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Database: PDB
Entry: 6P3W
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HEADER    CELL CYCLE                              24-MAY-19   6P3W              
TITLE     CRYSTAL STRUCTURE OF THE CYCLIN A-CDK2-ORC1 COMPLEX                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 2;                                 
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: CELL DIVISION PROTEIN KINASE 2,P33 PROTEIN KINASE;          
COMPND   5 EC: 2.7.11.22;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CYCLIN-A2;                                                 
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 SYNONYM: CYCLIN-A,CYCLIN A;                                          
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: ORC1 PEPTIDE;                                              
COMPND  14 CHAIN: E, F;                                                         
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CDK2, CDKN2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: CCNA2, CCN1, CCNA;                                             
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_TAXID: 9606;                                                
SOURCE  18 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    INHIBITOR COMPLEX, CELL CYCLE                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.WANG,J.SONG                                                         
REVDAT   1   31-JUL-19 6P3W    0                                                
JRNL        AUTH   B.WANG,J.SONG                                                
JRNL        TITL   STRUCTURAL BASIS FOR THE ORC1-CYCLIN A ASSOCIATION.          
JRNL        REF    PROTEIN SCI.                               2019              
JRNL        REFN                   ESSN 1469-896X                               
JRNL        PMID   31309634                                                     
JRNL        DOI    10.1002/PRO.3689                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.54 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.54                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.07                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 72395                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.120                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3709                            
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 20.0695 -  7.4019    1.00     2881   153  0.1424 0.2053        
REMARK   3     2  7.4019 -  5.9249    1.00     2726   172  0.1804 0.1824        
REMARK   3     3  5.9249 -  5.1907    1.00     2716   135  0.1754 0.2343        
REMARK   3     4  5.1907 -  4.7229    1.00     2688   157  0.1568 0.2149        
REMARK   3     5  4.7229 -  4.3882    1.00     2666   155  0.1565 0.1856        
REMARK   3     6  4.3882 -  4.1318    1.00     2649   145  0.1679 0.1953        
REMARK   3     7  4.1318 -  3.9265    1.00     2684   122  0.1746 0.2101        
REMARK   3     8  3.9265 -  3.7568    1.00     2651   140  0.1820 0.2160        
REMARK   3     9  3.7568 -  3.6130    1.00     2637   155  0.2012 0.2349        
REMARK   3    10  3.6130 -  3.4890    1.00     2625   157  0.2028 0.2550        
REMARK   3    11  3.4890 -  3.3804    1.00     2637   125  0.2264 0.2457        
REMARK   3    12  3.3804 -  3.2842    1.00     2644   133  0.2384 0.3016        
REMARK   3    13  3.2842 -  3.1981    1.00     2626   143  0.2547 0.3143        
REMARK   3    14  3.1981 -  3.1204    1.00     2603   148  0.2675 0.3251        
REMARK   3    15  3.1204 -  3.0497    1.00     2640   127  0.2712 0.3236        
REMARK   3    16  3.0497 -  2.9850    1.00     2631   128  0.2750 0.3253        
REMARK   3    17  2.9850 -  2.9255    1.00     2623   137  0.2839 0.3040        
REMARK   3    18  2.9255 -  2.8704    1.00     2612   129  0.2757 0.3014        
REMARK   3    19  2.8704 -  2.8193    1.00     2600   150  0.2779 0.2984        
REMARK   3    20  2.8193 -  2.7716    1.00     2623   129  0.2860 0.3268        
REMARK   3    21  2.7716 -  2.7270    1.00     2630   132  0.3028 0.3434        
REMARK   3    22  2.7270 -  2.6852    1.00     2590   150  0.3150 0.3261        
REMARK   3    23  2.6852 -  2.6458    1.00     2619   143  0.3185 0.3505        
REMARK   3    24  2.6458 -  2.6086    1.00     2563   156  0.3262 0.3167        
REMARK   3    25  2.6086 -  2.5734    0.99     2598   139  0.3497 0.4192        
REMARK   3    26  2.5734 -  2.5401    0.98     2524   149  0.3671 0.4146        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.000           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 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      :  0.003           9139                                  
REMARK   3   ANGLE     :  0.756          12437                                  
REMARK   3   CHIRALITY :  0.031           1418                                  
REMARK   3   PLANARITY :  0.005           1562                                  
REMARK   3   DIHEDRAL  : 13.614           3334                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 23                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 17 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -10.3412  90.7737  33.4585              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9512 T22:   0.9637                                     
REMARK   3      T33:   0.7215 T12:   0.1363                                     
REMARK   3      T13:   0.1929 T23:  -0.0711                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8378 L22:   7.9080                                     
REMARK   3      L33:   7.0706 L12:   1.9372                                     
REMARK   3      L13:   3.5641 L23:  -3.3061                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4220 S12:   1.6350 S13:  -0.4170                       
REMARK   3      S21:  -0.9923 S22:  -0.4685 S23:  -1.0186                       
REMARK   3      S31:   1.4428 S32:  -0.2950 S33:   1.0282                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 18 THROUGH 45 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.4606  86.0874  33.5734              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7375 T22:   0.6763                                     
REMARK   3      T33:   0.6140 T12:   0.0271                                     
REMARK   3      T13:   0.0799 T23:   0.0534                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5138 L22:   6.1210                                     
REMARK   3      L33:   3.8089 L12:  -4.5843                                     
REMARK   3      L13:  -4.2838 L23:   2.2522                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1763 S12:   0.3029 S13:  -0.1646                       
REMARK   3      S21:  -0.6809 S22:  -0.3952 S23:   0.7590                       
REMARK   3      S31:  -0.2095 S32:  -0.5139 S33:   0.3222                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 46 THROUGH 158 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   8.0065  89.5237  30.1511              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6935 T22:   0.5813                                     
REMARK   3      T33:   0.4763 T12:   0.0502                                     
REMARK   3      T13:   0.0727 T23:  -0.0329                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5908 L22:   2.5081                                     
REMARK   3      L33:   1.7253 L12:   0.5548                                     
REMARK   3      L13:  -0.5522 L23:  -0.6182                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1161 S12:  -0.0015 S13:  -0.1260                       
REMARK   3      S21:   0.1003 S22:   0.0223 S23:   0.1434                       
REMARK   3      S31:   0.0306 S32:  -0.0718 S33:   0.1295                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 159 THROUGH 298 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  20.4596  92.6375  15.2243              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6603 T22:   0.5382                                     
REMARK   3      T33:   0.4775 T12:   0.0398                                     
REMARK   3      T13:   0.1186 T23:   0.0384                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9106 L22:   3.5958                                     
REMARK   3      L33:   4.5815 L12:   0.3738                                     
REMARK   3      L13:  -0.1842 L23:   0.4615                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1357 S12:   0.2551 S13:  -0.1334                       
REMARK   3      S21:  -0.4983 S22:   0.0425 S23:  -0.3655                       
REMARK   3      S31:   0.1540 S32:   0.1628 S33:   0.0900                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 176 THROUGH 192 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  20.9079  73.4490  36.2041              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9798 T22:   0.7634                                     
REMARK   3      T33:   0.7227 T12:   0.1304                                     
REMARK   3      T13:   0.0452 T23:  -0.1077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1947 L22:   3.4878                                     
REMARK   3      L33:   6.9704 L12:   0.9879                                     
REMARK   3      L13:   3.9177 L23:  -3.6365                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4069 S12:   0.0643 S13:   0.5285                       
REMARK   3      S21:   1.5887 S22:  -0.3085 S23:  -0.2804                       
REMARK   3      S31:  -1.1496 S32:   0.1692 S33:  -0.2328                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 193 THROUGH 207 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   3.2031  53.6685  42.8979              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9085 T22:   0.7694                                     
REMARK   3      T33:   0.8980 T12:   0.1378                                     
REMARK   3      T13:   0.2429 T23:   0.0279                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5318 L22:   4.0508                                     
REMARK   3      L33:   6.7656 L12:   0.2484                                     
REMARK   3      L13:  -1.0788 L23:  -0.8891                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0275 S12:  -1.1285 S13:  -0.5438                       
REMARK   3      S21:   0.4402 S22:  -0.6642 S23:  -0.1855                       
REMARK   3      S31:   0.6714 S32:  -0.1103 S33:   0.5623                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 208 THROUGH 268 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   2.2244  58.1736  29.2300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7741 T22:   0.5400                                     
REMARK   3      T33:   0.6054 T12:  -0.0452                                     
REMARK   3      T13:   0.1737 T23:  -0.1306                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0972 L22:   3.6536                                     
REMARK   3      L33:   4.5417 L12:   0.8597                                     
REMARK   3      L13:  -1.6892 L23:  -1.8110                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3288 S12:   0.3613 S13:  -0.6642                       
REMARK   3      S21:  -0.3569 S22:  -0.1261 S23:  -0.0701                       
REMARK   3      S31:   0.6193 S32:  -0.1668 S33:   0.4705                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 269 THROUGH 310 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.4502  64.3810  27.1167              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7255 T22:   0.6263                                     
REMARK   3      T33:   0.6794 T12:   0.0629                                     
REMARK   3      T13:   0.0977 T23:  -0.1089                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0863 L22:   2.5374                                     
REMARK   3      L33:   3.4887 L12:   2.7216                                     
REMARK   3      L13:   0.2826 L23:  -0.8831                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2105 S12:   0.1691 S13:   0.0631                       
REMARK   3      S21:  -0.2006 S22:   0.1525 S23:   0.3703                       
REMARK   3      S31:   0.0138 S32:  -0.6368 S33:  -0.0104                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 311 THROUGH 326 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  25.4172  64.8056  26.2664              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9323 T22:   0.7655                                     
REMARK   3      T33:   0.7133 T12:  -0.0839                                     
REMARK   3      T13:   0.2381 T23:  -0.0221                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1017 L22:   4.4038                                     
REMARK   3      L33:   4.7004 L12:   0.8738                                     
REMARK   3      L13:   1.6350 L23:   4.3992                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0525 S12:   1.2269 S13:  -0.0814                       
REMARK   3      S21:  -1.1073 S22:   0.3469 S23:  -1.2509                       
REMARK   3      S31:  -1.0753 S32:   0.6605 S33:  -0.1178                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 327 THROUGH 368 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  21.2631  54.4590  30.1136              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8399 T22:   0.5719                                     
REMARK   3      T33:   0.6148 T12:   0.1141                                     
REMARK   3      T13:   0.2245 T23:   0.0111                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3533 L22:   2.9244                                     
REMARK   3      L33:   3.6065 L12:  -1.2041                                     
REMARK   3      L13:   0.6616 L23:   2.6063                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1661 S12:  -0.2602 S13:  -0.3382                       
REMARK   3      S21:   0.2621 S22:   0.0486 S23:   0.1804                       
REMARK   3      S31:  -0.0298 S32:   0.0843 S33:   0.2584                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 369 THROUGH 387 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  32.2073  60.6406  35.6319              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0244 T22:   0.8268                                     
REMARK   3      T33:   0.6772 T12:   0.1341                                     
REMARK   3      T13:   0.1035 T23:  -0.0241                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8488 L22:   3.3226                                     
REMARK   3      L33:   3.0716 L12:   0.2534                                     
REMARK   3      L13:  -0.4727 L23:   3.1353                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6645 S12:  -0.5521 S13:  -0.1995                       
REMARK   3      S21:   0.5468 S22:   0.6519 S23:  -0.4718                       
REMARK   3      S31:   0.8222 S32:   0.8923 S33:  -0.1328                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 388 THROUGH 432 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  20.6171  47.0677  25.7092              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1164 T22:   0.6656                                     
REMARK   3      T33:   0.8059 T12:   0.1001                                     
REMARK   3      T13:   0.3574 T23:  -0.0688                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8661 L22:   3.6975                                     
REMARK   3      L33:   3.7876 L12:  -1.1164                                     
REMARK   3      L13:   1.5716 L23:   0.2075                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2236 S12:   0.4760 S13:  -0.7319                       
REMARK   3      S21:  -0.1988 S22:  -0.0137 S23:  -0.0243                       
REMARK   3      S31:   0.8982 S32:   0.5488 S33:   0.1166                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 233 THROUGH 239 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.3740  48.2877  23.0602              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3343 T22:   0.9717                                     
REMARK   3      T33:   1.0995 T12:  -0.2298                                     
REMARK   3      T13:   0.1515 T23:  -0.1518                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8038 L22:   3.1366                                     
REMARK   3      L33:   0.2089 L12:   3.4368                                     
REMARK   3      L13:   0.5664 L23:   0.5195                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4310 S12:  -0.2068 S13:  -0.5236                       
REMARK   3      S21:  -0.2912 S22:   0.3796 S23:   0.9413                       
REMARK   3      S31:  -0.3118 S32:   0.2926 S33:   0.3426                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 45 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -20.1157  64.6110  49.4661              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8883 T22:   0.9036                                     
REMARK   3      T33:   0.8867 T12:  -0.0896                                     
REMARK   3      T13:   0.1923 T23:  -0.1246                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1228 L22:   3.9224                                     
REMARK   3      L33:   7.0029 L12:   0.9417                                     
REMARK   3      L13:   1.1591 L23:   5.2090                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0763 S12:  -0.0623 S13:  -0.0401                       
REMARK   3      S21:  -0.1002 S22:  -0.5824 S23:   0.8325                       
REMARK   3      S31:  -0.0026 S32:  -1.1044 S33:   0.4358                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 46 THROUGH 158 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -10.8443  57.5845  62.8389              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6570 T22:   0.6460                                     
REMARK   3      T33:   0.8095 T12:  -0.0634                                     
REMARK   3      T13:   0.2634 T23:  -0.0202                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3300 L22:   2.6886                                     
REMARK   3      L33:   3.4842 L12:  -0.1234                                     
REMARK   3      L13:   0.0769 L23:  -0.3161                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2045 S12:  -0.0519 S13:  -0.5435                       
REMARK   3      S21:  -0.4032 S22:   0.0677 S23:  -0.0233                       
REMARK   3      S31:   0.5407 S32:  -0.1335 S33:   0.1184                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 159 THROUGH 296 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -12.5976  52.2112  82.2488              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6440 T22:   0.8212                                     
REMARK   3      T33:   0.7885 T12:  -0.1106                                     
REMARK   3      T13:   0.1234 T23:   0.2347                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2979 L22:   2.3167                                     
REMARK   3      L33:   5.7895 L12:   0.5058                                     
REMARK   3      L13:  -0.9231 L23:   1.4382                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2080 S12:  -0.5267 S13:  -0.4774                       
REMARK   3      S21:   0.2803 S22:  -0.2670 S23:  -0.1686                       
REMARK   3      S31:   0.5271 S32:  -0.5690 S33:   0.1011                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 177 THROUGH 192 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   7.2844  68.2820  68.0960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8879 T22:   0.8731                                     
REMARK   3      T33:   0.9906 T12:  -0.0394                                     
REMARK   3      T13:   0.1997 T23:   0.0159                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6136 L22:   2.0272                                     
REMARK   3      L33:   4.5654 L12:  -3.0131                                     
REMARK   3      L13:   5.0414 L23:  -2.7534                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0589 S12:  -0.1172 S13:  -0.6002                       
REMARK   3      S21:  -0.0392 S22:  -0.5607 S23:  -0.5368                       
REMARK   3      S31:   1.2282 S32:  -0.2278 S33:   0.1300                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 193 THROUGH 268 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.0272  89.3807  62.0144              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5133 T22:   0.4845                                     
REMARK   3      T33:   0.5169 T12:   0.0011                                     
REMARK   3      T13:   0.0745 T23:  -0.0545                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8047 L22:   6.1557                                     
REMARK   3      L33:   6.0835 L12:   1.8904                                     
REMARK   3      L13:   0.2357 L23:  -1.9496                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0821 S12:  -0.1281 S13:  -0.0163                       
REMARK   3      S21:  -0.0175 S22:  -0.1430 S23:  -0.1946                       
REMARK   3      S31:  -0.3010 S32:   0.1388 S33:   0.2793                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 269 THROUGH 287 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -17.5402  89.0670  65.2973              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8705 T22:   0.9987                                     
REMARK   3      T33:   0.8678 T12:   0.0800                                     
REMARK   3      T13:   0.1981 T23:  -0.1125                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5052 L22:   8.5847                                     
REMARK   3      L33:   5.0682 L12:  -0.2325                                     
REMARK   3      L13:   0.1385 L23:  -6.6263                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4370 S12:  -0.2128 S13:  -0.3508                       
REMARK   3      S21:   1.0357 S22:   0.4262 S23:   0.4409                       
REMARK   3      S31:  -0.8607 S32:  -1.1059 S33:   0.1149                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 288 THROUGH 310 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.2881  81.6951  55.6616              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5728 T22:   0.5649                                     
REMARK   3      T33:   0.5639 T12:  -0.0703                                     
REMARK   3      T13:   0.1007 T23:  -0.0597                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3075 L22:   6.9227                                     
REMARK   3      L33:   8.1305 L12:  -3.4082                                     
REMARK   3      L13:   2.8811 L23:  -3.2430                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0956 S12:   0.6308 S13:  -0.4641                       
REMARK   3      S21:  -0.8205 S22:  -0.1857 S23:   0.2955                       
REMARK   3      S31:   0.2638 S32:   0.2521 S33:   0.1758                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 311 THROUGH 326 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   6.5994  75.8234  80.4922              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8626 T22:   0.8963                                     
REMARK   3      T33:   0.7864 T12:   0.0074                                     
REMARK   3      T13:   0.1308 T23:   0.1487                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5143 L22:   4.2423                                     
REMARK   3      L33:   5.7684 L12:  -2.4161                                     
REMARK   3      L13:  -4.6901 L23:   4.4795                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4397 S12:  -1.3451 S13:  -0.2741                       
REMARK   3      S21:   0.7567 S22:  -0.3643 S23:  -0.6740                       
REMARK   3      S31:   1.5264 S32:   0.6083 S33:   0.6843                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 327 THROUGH 432 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  10.5163  87.7118  78.2572              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5059 T22:   0.5997                                     
REMARK   3      T33:   0.6538 T12:  -0.0060                                     
REMARK   3      T13:   0.0436 T23:   0.0545                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7504 L22:   5.6216                                     
REMARK   3      L33:   4.6348 L12:  -1.4161                                     
REMARK   3      L13:   0.9749 L23:   1.1702                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3011 S12:  -0.2839 S13:  -0.2220                       
REMARK   3      S21:   0.1832 S22:   0.1394 S23:  -0.7280                       
REMARK   3      S31:   0.0429 S32:   0.4993 S33:   0.1802                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 236 THROUGH 239 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.2977 102.1525  61.7478              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8633 T22:   1.5763                                     
REMARK   3      T33:   1.4758 T12:  -0.0268                                     
REMARK   3      T13:  -0.1470 T23:  -0.1471                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2500 L22:   6.3502                                     
REMARK   3      L33:   9.0892 L12:   2.8154                                     
REMARK   3      L13:  -3.3699 L23:  -7.5971                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2206 S12:   0.1382 S13:   1.6907                       
REMARK   3      S21:  -0.0153 S22:  -1.2929 S23:   1.5677                       
REMARK   3      S31:  -1.1707 S32:  -0.9896 S33:   1.3286                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6P3W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAY-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000241833.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-MAY-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9774                             
REMARK 200  MONOCHROMATOR                  : NULL                               
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   : 72513                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.540                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.070                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 8.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.14380                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.8400                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.54                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 2.34900                            
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: 1F                                                   
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.49 M SODIUM PHOSPHATE MONOBASIC        
REMARK 280  MONOHYDRATE AND 0.91 M POTASSIUM PHOSPHATE DIBASIC, VAPOR           
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277.15K                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+2/3                                            
REMARK 290       6555   X-Y,X,Z+1/3                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+2/3                                            
REMARK 290      11555   -X+Y,Y,-Z                                               
REMARK 290      12555   X,X-Y,-Z+1/3                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      143.13800            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       71.56900            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      143.13800            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       71.56900            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      143.13800            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       71.56900            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      143.13800            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       71.56900            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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 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     ARG C   297                                                      
REMARK 465     LEU C   298                                                      
REMARK 465     PRO D   176                                                      
REMARK 465     ALA F   233                                                      
REMARK 465     ARG F   234                                                      
REMARK 465     LYS F   235                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A   2    CG   CD   OE1  OE2                                  
REMARK 470     LYS A   9    CD   CE   NZ                                        
REMARK 470     THR A  14    OG1  CG2                                            
REMARK 470     TYR A  15    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     VAL A  17    CG1  CG2                                            
REMARK 470     LYS A  34    CG   CD   CE   NZ                                   
REMARK 470     ILE A  35    CD1                                                 
REMARK 470     ARG A  36    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  40    CG   CD   OE1  OE2                                  
REMARK 470     ASN A  74    CG   OD1  ND2                                       
REMARK 470     LYS A  89    CD   CE   NZ                                        
REMARK 470     LYS A 250    CD   CE   NZ                                        
REMARK 470     GLU A 257    CD   OE1  OE2                                       
REMARK 470     LEU A 298    CG   CD1  CD2                                       
REMARK 470     LYS B 196    CD   CE   NZ                                        
REMARK 470     LYS B 201    CD   CE   NZ                                        
REMARK 470     LYS B 202    CE   NZ                                             
REMARK 470     LYS B 226    CE   NZ                                             
REMARK 470     GLN B 323    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 328    CG   CD   CE   NZ                                   
REMARK 470     ARG B 378    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 432    O                                                   
REMARK 470     GLU C   2    CG   CD   OE1  OE2                                  
REMARK 470     LYS C   6    CG   CD   CE   NZ                                   
REMARK 470     THR C  14    CB   OG1  CG2                                       
REMARK 470     TYR C  15    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP C  38    CG   OD1  OD2                                       
REMARK 470     GLU C  40    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS C  65    CG   CD   CE   NZ                                   
REMARK 470     GLU C  73    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  75    CG   CD   CE   NZ                                   
REMARK 470     LYS C  89    CG   CD   CE   NZ                                   
REMARK 470     LEU C  96    CG   CD1  CD2                                       
REMARK 470     GLN C 131    CG   CD   OE1  NE2                                  
REMARK 470     ARG C 157    CZ   NH1  NH2                                       
REMARK 470     TYR C 159    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS C 178    CD   CE   NZ                                        
REMARK 470     LYS C 237    CE   NZ                                             
REMARK 470     LYS C 250    CG   CD   CE   NZ                                   
REMARK 470     GLU C 257    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 273    CG   CD   CE   NZ                                   
REMARK 470     LYS C 278    CE   NZ                                             
REMARK 470     HIS C 295    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU C 296    CG   CD1  CD2                                       
REMARK 470     ASP D 177    CG   OD1  OD2                                       
REMARK 470     GLU D 180    CD   OE1  OE2                                       
REMARK 470     LYS D 194    CG   CD   CE   NZ                                   
REMARK 470     LYS D 196    CD   CE   NZ                                        
REMARK 470     GLN D 323    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 388    CD   CE   NZ                                        
REMARK 470     LEU D 432    O                                                   
REMARK 470     ARG F 236    NE   CZ   NH1  NH2                                  
REMARK 470     GLU F 238    CG   CD   OE1  OE2                                  
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A  169   CZ                                                  
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    THR A  41       49.82     33.11                                   
REMARK 500    ASP A 127       39.96   -144.16                                   
REMARK 500    ASP A 145       76.90     55.88                                   
REMARK 500    GLN B 322       75.72   -110.89                                   
REMARK 500    TRP B 372      103.70    -43.35                                   
REMARK 500    ASN B 431       73.30     53.11                                   
REMARK 500    GLU C  42      -51.26   -135.66                                   
REMARK 500    LEU C  58       74.94   -110.38                                   
REMARK 500    ASP C 145       71.13     58.19                                   
REMARK 500    PHE C 286       31.52    -94.68                                   
REMARK 500    TRP D 372      108.65    -43.97                                   
REMARK 500    HIS D 419       18.43     58.80                                   
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 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 504                 
DBREF  6P3W A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  6P3W B  176   432  UNP    P20248   CCNA2_HUMAN    176    432             
DBREF  6P3W E  233   239  PDB    6P3W     6P3W           233    239             
DBREF  6P3W C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  6P3W D  176   432  UNP    P20248   CCNA2_HUMAN    176    432             
DBREF  6P3W F  233   239  PDB    6P3W     6P3W           233    239             
SEQRES   1 A  298  MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY          
SEQRES   2 A  298  THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR          
SEQRES   3 A  298  GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR          
SEQRES   4 A  298  GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 A  298  SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS          
SEQRES   6 A  298  LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU          
SEQRES   7 A  298  VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET          
SEQRES   8 A  298  ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE          
SEQRES   9 A  298  LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE          
SEQRES  10 A  298  CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  11 A  298  GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU          
SEQRES  12 A  298  ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL          
SEQRES  13 A  298  ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP TYR ARG          
SEQRES  14 A  298  ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR          
SEQRES  15 A  298  ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU          
SEQRES  16 A  298  MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU          
SEQRES  17 A  298  ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR          
SEQRES  18 A  298  PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO          
SEQRES  19 A  298  ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP          
SEQRES  20 A  298  PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG          
SEQRES  21 A  298  SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS          
SEQRES  22 A  298  ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE          
SEQRES  23 A  298  GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU              
SEQRES   1 B  257  PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU ARG GLU          
SEQRES   2 B  257  MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET LYS          
SEQRES   3 B  257  LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE LEU          
SEQRES   4 B  257  VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS LEU          
SEQRES   5 B  257  GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE ASP          
SEQRES   6 B  257  ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS LEU          
SEQRES   7 B  257  GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER LYS          
SEQRES   8 B  257  PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE VAL          
SEQRES   9 B  257  TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN VAL LEU          
SEQRES  10 B  257  ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR PHE ASP          
SEQRES  11 B  257  LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN TYR          
SEQRES  12 B  257  PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL GLU SER          
SEQRES  13 B  257  LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP ALA          
SEQRES  14 B  257  ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE ALA GLY          
SEQRES  15 B  257  ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY GLN          
SEQRES  16 B  257  SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY TYR THR          
SEQRES  17 B  257  LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU HIS GLN          
SEQRES  18 B  257  THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER ILE          
SEQRES  19 B  257  ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY VAL SER          
SEQRES  20 B  257  LEU LEU ASN PRO PRO GLU THR LEU ASN LEU                      
SEQRES   1 E    7  ALA ARG LYS ARG LEU GLU LEU                                  
SEQRES   1 C  298  MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY          
SEQRES   2 C  298  THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR          
SEQRES   3 C  298  GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR          
SEQRES   4 C  298  GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 C  298  SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS          
SEQRES   6 C  298  LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU          
SEQRES   7 C  298  VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET          
SEQRES   8 C  298  ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE          
SEQRES   9 C  298  LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE          
SEQRES  10 C  298  CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  11 C  298  GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU          
SEQRES  12 C  298  ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL          
SEQRES  13 C  298  ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP TYR ARG          
SEQRES  14 C  298  ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR          
SEQRES  15 C  298  ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU          
SEQRES  16 C  298  MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU          
SEQRES  17 C  298  ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR          
SEQRES  18 C  298  PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO          
SEQRES  19 C  298  ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP          
SEQRES  20 C  298  PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG          
SEQRES  21 C  298  SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS          
SEQRES  22 C  298  ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE          
SEQRES  23 C  298  GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU              
SEQRES   1 D  257  PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU ARG GLU          
SEQRES   2 D  257  MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET LYS          
SEQRES   3 D  257  LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE LEU          
SEQRES   4 D  257  VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS LEU          
SEQRES   5 D  257  GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE ASP          
SEQRES   6 D  257  ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS LEU          
SEQRES   7 D  257  GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER LYS          
SEQRES   8 D  257  PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE VAL          
SEQRES   9 D  257  TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN VAL LEU          
SEQRES  10 D  257  ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR PHE ASP          
SEQRES  11 D  257  LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN TYR          
SEQRES  12 D  257  PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL GLU SER          
SEQRES  13 D  257  LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP ALA          
SEQRES  14 D  257  ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE ALA GLY          
SEQRES  15 D  257  ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY GLN          
SEQRES  16 D  257  SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY TYR THR          
SEQRES  17 D  257  LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU HIS GLN          
SEQRES  18 D  257  THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER ILE          
SEQRES  19 D  257  ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY VAL SER          
SEQRES  20 D  257  LEU LEU ASN PRO PRO GLU THR LEU ASN LEU                      
SEQRES   1 F    7  ALA ARG LYS ARG LEU GLU LEU                                  
HET    PO4  A 301       5                                                       
HET    PO4  A 302       5                                                       
HET    PO4  A 303       5                                                       
HET    PO4  B 501       5                                                       
HET    PO4  C 301       5                                                       
HET    PO4  C 302       5                                                       
HET    PO4  C 303       5                                                       
HET    PO4  C 304       5                                                       
HET    PO4  D 501       5                                                       
HET    PO4  D 502       5                                                       
HET    PO4  D 503       5                                                       
HET    PO4  D 504       5                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   7  PO4    12(O4 P 3-)                                                  
FORMUL  19  HOH   *50(H2 O)                                                     
HELIX    1 AA1 PRO A   45  LYS A   56  1                                  12    
HELIX    2 AA2 LEU A   87  SER A   94  1                                   8    
HELIX    3 AA3 PRO A  100  HIS A  121  1                                  22    
HELIX    4 AA4 LYS A  129  GLN A  131  5                                   3    
HELIX    5 AA5 THR A  165  ARG A  169  5                                   5    
HELIX    6 AA6 ALA A  170  LEU A  175  1                                   6    
HELIX    7 AA7 THR A  182  ARG A  199  1                                  18    
HELIX    8 AA8 SER A  207  GLY A  220  1                                  14    
HELIX    9 AA9 GLY A  229  MET A  233  5                                   5    
HELIX   10 AB1 ASP A  247  VAL A  252  1                                   6    
HELIX   11 AB2 ASP A  256  LEU A  267  1                                  12    
HELIX   12 AB3 ASP A  270  ARG A  274  5                                   5    
HELIX   13 AB4 SER A  276  ALA A  282  1                                   7    
HELIX   14 AB5 HIS A  283  GLN A  287  5                                   5    
HELIX   15 AB6 ASP B  177  CYS B  193  1                                  17    
HELIX   16 AB7 GLY B  198  GLN B  203  5                                   6    
HELIX   17 AB8 THR B  207  TYR B  225  1                                  19    
HELIX   18 AB9 GLN B  228  MET B  246  1                                  19    
HELIX   19 AC1 LEU B  249  GLU B  269  1                                  21    
HELIX   20 AC2 GLU B  274  THR B  282  1                                   9    
HELIX   21 AC3 THR B  287  LEU B  302  1                                  16    
HELIX   22 AC4 THR B  310  LEU B  320  1                                  11    
HELIX   23 AC5 ASN B  326  ASP B  343  1                                  18    
HELIX   24 AC6 ASP B  343  LEU B  348  1                                   6    
HELIX   25 AC7 LEU B  351  GLY B  369  1                                  19    
HELIX   26 AC8 PRO B  373  GLY B  381  1                                   9    
HELIX   27 AC9 LEU B  387  LYS B  400  1                                  14    
HELIX   28 AD1 ALA B  401  HIS B  404  5                                   4    
HELIX   29 AD2 GLN B  407  TYR B  413  1                                   7    
HELIX   30 AD3 LYS B  414  HIS B  419  5                                   6    
HELIX   31 AD4 GLY B  420  LEU B  424  5                                   5    
HELIX   32 AD5 PRO C   45  LYS C   56  1                                  12    
HELIX   33 AD6 LEU C   87  SER C   94  1                                   8    
HELIX   34 AD7 PRO C  100  HIS C  121  1                                  22    
HELIX   35 AD8 THR C  165  ARG C  169  5                                   5    
HELIX   36 AD9 ALA C  170  LEU C  175  1                                   6    
HELIX   37 AE1 SER C  181  ARG C  199  1                                  19    
HELIX   38 AE2 SER C  207  GLY C  220  1                                  14    
HELIX   39 AE3 GLY C  229  MET C  233  5                                   5    
HELIX   40 AE4 ASP C  247  VAL C  252  1                                   6    
HELIX   41 AE5 ASP C  256  LEU C  267  1                                  12    
HELIX   42 AE6 SER C  276  ALA C  282  1                                   7    
HELIX   43 AE7 HIS C  283  VAL C  289  5                                   7    
HELIX   44 AE8 TYR D  178  CYS D  193  1                                  16    
HELIX   45 AE9 GLY D  198  GLN D  203  5                                   6    
HELIX   46 AF1 THR D  207  TYR D  225  1                                  19    
HELIX   47 AF2 GLN D  228  LEU D  243  1                                  16    
HELIX   48 AF3 LEU D  249  GLY D  251  5                                   3    
HELIX   49 AF4 LYS D  252  GLU D  269  1                                  18    
HELIX   50 AF5 GLU D  274  THR D  282  1                                   9    
HELIX   51 AF6 THR D  287  THR D  303  1                                  17    
HELIX   52 AF7 THR D  310  PHE D  319  1                                  10    
HELIX   53 AF8 LEU D  320  GLN D  322  5                                   3    
HELIX   54 AF9 ASN D  326  SER D  340  1                                  15    
HELIX   55 AG1 ASP D  343  LEU D  348  1                                   6    
HELIX   56 AG2 LEU D  351  THR D  368  1                                  18    
HELIX   57 AG3 PRO D  373  GLY D  381  1                                   9    
HELIX   58 AG4 LEU D  387  ALA D  401  1                                  15    
HELIX   59 AG5 PRO D  402  HIS D  404  5                                   3    
HELIX   60 AG6 GLN D  407  TYR D  413  1                                   7    
HELIX   61 AG7 LYS D  414  HIS D  419  5                                   6    
HELIX   62 AG8 GLY D  420  LEU D  424  5                                   5    
SHEET    1 AA1 5 PHE A   4  GLU A  12  0                                        
SHEET    2 AA1 5 VAL A  17  ASN A  23 -1  O  LYS A  20   N  VAL A   7           
SHEET    3 AA1 5 VAL A  29  ARG A  36 -1  O  LEU A  32   N  TYR A  19           
SHEET    4 AA1 5 LYS A  75  GLU A  81 -1  O  PHE A  80   N  ALA A  31           
SHEET    5 AA1 5 LEU A  66  HIS A  71 -1  N  ASP A  68   O  VAL A  79           
SHEET    1 AA2 3 GLN A  85  ASP A  86  0                                        
SHEET    2 AA2 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3 AA2 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1 AA3 2 VAL A 123  LEU A 124  0                                        
SHEET    2 AA3 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SHEET    1 AA4 5 PHE C   4  GLU C  12  0                                        
SHEET    2 AA4 5 VAL C  17  ASN C  23 -1  O  LYS C  20   N  GLU C   8           
SHEET    3 AA4 5 VAL C  29  ARG C  36 -1  O  LEU C  32   N  TYR C  19           
SHEET    4 AA4 5 LYS C  75  GLU C  81 -1  O  PHE C  80   N  ALA C  31           
SHEET    5 AA4 5 LEU C  66  HIS C  71 -1  N  LEU C  67   O  VAL C  79           
SHEET    1 AA5 3 GLN C  85  ASP C  86  0                                        
SHEET    2 AA5 3 LEU C 133  ILE C 135 -1  O  ILE C 135   N  GLN C  85           
SHEET    3 AA5 3 ILE C 141  LEU C 143 -1  O  LYS C 142   N  LEU C 134           
SHEET    1 AA6 2 VAL C 123  LEU C 124  0                                        
SHEET    2 AA6 2 ARG C 150  ALA C 151 -1  O  ARG C 150   N  LEU C 124           
CISPEP   1 ASP D  345    PRO D  346          0         6.00                     
SITE     1 AC1  2 ARG A 157  LYS A 178                                          
SITE     1 AC2  3 LYS A 129  GLN A 131  THR A 165                               
SITE     1 AC3  2 GLN A   5  ARG A  22                                          
SITE     1 AC4  3 ARG B 187  LYS B 379  THR B 380                               
SITE     1 AC5  2 ARG B 293  LYS C  24                                          
SITE     1 AC6  4 LYS C  33  PHE C  80  ALA C 144  ASP C 145                    
SITE     1 AC7  8 LEU C  37  GLY C  43  VAL C  44  HIS C  71                    
SITE     2 AC7  8 GLU C  73  LEU D 292  GLU D 295  HIS D 296                    
SITE     1 AC8  1 ARG C 260                                                     
SITE     1 AC9  4 MET A   1  HIS C  71  HIS D 296  LYS D 300                    
SITE     1 AD1  2 LYS A  24  ARG D 293                                          
SITE     1 AD2  3 ASN C 272  TYR D 178  HIS D 179                               
SITE     1 AD3  1 LYS D 252                                                     
CRYST1  186.396  186.396  214.707  90.00  90.00 120.00 P 62 2 2     24          
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      0.005365  0.003097  0.000000        0.00000                         
SCALE2      0.000000  0.006195  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004658        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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