S32:  -0.1450 S33:  -0.0010                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain B and resseq 77:241                              
REMARK   3    ORIGIN FOR THE GROUP (A): -32.1692  -2.1246  38.9260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4641 T22:   0.4578                                     
REMARK   3      T33:   0.4839 T12:   0.0768                                     
REMARK   3      T13:  -0.0509 T23:  -0.1861                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9257 L22:   1.2143                                     
REMARK   3      L33:   3.9970 L12:   1.3978                                     
REMARK   3      L13:   0.2035 L23:   1.0032                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0711 S12:  -0.0748 S13:   0.1333                       
REMARK   3      S21:   0.1542 S22:  -0.1934 S23:   0.1188                       
REMARK   3      S31:   0.1878 S32:   0.0808 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain C and resseq 77:241                              
REMARK   3    ORIGIN FOR THE GROUP (A): -30.7053  11.8644  64.9840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5288 T22:   0.4717                                     
REMARK   3      T33:   0.5118 T12:  -0.0605                                     
REMARK   3      T13:  -0.0061 T23:  -0.1805                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9989 L22:   1.0709                                     
REMARK   3      L33:   1.5975 L12:   1.9348                                     
REMARK   3      L13:   1.2925 L23:   0.6769                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1704 S12:  -0.0680 S13:   0.0578                       
REMARK   3      S21:   0.1012 S22:  -0.2259 S23:   0.0264                       
REMARK   3      S31:  -0.0726 S32:   0.0475 S33:   0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain D and resseq 77:241                              
REMARK   3    ORIGIN FOR THE GROUP (A): -11.2169  26.1137  82.3417              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3624 T22:   0.4275                                     
REMARK   3      T33:   0.4076 T12:  -0.0556                                     
REMARK   3      T13:   0.0501 T23:  -0.0346                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4186 L22:   0.6692                                     
REMARK   3      L33:   2.0363 L12:   0.8104                                     
REMARK   3      L13:  -0.8330 L23:  -1.2202                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2894 S12:  -0.0578 S13:  -0.1884                       
REMARK   3      S21:   0.0397 S22:  -0.0456 S23:  -0.1791                       
REMARK   3      S31:  -0.0063 S32:  -0.1389 S33:   0.0000                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain A and resseq 242:290                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.4129 -35.3195  -0.6690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4661 T22:   0.7174                                     
REMARK   3      T33:   0.6651 T12:   0.0598                                     
REMARK   3      T13:   0.0348 T23:  -0.3649                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7483 L22:   0.9002                                     
REMARK   3      L33:   0.2699 L12:  -0.7457                                     
REMARK   3      L13:  -0.2643 L23:   0.5283                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1740 S12:   0.3600 S13:  -0.6917                       
REMARK   3      S21:   0.0622 S22:  -0.1903 S23:  -0.0955                       
REMARK   3      S31:  -0.3332 S32:  -0.5269 S33:  -0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain B and resseq 242:290                             
REMARK   3    ORIGIN FOR THE GROUP (A): -40.6837 -20.6572  18.3254              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4938 T22:   0.6812                                     
REMARK   3      T33:   0.6075 T12:  -0.0498                                     
REMARK   3      T13:   0.0167 T23:  -0.3887                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2756 L22:   0.7532                                     
REMARK   3      L33:   0.8708 L12:  -0.6550                                     
REMARK   3      L13:  -0.1347 L23:   0.7408                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5914 S12:   0.0122 S13:  -0.0311                       
REMARK   3      S21:  -0.1745 S22:  -0.0584 S23:   0.0070                       
REMARK   3      S31:   0.2652 S32:   0.0676 S33:  -0.0012                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain C and resseq 242:290                             
REMARK   3    ORIGIN FOR THE GROUP (A): -51.1465  -6.7552  56.5918              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6447 T22:   0.7024                                     
REMARK   3      T33:   0.8355 T12:  -0.1750                                     
REMARK   3      T13:   0.1798 T23:  -0.4604                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7153 L22:   0.5794                                     
REMARK   3      L33:   0.7056 L12:   0.6056                                     
REMARK   3      L13:  -0.0053 L23:   0.1170                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2503 S12:   0.6179 S13:  -0.0271                       
REMARK   3      S21:  -0.0205 S22:  -0.6151 S23:   0.2241                       
REMARK   3      S31:   0.2876 S32:  -0.4439 S33:  -0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain D and resseq 242:290                             
REMARK   3    ORIGIN FOR THE GROUP (A): -31.3556   7.1571  90.8350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6387 T22:   0.7067                                     
REMARK   3      T33:   0.5328 T12:  -0.2912                                     
REMARK   3      T13:   0.0042 T23:   0.0610                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8808 L22:   1.2567                                     
REMARK   3      L33:   0.6307 L12:   1.1841                                     
REMARK   3      L13:   0.2263 L23:   0.1357                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0253 S12:  -0.1643 S13:   0.2782                       
REMARK   3      S21:  -0.6309 S22:  -0.0141 S23:   0.4643                       
REMARK   3      S31:   0.4594 S32:  -1.1570 S33:  -0.0000                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain A and resseq 291:399                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.5168 -57.4281  16.3206              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1196 T22:   0.0972                                     
REMARK   3      T33:   0.6063 T12:  -0.0135                                     
REMARK   3      T13:  -0.0120 T23:  -0.3072                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7722 L22:   2.1181                                     
REMARK   3      L33:   3.6346 L12:   0.0437                                     
REMARK   3      L13:   0.0237 L23:  -2.0551                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6636 S12:  -0.1458 S13:  -0.1295                       
REMARK   3      S21:  -0.4947 S22:  -1.1891 S23:  -0.3239                       
REMARK   3      S31:   0.4967 S32:   1.6215 S33:  -0.2676                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: chain B and resseq 291:399                             
REMARK   3    ORIGIN FOR THE GROUP (A): -30.7741 -43.0580  32.2968              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8161 T22:   0.7502                                     
REMARK   3      T33:   0.9783 T12:  -0.1608                                     
REMARK   3      T13:   0.2466 T23:  -0.0436                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4233 L22:   0.7000                                     
REMARK   3      L33:   0.7986 L12:   0.7110                                     
REMARK   3      L13:  -0.3664 L23:  -0.5746                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3915 S12:  -0.2321 S13:  -0.4996                       
REMARK   3      S21:  -0.3403 S22:  -0.9482 S23:  -0.1713                       
REMARK   3      S31:  -0.6090 S32:   0.4811 S33:  -0.0150                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: chain C and resseq 291:399                             
REMARK   3    ORIGIN FOR THE GROUP (A): -34.1015 -29.0465  58.9862              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7577 T22:   0.6546                                     
REMARK   3      T33:   1.0636 T12:  -0.3142                                     
REMARK   3      T13:   0.1354 T23:   0.0171                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0339 L22:   0.1015                                     
REMARK   3      L33:   0.7181 L12:   0.0556                                     
REMARK   3      L13:   0.1699 L23:   0.1090                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2314 S12:   0.2514 S13:   0.3019                       
REMARK   3      S21:   0.2215 S22:  -1.0286 S23:   0.1554                       
REMARK   3      S31:   0.4221 S32:  -0.6550 S33:  -0.0219                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: chain D and resseq 291:399                             
REMARK   3    ORIGIN FOR THE GROUP (A): -17.3476 -14.8751  80.4037              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3809 T22:   0.8531                                     
REMARK   3      T33:   1.0923 T12:  -0.1256                                     
REMARK   3      T13:  -0.0934 T23:   0.0778                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8919 L22:   0.2722                                     
REMARK   3      L33:   0.0169 L12:  -0.9275                                     
REMARK   3      L13:   0.3077 L23:  -0.0898                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2032 S12:  -0.2571 S13:   0.7898                       
REMARK   3      S21:  -0.2252 S22:  -0.3069 S23:   0.3274                       
REMARK   3      S31:   0.7809 S32:  -0.2687 S33:  -0.0000                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN B AND NOT RESSEQ 255:265              
REMARK   3     SELECTION          : CHAIN A AND NOT RESSEQ 255:265              
REMARK   3     ATOM PAIRS NUMBER  : 2552                                        
REMARK   3     RMSD               : 0.059                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN B AND NOT RESSEQ 255:265              
REMARK   3     SELECTION          : CHAIN C AND NOT RESSEQ 255:265              
REMARK   3     ATOM PAIRS NUMBER  : 2552                                        
REMARK   3     RMSD               : 0.056                                       
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: CHAIN B AND NOT RESSEQ 255:265              
REMARK   3     SELECTION          : CHAIN D AND NOT RESSEQ 255:265              
REMARK   3     ATOM PAIRS NUMBER  : 2552                                        
REMARK   3     RMSD               : 0.063                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3R8F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB064619.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JUL-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1159                             
REMARK 200  MONOCHROMATOR                  : DOUBLE FLAT CRYSTAL, SI(111)       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32862                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.47                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.61200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX (PHENIX.AUTOMR)                                
REMARK 200 STARTING MODEL: PDB ENTRY 2HCB                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-35 MM SODIUM CACODYLATE, PH 6.5,      
REMARK 280  26% 1,2-PROPANEDIOL, 1-2% PEG2000 MME, VAPOR DIFFUSION, HANGING     
REMARK 280  DROP, TEMPERATURE 291K                                              
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       49.89850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      100.63300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.10950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      100.63300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       49.89850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.10950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
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     LYS A    76                                                      
REMARK 465     ARG A   328                                                      
REMARK 465     LYS A   378                                                      
REMARK 465     LYS A   379                                                      
REMARK 465     ASP A   380                                                      
REMARK 465     LYS B    76                                                      
REMARK 465     ARG B   328                                                      
REMARK 465     LYS B   378                                                      
REMARK 465     LYS B   379                                                      
REMARK 465     ASP B   380                                                      
REMARK 465     LYS C    76                                                      
REMARK 465     ARG C   328                                                      
REMARK 465     LYS C   378                                                      
REMARK 465     LYS C   379                                                      
REMARK 465     ASP C   380                                                      
REMARK 465     LYS D    76                                                      
REMARK 465     ARG D   328                                                      
REMARK 465     LYS D   378                                                      
REMARK 465     LYS D   379                                                      
REMARK 465     ASP D   380                                                      
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   CA   GLY B   124     O2A  ACP B   700              2.11            
REMARK 500   O2'  ACP B   700     O    HOH B     9              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE2  GLU A   292     OD1  ASN B   258     4545     1.78            
REMARK 500   OE1  GLU A   292     OE2  GLU B   260     4545     2.11            
REMARK 500   OD1  ASN A   258     CB   LYS B   263     4545     2.14            
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 146      141.34   -170.78                                   
REMARK 500    PRO A 217      -35.58    -37.16                                   
REMARK 500    PHE A 311      -52.73   -125.25                                   
REMARK 500    LYS A 330        0.62     83.80                                   
REMARK 500    ASP A 362       -4.60     85.92                                   
REMARK 500    SER B 146      141.37   -170.78                                   
REMARK 500    PRO B 217      -35.68    -37.05                                   
REMARK 500    LEU B 261        3.68     82.51                                   
REMARK 500    PHE B 311      -52.76   -125.21                                   
REMARK 500    LYS B 330        0.60     83.81                                   
REMARK 500    ASP B 362       -4.62     85.94                                   
REMARK 500    SER C 146      141.34   -170.77                                   
REMARK 500    PRO C 217      -35.58    -37.12                                   
REMARK 500    PHE C 311      -52.81   -125.17                                   
REMARK 500    LYS C 330        0.54     83.88                                   
REMARK 500    ASP C 362       -4.67     85.94                                   
REMARK 500    SER D 146      141.33   -170.80                                   
REMARK 500    PRO D 217      -35.66    -37.08                                   
REMARK 500    PHE D 311      -52.81   -125.23                                   
REMARK 500    LYS D 330        0.62     83.77                                   
REMARK 500    ASP D 362       -4.60     85.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR D 126   OG1                                                    
REMARK 620 2 ACP D 700   O3G 105.5                                              
REMARK 620 3 ACP D 700   O1B  55.2  60.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C 126   OG1                                                    
REMARK 620 2 ACP C 700   O3G 104.1                                              
REMARK 620 3 ACP C 700   O1B  57.2  60.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B 126   OG1                                                    
REMARK 620 2 ACP B 700   O1G 100.7                                              
REMARK 620 3 ACP B 700   O1B  59.8  57.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 126   OG1                                                    
REMARK 620 2 ACP A 700   O3G  99.7                                              
REMARK 620 3 ACP A 700   O2B  55.4  56.0                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP A 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP B 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP C 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP D 700                 
DBREF  3R8F A   76   399  UNP    O66659   DNAA_AQUAE      76    399             
DBREF  3R8F B   76   399  UNP    O66659   DNAA_AQUAE      76    399             
DBREF  3R8F C   76   399  UNP    O66659   DNAA_AQUAE      76    399             
DBREF  3R8F D   76   399  UNP    O66659   DNAA_AQUAE      76    399             
DBREF  3R8F E    1    12  PDB    3R8F     3R8F             1     12             
SEQRES   1 A  324  LYS ASP PHE LEU ASN PRO LYS TYR THR LEU GLU ASN PHE          
SEQRES   2 A  324  ILE VAL GLY GLU GLY ASN ARG LEU ALA TYR GLU VAL VAL          
SEQRES   3 A  324  LYS GLU ALA LEU GLU ASN LEU GLY SER LEU TYR ASN PRO          
SEQRES   4 A  324  ILE PHE ILE TYR GLY SER VAL GLY THR GLY LYS THR HIS          
SEQRES   5 A  324  LEU LEU GLN ALA ALA GLY ASN GLU ALA LYS LYS ARG GLY          
SEQRES   6 A  324  TYR ARG VAL ILE TYR SER SER ALA ASP ASP PHE ALA GLN          
SEQRES   7 A  324  ALA MET VAL GLU HIS LEU LYS LYS GLY THR ILE ASN GLU          
SEQRES   8 A  324  PHE ARG ASN MET TYR LYS SER VAL ASP LEU LEU LEU LEU          
SEQRES   9 A  324  ASP ASP VAL GLN PHE LEU SER GLY LYS GLU ARG THR GLN          
SEQRES  10 A  324  ILE GLU PHE PHE HIS ILE PHE ASN THR LEU TYR LEU LEU          
SEQRES  11 A  324  GLU LYS GLN ILE ILE LEU ALA SER ASP ARG HIS PRO GLN          
SEQRES  12 A  324  LYS LEU ASP GLY VAL SER ASP ARG LEU VAL SER ARG PHE          
SEQRES  13 A  324  GLU GLY GLY ILE LEU VAL GLU ILE GLU LEU ASP ASN LYS          
SEQRES  14 A  324  THR ARG PHE LYS ILE ILE LYS GLU LYS LEU LYS GLU PHE          
SEQRES  15 A  324  ASN LEU GLU LEU ARG LYS GLU VAL ILE ASP TYR LEU LEU          
SEQRES  16 A  324  GLU ASN THR LYS ASN VAL ARG GLU ILE GLU GLY LYS ILE          
SEQRES  17 A  324  LYS LEU ILE LYS LEU LYS GLY PHE GLU GLY LEU GLU ARG          
SEQRES  18 A  324  LYS GLU ARG LYS GLU ARG ASP LYS LEU MET GLN ILE VAL          
SEQRES  19 A  324  GLU PHE VAL ALA ASN TYR TYR ALA VAL LYS VAL GLU ASP          
SEQRES  20 A  324  ILE LEU SER ASP LYS ARG ASN LYS ARG THR SER GLU ALA          
SEQRES  21 A  324  ARG LYS ILE ALA MET TYR LEU CYS ARG LYS VAL CYS SER          
SEQRES  22 A  324  ALA SER LEU ILE GLU ILE ALA ARG ALA PHE LYS ARG LYS          
SEQRES  23 A  324  ASP HIS THR THR VAL ILE HIS ALA ILE ARG SER VAL GLU          
SEQRES  24 A  324  GLU GLU LYS LYS LYS ASP ARG LYS PHE LYS HIS LEU VAL          
SEQRES  25 A  324  GLY PHE LEU GLU LYS GLN ALA PHE ASP LYS ILE CYS              
SEQRES   1 B  324  LYS ASP PHE LEU ASN PRO LYS TYR THR LEU GLU ASN PHE          
SEQRES   2 B  324  ILE VAL GLY GLU GLY ASN ARG LEU ALA TYR GLU VAL VAL          
SEQRES   3 B  324  LYS GLU ALA LEU GLU ASN LEU GLY SER LEU TYR ASN PRO          
SEQRES   4 B  324  ILE PHE ILE TYR GLY SER VAL GLY THR GLY LYS THR HIS          
SEQRES   5 B  324  LEU LEU GLN ALA ALA GLY ASN GLU ALA LYS LYS ARG GLY          
SEQRES   6 B  324  TYR ARG VAL ILE TYR SER SER ALA ASP ASP PHE ALA GLN          
SEQRES   7 B  324  ALA MET VAL GLU HIS LEU LYS LYS GLY THR ILE ASN GLU          
SEQRES   8 B  324  PHE ARG ASN MET TYR LYS SER VAL ASP LEU LEU LEU LEU          
SEQRES   9 B  324  ASP ASP VAL GLN PHE LEU SER GLY LYS GLU ARG THR GLN          
SEQRES  10 B  324  ILE GLU PHE PHE HIS ILE PHE ASN THR LEU TYR LEU LEU          
SEQRES  11 B  324  GLU LYS GLN ILE ILE LEU ALA SER ASP ARG HIS PRO GLN          
SEQRES  12 B  324  LYS LEU ASP GLY VAL SER ASP ARG LEU VAL SER ARG PHE          
SEQRES  13 B  324  GLU GLY GLY ILE LEU VAL GLU ILE GLU LEU ASP ASN LYS          
SEQRES  14 B  324  THR ARG PHE LYS ILE ILE LYS GLU LYS LEU LYS GLU PHE          
SEQRES  15 B  324  ASN LEU GLU LEU ARG LYS GLU VAL ILE ASP TYR LEU LEU          
SEQRES  16 B  324  GLU ASN THR LYS ASN VAL ARG GLU ILE GLU GLY LYS ILE          
SEQRES  17 B  324  LYS LEU ILE LYS LEU LYS GLY PHE GLU GLY LEU GLU ARG          
SEQRES  18 B  324  LYS GLU ARG LYS GLU ARG ASP LYS LEU MET GLN ILE VAL          
SEQRES  19 B  324  GLU PHE VAL ALA ASN TYR TYR ALA VAL LYS VAL GLU ASP          
SEQRES  20 B  324  ILE LEU SER ASP LYS ARG ASN LYS ARG THR SER GLU ALA          
SEQRES  21 B  324  ARG LYS ILE ALA MET TYR LEU CYS ARG LYS VAL CYS SER          
SEQRES  22 B  324  ALA SER LEU ILE GLU ILE ALA ARG ALA PHE LYS ARG LYS          
SEQRES  23 B  324  ASP HIS THR THR VAL ILE HIS ALA ILE ARG SER VAL GLU          
SEQRES  24 B  324  GLU GLU LYS LYS LYS ASP ARG LYS PHE LYS HIS LEU VAL          
SEQRES  25 B  324  GLY PHE LEU GLU LYS GLN ALA PHE ASP LYS ILE CYS              
SEQRES   1 C  324  LYS ASP PHE LEU ASN PRO LYS TYR THR LEU GLU ASN PHE          
SEQRES   2 C  324  ILE VAL GLY GLU GLY ASN ARG LEU ALA TYR GLU VAL VAL          
SEQRES   3 C  324  LYS GLU ALA LEU GLU ASN LEU GLY SER LEU TYR ASN PRO          
SEQRES   4 C  324  ILE PHE ILE TYR GLY SER VAL GLY THR GLY LYS THR HIS          
SEQRES   5 C  324  LEU LEU GLN ALA ALA GLY ASN GLU ALA LYS LYS ARG GLY          
SEQRES   6 C  324  TYR ARG VAL ILE TYR SER SER ALA ASP ASP PHE ALA GLN          
SEQRES   7 C  324  ALA MET VAL GLU HIS LEU LYS LYS GLY THR ILE ASN GLU          
SEQRES   8 C  324  PHE ARG ASN MET TYR LYS SER VAL ASP LEU LEU LEU LEU          
SEQRES   9 C  324  ASP ASP VAL GLN PHE LEU SER GLY LYS GLU ARG THR GLN          
SEQRES  10 C  324  ILE GLU PHE PHE HIS ILE PHE ASN THR LEU TYR LEU LEU          
SEQRES  11 C  324  GLU LYS GLN ILE ILE LEU ALA SER ASP ARG HIS PRO GLN          
SEQRES  12 C  324  LYS LEU ASP GLY VAL SER ASP ARG LEU VAL SER ARG PHE          
SEQRES  13 C  324  GLU GLY GLY ILE LEU VAL GLU ILE GLU LEU ASP ASN LYS          
SEQRES  14 C  324  THR ARG PHE LYS ILE ILE LYS GLU LYS LEU LYS GLU PHE          
SEQRES  15 C  324  ASN LEU GLU LEU ARG LYS GLU VAL ILE ASP TYR LEU LEU          
SEQRES  16 C  324  GLU ASN THR LYS ASN VAL ARG GLU ILE GLU GLY LYS ILE          
SEQRES  17 C  324  LYS LEU ILE LYS LEU LYS GLY PHE GLU GLY LEU GLU ARG          
SEQRES  18 C  324  LYS GLU ARG LYS GLU ARG ASP LYS LEU MET GLN ILE VAL          
SEQRES  19 C  324  GLU PHE VAL ALA ASN TYR TYR ALA VAL LYS VAL GLU ASP          
SEQRES  20 C  324  ILE LEU SER ASP LYS ARG ASN LYS ARG THR SER GLU ALA          
SEQRES  21 C  324  ARG LYS ILE ALA MET TYR LEU CYS ARG LYS VAL CYS SER          
SEQRES  22 C  324  ALA SER LEU ILE GLU ILE ALA ARG ALA PHE LYS ARG LYS          
SEQRES  23 C  324  ASP HIS THR THR VAL ILE HIS ALA ILE ARG SER VAL GLU          
SEQRES  24 C  324  GLU GLU LYS LYS LYS ASP ARG LYS PHE LYS HIS LEU VAL          
SEQRES  25 C  324  GLY PHE LEU GLU LYS GLN ALA PHE ASP LYS ILE CYS              
SEQRES   1 D  324  LYS ASP PHE LEU ASN PRO LYS TYR THR LEU GLU ASN PHE          
SEQRES   2 D  324  ILE VAL GLY GLU GLY ASN ARG LEU ALA TYR GLU VAL VAL          
SEQRES   3 D  324  LYS GLU ALA LEU GLU ASN LEU GLY SER LEU TYR ASN PRO          
SEQRES   4 D  324  ILE PHE ILE TYR GLY SER VAL GLY THR GLY LYS THR HIS          
SEQRES   5 D  324  LEU LEU GLN ALA ALA GLY ASN GLU ALA LYS LYS ARG GLY          
SEQRES   6 D  324  TYR ARG VAL ILE TYR SER SER ALA ASP ASP PHE ALA GLN          
SEQRES   7 D  324  ALA MET VAL GLU HIS LEU LYS LYS GLY THR ILE ASN GLU          
SEQRES   8 D  324  PHE ARG ASN MET TYR LYS SER VAL ASP LEU LEU LEU LEU          
SEQRES   9 D  324  ASP ASP VAL GLN PHE LEU SER GLY LYS GLU ARG THR GLN          
SEQRES  10 D  324  ILE GLU PHE PHE HIS ILE PHE ASN THR LEU TYR LEU LEU          
SEQRES  11 D  324  GLU LYS GLN ILE ILE LEU ALA SER ASP ARG HIS PRO GLN          
SEQRES  12 D  324  LYS LEU ASP GLY VAL SER ASP ARG LEU VAL SER ARG PHE          
SEQRES  13 D  324  GLU GLY GLY ILE LEU VAL GLU ILE GLU LEU ASP ASN LYS          
SEQRES  14 D  324  THR ARG PHE LYS ILE ILE LYS GLU LYS LEU LYS GLU PHE          
SEQRES  15 D  324  ASN LEU GLU LEU ARG LYS GLU VAL ILE ASP TYR LEU LEU          
SEQRES  16 D  324  GLU ASN THR LYS ASN VAL ARG GLU ILE GLU GLY LYS ILE          
SEQRES  17 D  324  LYS LEU ILE LYS LEU LYS GLY PHE GLU GLY LEU GLU ARG          
SEQRES  18 D  324  LYS GLU ARG LYS GLU ARG ASP LYS LEU MET GLN ILE VAL          
SEQRES  19 D  324  GLU PHE VAL ALA ASN TYR TYR ALA VAL LYS VAL GLU ASP          
SEQRES  20 D  324  ILE LEU SER ASP LYS ARG ASN LYS ARG THR SER GLU ALA          
SEQRES  21 D  324  ARG LYS ILE ALA MET TYR LEU CYS ARG LYS VAL CYS SER          
SEQRES  22 D  324  ALA SER LEU ILE GLU ILE ALA ARG ALA PHE LYS ARG LYS          
SEQRES  23 D  324  ASP HIS THR THR VAL ILE HIS ALA ILE ARG SER VAL GLU          
SEQRES  24 D  324  GLU GLU LYS LYS LYS ASP ARG LYS PHE LYS HIS LEU VAL          
SEQRES  25 D  324  GLY PHE LEU GLU LYS GLN ALA PHE ASP LYS ILE CYS              
SEQRES   1 E   12   DA  DA  DA  DA  DA  DA  DA  DA  DA  DA  DA  DA              
HET     MG  A 401       1                                                       
HET    ACP  A 700      31                                                       
HET     MG  B 401       1                                                       
HET    ACP  B 700      31                                                       
HET     MG  C 401       1                                                       
HET    ACP  C 700      31                                                       
HET     MG  D 401       1                                                       
HET    ACP  D 700      31                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER                     
HETSYN     ACP ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE                 
FORMUL   6   MG    4(MG 2+)                                                     
FORMUL   7  ACP    4(C11 H18 N5 O12 P3)                                         
FORMUL  14  HOH   *22(H2 O)                                                     
HELIX    1   1 ASN A   94  ASN A  107  1                                  14    
HELIX    2   2 GLY A  124  ARG A  139  1                                  16    
HELIX    3   3 ALA A  148  LYS A  161  1                                  14    
HELIX    4   4 THR A  163  SER A  173  1                                  11    
HELIX    5   5 ASP A  181  SER A  186  5                                   6    
HELIX    6   6 LYS A  188  LEU A  205  1                                  18    
HELIX    7   7 HIS A  216  LEU A  220  5                                   5    
HELIX    8   8 SER A  224  GLY A  233  1                                  10    
HELIX    9   9 ASP A  242  PHE A  257  1                                  16    
HELIX   10  10 ARG A  262  THR A  273  1                                  12    
HELIX   11  11 ASN A  275  GLY A  290  1                                  16    
HELIX   12  12 GLY A  290  LYS A  304  1                                  15    
HELIX   13  13 MET A  306  PHE A  311  1                                   6    
HELIX   14  14 PHE A  311  TYR A  316  1                                   6    
HELIX   15  15 LYS A  319  SER A  325  1                                   7    
HELIX   16  16 THR A  332  VAL A  346  1                                  15    
HELIX   17  17 SER A  350  LYS A  359  1                                  10    
HELIX   18  18 THR A  364  GLU A  376  1                                  13    
HELIX   19  19 LYS A  382  CYS A  399  1                                  18    
HELIX   20  20 ASN B   94  ASN B  107  1                                  14    
HELIX   21  21 GLY B  124  ARG B  139  1                                  16    
HELIX   22  22 ALA B  148  LYS B  161  1                                  14    
HELIX   23  23 THR B  163  SER B  173  1                                  11    
HELIX   24  24 ASP B  181  SER B  186  5                                   6    
HELIX   25  25 LYS B  188  LEU B  205  1                                  18    
HELIX   26  26 HIS B  216  LEU B  220  5                                   5    
HELIX   27  27 SER B  224  GLY B  233  1                                  10    
HELIX   28  28 ASP B  242  PHE B  257  1                                  16    
HELIX   29  29 ARG B  262  THR B  273  1                                  12    
HELIX   30  30 ASN B  275  GLY B  290  1                                  16    
HELIX   31  31 GLY B  290  LYS B  304  1                                  15    
HELIX   32  32 MET B  306  PHE B  311  1                                   6    
HELIX   33  33 PHE B  311  TYR B  316  1                                   6    
HELIX   34  34 LYS B  319  SER B  325  1                                   7    
HELIX   35  35 THR B  332  VAL B  346  1                                  15    
HELIX   36  36 SER B  350  LYS B  359  1                                  10    
HELIX   37  37 THR B  364  GLU B  376  1                                  13    
HELIX   38  38 LYS B  382  CYS B  399  1                                  18    
HELIX   39  39 ASN C   94  ASN C  107  1                                  14    
HELIX   40  40 GLY C  124  ARG C  139  1                                  16    
HELIX   41  41 ALA C  148  LYS C  161  1                                  14    
HELIX   42  42 THR C  163  SER C  173  1                                  11    
HELIX   43  43 ASP C  181  SER C  186  5                                   6    
HELIX   44  44 LYS C  188  LEU C  205  1                                  18    
HELIX   45  45 HIS C  216  LEU C  220  5                                   5    
HELIX   46  46 SER C  224  GLY C  233  1                                  10    
HELIX   47  47 ASP C  242  PHE C  257  1                                  16    
HELIX   48  48 ARG C  262  THR C  273  1                                  12    
HELIX   49  49 ASN C  275  GLY C  290  1                                  16    
HELIX   50  50 GLY C  290  LYS C  304  1                                  15    
HELIX   51  51 MET C  306  PHE C  311  1                                   6    
HELIX   52  52 PHE C  311  TYR C  316  1                                   6    
HELIX   53  53 LYS C  319  SER C  325  1                                   7    
HELIX   54  54 THR C  332  VAL C  346  1                                  15    
HELIX   55  55 SER C  350  LYS C  359  1                                  10    
HELIX   56  56 THR C  364  GLU C  376  1                                  13    
HELIX   57  57 LYS C  382  CYS C  399  1                                  18    
HELIX   58  58 ASN D   94  ASN D  107  1                                  14    
HELIX   59  59 GLY D  124  ARG D  139  1                                  16    
HELIX   60  60 ALA D  148  LYS D  161  1                                  14    
HELIX   61  61 THR D  163  SER D  173  1                                  11    
HELIX   62  62 ASP D  181  SER D  186  5                                   6    
HELIX   63  63 LYS D  188  LEU D  205  1                                  18    
HELIX   64  64 HIS D  216  LEU D  220  5                                   5    
HELIX   65  65 SER D  224  GLY D  233  1                                  10    
HELIX   66  66 ASP D  242  PHE D  257  1                                  16    
HELIX   67  67 ARG D  262  THR D  273  1                                  12    
HELIX   68  68 ASN D  275  GLY D  290  1                                  16    
HELIX   69  69 GLY D  290  LYS D  304  1                                  15    
HELIX   70  70 MET D  306  PHE D  311  1                                   6    
HELIX   71  71 PHE D  311  TYR D  316  1                                   6    
HELIX   72  72 LYS D  319  SER D  325  1                                   7    
HELIX   73  73 THR D  332  VAL D  346  1                                  15    
HELIX   74  74 SER D  350  LYS D  359  1                                  10    
HELIX   75  75 THR D  364  GLU D  376  1                                  13    
HELIX   76  76 LYS D  382  CYS D  399  1                                  18    
SHEET    1   A 5 VAL A 143  SER A 147  0                                        
SHEET    2   A 5 LEU A 176  ASP A 180  1  O  LEU A 178   N  ILE A 144           
SHEET    3   A 5 GLN A 208  SER A 213  1  O  ILE A 210   N  LEU A 177           
SHEET    4   A 5 PRO A 114  GLY A 119  1  N  ILE A 115   O  LEU A 211           
SHEET    5   A 5 ILE A 235  ILE A 239  1  O  ILE A 235   N  PHE A 116           
SHEET    1   B 5 VAL B 143  SER B 147  0                                        
SHEET    2   B 5 LEU B 176  ASP B 180  1  O  LEU B 178   N  ILE B 144           
SHEET    3   B 5 GLN B 208  SER B 213  1  O  ILE B 210   N  LEU B 177           
SHEET    4   B 5 PRO B 114  GLY B 119  1  N  ILE B 115   O  LEU B 211           
SHEET    5   B 5 ILE B 235  ILE B 239  1  O  ILE B 235   N  PHE B 116           
SHEET    1   C 5 VAL C 143  SER C 147  0                                        
SHEET    2   C 5 LEU C 176  ASP C 180  1  O  LEU C 178   N  ILE C 144           
SHEET    3   C 5 GLN C 208  SER C 213  1  O  ILE C 210   N  LEU C 177           
SHEET    4   C 5 PRO C 114  GLY C 119  1  N  ILE C 115   O  LEU C 211           
SHEET    5   C 5 ILE C 235  ILE C 239  1  O  ILE C 235   N  PHE C 116           
SHEET    1   D 5 VAL D 143  SER D 147  0                                        
SHEET    2   D 5 LEU D 176  ASP D 180  1  O  LEU D 178   N  ILE D 144           
SHEET    3   D 5 GLN D 208  SER D 213  1  O  ILE D 210   N  LEU D 177           
SHEET    4   D 5 PRO D 114  GLY D 119  1  N  ILE D 115   O  LEU D 211           
SHEET    5   D 5 ILE D 235  ILE D 239  1  O  ILE D 235   N  PHE D 116           
LINK         OG1 THR D 126                MG    MG D 401     1555   1555  2.50  
LINK         OG1 THR C 126                MG    MG C 401     1555   1555  2.50  
LINK         OG1 THR B 126                MG    MG B 401     1555   1555  2.50  
LINK         OG1 THR A 126                MG    MG A 401     1555   1555  2.50  
LINK        MG    MG D 401                 O3G ACP D 700     1555   1555  1.79  
LINK        MG    MG A 401                 O3G ACP A 700     1555   1555  2.05  
LINK        MG    MG C 401                 O3G ACP C 700     1555   1555  2.07  
LINK        MG    MG B 401                 O1G ACP B 700     1555   1555  2.30  
LINK        MG    MG C 401                 O1B ACP C 700     1555   1555  2.47  
LINK        MG    MG B 401                 O1B ACP B 700     1555   1555  2.51  
LINK        MG    MG D 401                 O1B ACP D 700     1555   1555  2.61  
LINK        MG    MG A 401                 O2B ACP A 700     1555   1555  2.73  
SITE     1 AC1  4 THR A 126  ASP A 180  ASP A 181  ACP A 700                    
SITE     1 AC2 19 HOH A   3  TYR A  83  ASN A  87  PHE A  88                    
SITE     2 AC2 19 ILE A  89  ASN A  94  VAL A 121  GLY A 122                    
SITE     3 AC2 19 THR A 123  GLY A 124  LYS A 125  THR A 126                    
SITE     4 AC2 19 HIS A 127  LYS A 253  VAL A 276  ARG A 277                    
SITE     5 AC2 19 GLU A 280   MG A 401  ARG D 230                               
SITE     1 AC3  4 THR B 126  ASP B 180  ASP B 181  ACP B 700                    
SITE     1 AC4 18 ARG A 230  HOH B   9  TYR B  83  ASN B  87                    
SITE     2 AC4 18 PHE B  88  ILE B  89  VAL B 121  GLY B 122                    
SITE     3 AC4 18 THR B 123  GLY B 124  LYS B 125  THR B 126                    
SITE     4 AC4 18 HIS B 127  LYS B 253  VAL B 276  ARG B 277                    
SITE     5 AC4 18 GLU B 280   MG B 401                                          
SITE     1 AC5  4 THR C 126  ASP C 180  ASP C 181  ACP C 700                    
SITE     1 AC6 17 ARG B 230  ASN C  87  PHE C  88  ILE C  89                    
SITE     2 AC6 17 ASN C  94  VAL C 121  GLY C 122  THR C 123                    
SITE     3 AC6 17 GLY C 124  LYS C 125  THR C 126  HIS C 127                    
SITE     4 AC6 17 LYS C 253  VAL C 276  ARG C 277  GLU C 280                    
SITE     5 AC6 17  MG C 401                                                     
SITE     1 AC7  4 THR D 126  ASP D 180  ASP D 181  ACP D 700                    
SITE     1 AC8 19 ARG C 230  HOH D  22  TYR D  83  ASN D  87                    
SITE     2 AC8 19 PHE D  88  ILE D  89  ASN D  94  VAL D 121                    
SITE     3 AC8 19 GLY D 122  THR D 123  GLY D 124  LYS D 125                    
SITE     4 AC8 19 THR D 126  HIS D 127  LYS D 253  VAL D 276                    
SITE     5 AC8 19 ARG D 277  GLU D 280   MG D 401                               
CRYST1   99.797  114.219  201.266  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      0.010020  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008755  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004969        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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