GenomeNet

Database: PDB
Entry: 3QHR
LinkDB: 3QHR
Original site: 3QHR 
HEADER    TRANSFERASE/PROTEIN BINDING             26-JAN-11   3QHR              
TITLE     STRUCTURE OF A PCDK2/CYCLINA TRANSITION-STATE MIMIC                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION PROTEIN KINASE 2;                            
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: 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 FRAGMENT: UNP RESIDUES 163-422;                                      
COMPND  11 SYNONYM: CYCLIN-A;                                                   
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: CDK2 SUBSTRATE PEPTIDE: PKTPKKAKKL;                        
COMPND  15 CHAIN: J, K, L, M;                                                   
COMPND  16 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;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  12 ORGANISM_COMMON: MOUSE;                                              
SOURCE  13 ORGANISM_TAXID: 10090;                                               
SOURCE  14 GENE: CCNA2, CCNA, CYCA;                                             
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET28A;                                   
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 SYNTHETIC: YES;                                                      
SOURCE  21 OTHER_DETAILS: OPTIMAL SUBSTRATE SEQUENCE                            
KEYWDS    KINASE CATALYTIC DOMAIN, PROTEIN KINASE, CYCLIN, PHOSPHORYLATED THR-  
KEYWDS   2 160, TRANSFERASE-PROTEIN BINDING COMPLEX                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.YOUNG,D.M.JACOBSEN,Z.Q.BAO                                        
REVDAT   1   25-MAY-11 3QHR    0                                                
JRNL        AUTH   Z.Q.BAO,D.M.JACOBSEN,M.A.YOUNG                               
JRNL        TITL   BRIEFLY BOUND TO ACTIVATE: TRANSIENT BINDING OF A SECOND     
JRNL        TITL 2 CATALYTIC MAGNESIUM ACTIVATES THE STRUCTURE AND DYNAMICS OF  
JRNL        TITL 3 CDK2 KINASE FOR CATALYSIS.                                   
JRNL        REF    STRUCTURE                     V.  19   675 2011              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   21565702                                                     
JRNL        DOI    10.1016/J.STR.2011.02.016                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.17 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.1_743)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.17                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.80                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 83847                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.210                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4192                            
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 37.8104 -  6.7305    0.99     2686   146  0.1869 0.2052        
REMARK   3     2  6.7305 -  5.3470    1.00     2681   142  0.1995 0.2040        
REMARK   3     3  5.3470 -  4.6725    1.00     2669   138  0.1413 0.1553        
REMARK   3     4  4.6725 -  4.2459    1.00     2667   142  0.1377 0.1759        
REMARK   3     5  4.2459 -  3.9419    1.00     2645   143  0.1406 0.1748        
REMARK   3     6  3.9419 -  3.7097    1.00     2670   128  0.1425 0.1739        
REMARK   3     7  3.7097 -  3.5241    1.00     2667   135  0.1429 0.1737        
REMARK   3     8  3.5241 -  3.3708    1.00     2643   156  0.1475 0.1673        
REMARK   3     9  3.3708 -  3.2411    1.00     2652   150  0.1476 0.1854        
REMARK   3    10  3.2411 -  3.1293    1.00     2650   143  0.1595 0.1824        
REMARK   3    11  3.1293 -  3.0315    1.00     2650   144  0.1640 0.1897        
REMARK   3    12  3.0315 -  2.9449    1.00     2602   154  0.1618 0.1922        
REMARK   3    13  2.9449 -  2.8674    1.00     2696   156  0.1651 0.2296        
REMARK   3    14  2.8674 -  2.7974    1.00     2651   135  0.1745 0.2363        
REMARK   3    15  2.7974 -  2.7339    1.00     2649   129  0.1754 0.2189        
REMARK   3    16  2.7339 -  2.6757    1.00     2656   133  0.1930 0.2655        
REMARK   3    17  2.6757 -  2.6222    1.00     2630   142  0.2060 0.2467        
REMARK   3    18  2.6222 -  2.5727    1.00     2648   162  0.2089 0.2390        
REMARK   3    19  2.5727 -  2.5268    1.00     2597   140  0.2101 0.2717        
REMARK   3    20  2.5268 -  2.4840    1.00     2754   108  0.2186 0.2664        
REMARK   3    21  2.4840 -  2.4439    1.00     2605   131  0.2312 0.2724        
REMARK   3    22  2.4439 -  2.4063    1.00     2666   161  0.2358 0.2882        
REMARK   3    23  2.4063 -  2.3709    1.00     2608   128  0.2443 0.3106        
REMARK   3    24  2.3709 -  2.3375    1.00     2698   130  0.2567 0.2932        
REMARK   3    25  2.3375 -  2.3060    1.00     2587   151  0.2756 0.3163        
REMARK   3    26  2.3060 -  2.2760    1.00     2671   132  0.2833 0.2898        
REMARK   3    27  2.2760 -  2.2476    1.00     2696   136  0.2986 0.3061        
REMARK   3    28  2.2476 -  2.2205    1.00     2615   132  0.3107 0.3559        
REMARK   3    29  2.2205 -  2.1947    1.00     2679   125  0.3094 0.3467        
REMARK   3    30  2.1947 -  2.1700    1.00     2667   140  0.3257 0.3227        
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              : 0.37                                          
REMARK   3   B_SOL              : 57.53                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.700            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.850           
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) : 6.75170                                              
REMARK   3    B22 (A**2) : -4.31770                                             
REMARK   3    B33 (A**2) : -2.43400                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 8.23840                                              
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      :  0.011           9685                                  
REMARK   3   ANGLE     :  1.216          13115                                  
REMARK   3   CHIRALITY :  0.082           1474                                  
REMARK   3   PLANARITY :  0.006           1624                                  
REMARK   3   DIHEDRAL  : 14.853           3644                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 24                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 1:27)                               
REMARK   3    ORIGIN FOR THE GROUP (A):   6.1957 -32.9255 -34.0419              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7689 T22:   0.2894                                     
REMARK   3      T33:   0.4721 T12:  -0.0612                                     
REMARK   3      T13:  -0.1958 T23:   0.0394                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6697 L22:   6.7122                                     
REMARK   3      L33:   3.5958 L12:   0.1862                                     
REMARK   3      L13:  -1.4756 L23:  -2.6934                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5106 S12:   0.0323 S13:  -0.3350                       
REMARK   3      S21:  -0.1311 S22:  -0.0566 S23:   1.3751                       
REMARK   3      S31:   0.7201 S32:  -0.6706 S33:  -0.4177                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 28:56)                              
REMARK   3    ORIGIN FOR THE GROUP (A):   7.8493 -40.6671 -22.3775              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4843 T22:   0.3132                                     
REMARK   3      T33:   0.2532 T12:  -0.1246                                     
REMARK   3      T13:  -0.0459 T23:  -0.0348                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4833 L22:   9.4802                                     
REMARK   3      L33:   4.8128 L12:   1.8233                                     
REMARK   3      L13:  -1.5467 L23:  -6.5944                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0252 S12:   0.1944 S13:   0.3869                       
REMARK   3      S21:  -0.7839 S22:   0.5946 S23:   0.9129                       
REMARK   3      S31:   0.7189 S32:  -0.8938 S33:  -0.5199                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 57:99)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  15.9258 -39.7945 -33.1791              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5481 T22:   0.1418                                     
REMARK   3      T33:   0.1103 T12:  -0.0068                                     
REMARK   3      T13:  -0.0112 T23:   0.0176                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0041 L22:   3.5538                                     
REMARK   3      L33:   5.8456 L12:  -1.5368                                     
REMARK   3      L13:  -1.6558 L23:   0.7857                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1788 S12:   0.3903 S13:   0.0882                       
REMARK   3      S21:  -0.6512 S22:  -0.0826 S23:   0.1025                       
REMARK   3      S31:  -0.5040 S32:  -0.4652 S33:  -0.0072                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 100:160)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  24.0409 -48.0296 -28.9107              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3022 T22:   0.1011                                     
REMARK   3      T33:   0.1284 T12:  -0.0217                                     
REMARK   3      T13:   0.0237 T23:  -0.0398                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4680 L22:   3.8933                                     
REMARK   3      L33:   4.2906 L12:   0.0501                                     
REMARK   3      L13:  -0.7988 L23:   0.7299                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0968 S12:  -0.0266 S13:  -0.0737                       
REMARK   3      S21:  -0.1793 S22:   0.0028 S23:  -0.0122                       
REMARK   3      S31:  -0.1422 S32:   0.1626 S33:  -0.0610                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 161:296)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  26.2405 -63.0687 -33.3470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3562 T22:   0.1904                                     
REMARK   3      T33:   0.1796 T12:   0.0350                                     
REMARK   3      T13:   0.0404 T23:  -0.0644                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1305 L22:   5.6147                                     
REMARK   3      L33:   2.7130 L12:   1.5714                                     
REMARK   3      L13:  -0.0281 L23:   0.2652                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0251 S12:   0.0810 S13:  -0.1742                       
REMARK   3      S21:  -0.2703 S22:   0.0614 S23:  -0.0700                       
REMARK   3      S31:   0.1754 S32:   0.1734 S33:  -0.0442                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 175:193)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  31.8136 -44.4490 -12.2184              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3438 T22:   0.3423                                     
REMARK   3      T33:   0.3165 T12:  -0.0185                                     
REMARK   3      T13:   0.0887 T23:  -0.0904                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8284 L22:   4.0527                                     
REMARK   3      L33:   3.5852 L12:  -0.2799                                     
REMARK   3      L13:  -0.0617 L23:   3.7975                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0564 S12:   1.0242 S13:  -0.7515                       
REMARK   3      S21:  -0.8607 S22:  -0.4614 S23:  -0.1767                       
REMARK   3      S31:  -0.2868 S32:   0.1719 S33:   0.2982                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 194:236)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  13.0929 -42.3013   3.6488              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2799 T22:   0.2389                                     
REMARK   3      T33:   0.1720 T12:   0.0871                                     
REMARK   3      T13:   0.0175 T23:   0.0411                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6641 L22:   3.9450                                     
REMARK   3      L33:   6.1083 L12:  -1.7253                                     
REMARK   3      L13:  -1.3258 L23:   4.8732                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2310 S12:  -0.3715 S13:   0.0280                       
REMARK   3      S21:   0.5215 S22:   0.2930 S23:   0.1371                       
REMARK   3      S31:   0.0707 S32:   0.3756 S33:  -0.1073                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 237:308)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   6.1739 -40.9062  -4.9559              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1837 T22:   0.1310                                     
REMARK   3      T33:   0.1893 T12:   0.0082                                     
REMARK   3      T13:  -0.0189 T23:   0.0403                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1452 L22:   5.0960                                     
REMARK   3      L33:   4.5879 L12:  -0.3260                                     
REMARK   3      L13:  -1.8110 L23:   1.5716                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1223 S12:   0.1171 S13:   0.0060                       
REMARK   3      S21:   0.0553 S22:   0.1005 S23:   0.3777                       
REMARK   3      S31:   0.0076 S32:  -0.1112 S33:   0.0155                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 309:399)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  31.4271 -50.0314   4.2507              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1652 T22:   0.2779                                     
REMARK   3      T33:   0.1972 T12:   0.1094                                     
REMARK   3      T13:  -0.0232 T23:   0.0032                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4507 L22:   3.6882                                     
REMARK   3      L33:   3.5972 L12:   0.5790                                     
REMARK   3      L13:  -0.2758 L23:  -1.2063                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2923 S12:  -0.5733 S13:  -0.2201                       
REMARK   3      S21:   0.1884 S22:   0.2253 S23:  -0.4077                       
REMARK   3      S31:   0.1714 S32:   0.3259 S33:   0.0360                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 400:432)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  21.7838 -56.1725  12.9177              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4458 T22:   0.5584                                     
REMARK   3      T33:   0.1474 T12:   0.2132                                     
REMARK   3      T13:   0.1482 T23:   0.2018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3975 L22:   3.1575                                     
REMARK   3      L33:   6.4980 L12:  -2.1071                                     
REMARK   3      L13:  -0.4661 L23:   0.2113                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5168 S12:  -1.2763 S13:  -1.3968                       
REMARK   3      S21:   0.4539 S22:   0.4692 S23:   0.1699                       
REMARK   3      S31:   0.3263 S32:   0.6399 S33:   0.0752                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 1:27)                               
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.5066 -18.1621  -3.6282              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5169 T22:   0.2994                                     
REMARK   3      T33:   0.7654 T12:   0.1366                                     
REMARK   3      T13:   0.1705 T23:   0.0877                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4902 L22:   2.5743                                     
REMARK   3      L33:   3.3627 L12:  -1.6157                                     
REMARK   3      L13:   1.7309 L23:  -2.8465                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7321 S12:   0.6843 S13:   0.8315                       
REMARK   3      S21:  -0.4813 S22:  -0.3927 S23:   1.0155                       
REMARK   3      S31:  -0.2858 S32:  -0.3560 S33:  -0.3168                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 28:56)                              
REMARK   3    ORIGIN FOR THE GROUP (A):   4.3187 -10.2878 -12.4113              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5319 T22:   0.3523                                     
REMARK   3      T33:   0.2918 T12:   0.1687                                     
REMARK   3      T13:   0.0646 T23:   0.0283                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0260 L22:   8.4248                                     
REMARK   3      L33:   5.0832 L12:   3.8390                                     
REMARK   3      L13:  -3.7205 L23:  -6.3357                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2705 S12:   0.6384 S13:   0.2524                       
REMARK   3      S21:  -0.4384 S22:   0.5269 S23:   0.8880                       
REMARK   3      S31:  -0.0309 S32:  -0.8105 S33:  -0.6820                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 57:99)                              
REMARK   3    ORIGIN FOR THE GROUP (A):   4.8557 -11.1270   1.0979              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3208 T22:   0.1423                                     
REMARK   3      T33:   0.2403 T12:   0.0032                                     
REMARK   3      T13:   0.1239 T23:   0.0609                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0149 L22:   5.6802                                     
REMARK   3      L33:   5.2249 L12:   0.4408                                     
REMARK   3      L13:  -0.2299 L23:   2.9184                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2395 S12:  -0.0631 S13:  -0.0304                       
REMARK   3      S21:   0.4565 S22:  -0.1067 S23:   0.4805                       
REMARK   3      S31:   0.8453 S32:  -0.3163 S33:   0.3892                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 100:160)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  13.7834  -2.6734   2.1114              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3076 T22:   0.1279                                     
REMARK   3      T33:   0.1536 T12:   0.0543                                     
REMARK   3      T13:   0.0506 T23:  -0.0116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2088 L22:   3.5300                                     
REMARK   3      L33:   4.8203 L12:  -0.3766                                     
REMARK   3      L13:  -0.0906 L23:   0.7656                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0073 S12:  -0.0396 S13:   0.1720                       
REMARK   3      S21:   0.0653 S22:  -0.0086 S23:  -0.0063                       
REMARK   3      S31:   0.1989 S32:   0.3230 S33:   0.0254                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 161:296)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  12.7641  12.3488   6.9642              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1999 T22:   0.1986                                     
REMARK   3      T33:   0.1950 T12:  -0.0244                                     
REMARK   3      T13:   0.0464 T23:  -0.0667                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1992 L22:   6.2559                                     
REMARK   3      L33:   3.0322 L12:  -1.8778                                     
REMARK   3      L13:  -0.0637 L23:  -0.9544                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0814 S12:  -0.2494 S13:   0.3976                       
REMARK   3      S21:   0.2020 S22:   0.0321 S23:  -0.0929                       
REMARK   3      S31:   0.0588 S32:   0.2407 S33:  -0.0885                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 175:193)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  29.8478  -5.6146  -7.2512              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4518 T22:   0.5831                                     
REMARK   3      T33:   0.2723 T12:   0.1610                                     
REMARK   3      T13:   0.0717 T23:  -0.0449                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8961 L22:   3.4762                                     
REMARK   3      L33:   3.4490 L12:  -3.6355                                     
REMARK   3      L13:  -3.6546 L23:   3.4689                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2272 S12:  -0.7505 S13:   0.5072                       
REMARK   3      S21:   0.4588 S22:   0.0291 S23:   0.0196                       
REMARK   3      S31:  -0.2981 S32:   0.6192 S33:   0.1036                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 194:254)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  22.1396 -10.4818 -30.7600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4449 T22:   0.2507                                     
REMARK   3      T33:   0.1787 T12:  -0.0161                                     
REMARK   3      T13:   0.0913 T23:  -0.0174                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3608 L22:   7.1093                                     
REMARK   3      L33:   7.4947 L12:   0.8462                                     
REMARK   3      L13:  -1.1941 L23:   3.3949                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2066 S12:   0.1193 S13:  -0.1930                       
REMARK   3      S21:  -0.6579 S22:   0.3370 S23:  -0.3356                       
REMARK   3      S31:   0.1430 S32:   0.5854 S33:  -0.1153                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 255:307)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  10.3688  -7.6406 -26.9053              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3826 T22:   0.1638                                     
REMARK   3      T33:   0.2073 T12:   0.0462                                     
REMARK   3      T13:   0.0324 T23:   0.0036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5529 L22:   3.6305                                     
REMARK   3      L33:   6.7632 L12:  -0.1979                                     
REMARK   3      L13:   1.6102 L23:   0.5962                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1293 S12:  -0.1377 S13:  -0.0581                       
REMARK   3      S21:  -0.3673 S22:   0.0913 S23:   0.2375                       
REMARK   3      S31:  -0.1255 S32:  -0.1749 S33:   0.0295                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 308:401)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  38.4298   0.1944 -21.4655              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4348 T22:   0.6187                                     
REMARK   3      T33:   0.3003 T12:  -0.0716                                     
REMARK   3      T13:   0.1050 T23:  -0.1257                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9501 L22:   3.3516                                     
REMARK   3      L33:   5.8354 L12:   0.1215                                     
REMARK   3      L13:   0.1639 L23:  -1.2089                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3300 S12:   0.0023 S13:   0.0399                       
REMARK   3      S21:  -0.1404 S22:   0.3542 S23:  -0.5241                       
REMARK   3      S31:  -0.4013 S32:   1.3735 S33:  -0.0451                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 402:432)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  34.9900   6.5933 -33.5660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7691 T22:   0.6711                                     
REMARK   3      T33:   0.2527 T12:  -0.3176                                     
REMARK   3      T13:   0.2010 T23:  -0.0196                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5219 L22:   4.0000                                     
REMARK   3      L33:   7.6061 L12:   0.4121                                     
REMARK   3      L13:   0.0335 L23:   3.2088                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7540 S12:   0.5634 S13:   0.5734                       
REMARK   3      S21:  -0.7334 S22:   0.5775 S23:  -0.2653                       
REMARK   3      S31:  -1.0214 S32:   1.2723 S33:  -0.0266                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: (CHAIN J AND RESID -2:7)                               
REMARK   3    ORIGIN FOR THE GROUP (A):   2.1983   7.0700 -12.6573              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3833 T22:   1.0321                                     
REMARK   3      T33:   0.4257 T12:   0.2059                                     
REMARK   3      T13:   0.1684 T23:   0.0333                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0714 L22:   5.3304                                     
REMARK   3      L33:   3.2330 L12:  -0.0638                                     
REMARK   3      L13:   0.8254 L23:   4.0805                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1777 S12:  -0.7423 S13:   0.0105                       
REMARK   3      S21:  -0.1209 S22:  -0.2147 S23:   1.0087                       
REMARK   3      S31:  -1.4460 S32:  -0.6764 S33:   0.1699                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: (CHAIN K AND RESID -2:7)                               
REMARK   3    ORIGIN FOR THE GROUP (A):   6.1787 -57.9457 -22.9832              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0532 T22:   1.1034                                     
REMARK   3      T33:   0.5423 T12:  -0.1664                                     
REMARK   3      T13:   0.2315 T23:   0.0575                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5698 L22:   7.8509                                     
REMARK   3      L33:   2.7103 L12:  -3.2050                                     
REMARK   3      L13:  -1.1926 L23:   4.5093                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4966 S12:   0.5629 S13:  -1.0295                       
REMARK   3      S21:   0.1265 S22:  -0.2163 S23:   0.9236                       
REMARK   3      S31:   0.5066 S32:  -0.7061 S33:   0.4992                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: (CHAIN A AND RESID 297:297)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  11.9794 -43.2213 -33.7946              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0309 T22:   0.3888                                     
REMARK   3      T33:   0.7516 T12:   0.0831                                     
REMARK   3      T13:   0.1561 T23:   0.1792                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9347 L22:   1.6715                                     
REMARK   3      L33:   7.6508 L12:  -2.8416                                     
REMARK   3      L13:   6.1320 L23:  -3.5019                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0266 S12:  -0.0482 S13:   0.4116                       
REMARK   3      S21:   0.9035 S22:  -0.5757 S23:   1.6009                       
REMARK   3      S31:   0.2335 S32:   0.1976 S33:   0.5284                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 297:297)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   1.1935  -7.7185  -0.6903              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0629 T22:   0.5189                                     
REMARK   3      T33:   0.6639 T12:   0.1061                                     
REMARK   3      T13:   0.1782 T23:   0.0618                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1970 L22:   5.0405                                     
REMARK   3      L33:   5.3835 L12:   4.5792                                     
REMARK   3      L13:  -5.0245 L23:  -1.2076                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6969 S12:   0.9057 S13:   0.8578                       
REMARK   3      S21:  -2.5655 S22:  -0.8025 S23:  -0.4560                       
REMARK   3      S31:  -0.6039 S32:  -0.2376 S33:   0.1392                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 4                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq -1:159 or resseq 160:   
REMARK   3                          296 )                                       
REMARK   3     SELECTION          : chain C                                     
REMARK   3     ATOM PAIRS NUMBER  : 2396                                        
REMARK   3     RMSD               : 0.228                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain B and (resseq 172:432 )               
REMARK   3     SELECTION          : chain D                                     
REMARK   3     ATOM PAIRS NUMBER  : 2099                                        
REMARK   3     RMSD               : 0.420                                       
REMARK   3   NCS GROUP : 3                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq 297:297)                
REMARK   3     SELECTION          : chain C                                     
REMARK   3     ATOM PAIRS NUMBER  : 27                                          
REMARK   3     RMSD               : 0.021                                       
REMARK   3   NCS GROUP : 4                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain L and (resseq 5:7 )                   
REMARK   3     SELECTION          : chain M                                     
REMARK   3     ATOM PAIRS NUMBER  : 26                                          
REMARK   3     RMSD               : 0.127                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3QHR COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-FEB-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB063660.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-FEB-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872                            
REMARK 200  MONOCHROMATOR                  : DIAMOND LAUE                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 83902                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.170                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.805                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.13200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.17                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.29                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.01200                            
REMARK 200  R SYM FOR SHELL            (I) : 1.22200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.500                              
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: UNPUBLISHED STRUCTURE                                
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% W/V POLY(ACRYLIC ACID SODIUM SALT)   
REMARK 280  5100, 20MM MGCL2, 100MM HEPES PH 8.0, VAPOR DIFFUSION, SITTING      
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       81.95500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23240 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, L, K                            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9560 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, M, J                            
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 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     PRO L   -2                                                       
REMARK 475     LYS L   -1                                                       
REMARK 475     THR L    0                                                       
REMARK 475     PRO L    1                                                       
REMARK 475     LYS L    2                                                       
REMARK 475     LYS L    3                                                       
REMARK 475     PRO M   -2                                                       
REMARK 475     LYS M   -1                                                       
REMARK 475     THR M    0                                                       
REMARK 475     PRO M    1                                                       
REMARK 475     LYS M    2                                                       
REMARK 475     LYS M    3                                                       
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  39       -1.30     80.84                                   
REMARK 500    THR A  72     -165.55   -117.95                                   
REMARK 500    ASP A 127       40.00   -148.23                                   
REMARK 500    ASP A 145       75.32     55.27                                   
REMARK 500    VAL A 164      129.74     85.76                                   
REMARK 500    SER A 181     -152.78   -152.13                                   
REMARK 500    ALA B 307       59.11    -90.98                                   
REMARK 500    LYS B 417      -39.53    -39.63                                   
REMARK 500    THR C  39        5.90     81.06                                   
REMARK 500    THR C  72     -166.16   -118.07                                   
REMARK 500    ASP C 127       41.33   -149.88                                   
REMARK 500    ASP C 145       72.74     53.96                                   
REMARK 500    VAL C 164      137.24     81.05                                   
REMARK 500    SER C 181     -153.58   -127.70                                   
REMARK 500    VAL D 175       10.23   -146.29                                   
REMARK 500    ALA D 307       59.64    -92.63                                   
REMARK 500    THR K   0      130.04    -38.98                                   
REMARK 500    LYS L   2      -66.30   -131.81                                   
REMARK 500    LYS M   2      -70.01   -134.69                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH C 384        DISTANCE =  5.16 ANGSTROMS                       
REMARK 525    HOH C 396        DISTANCE =  5.21 ANGSTROMS                       
REMARK 525    HOH C 413        DISTANCE =  5.16 ANGSTROMS                       
REMARK 525    HOH C 538        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH D 507        DISTANCE =  5.27 ANGSTROMS                       
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 C 298  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 145   OD2                                                    
REMARK 620 2 ADP C 297   O2B  94.5                                              
REMARK 620 3 ASP C 145   OD1  55.8  94.9                                        
REMARK 620 4 HOH C 551   O   141.9  91.6  86.2                                  
REMARK 620 5 HOH C 304   O    77.0 167.0  72.2  89.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 299  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 132   OD1                                                    
REMARK 620 2 ADP A 297   O3B 172.2                                              
REMARK 620 3 ADP A 297   O1A  90.2  82.0                                        
REMARK 620 4 ASP A 145   OD2  91.3  88.2  81.6                                  
REMARK 620 5 HOH A 341   O    86.2  93.0  89.3 170.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 298  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 145   OD2                                                    
REMARK 620 2 ADP A 297   O2B  94.4                                              
REMARK 620 3 ASP A 145   OD1  56.6  97.9                                        
REMARK 620 4 HOH A 333   O   150.1 111.4 103.3                                  
REMARK 620 5 HOH A 306   O    75.7 168.7  81.3  79.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 299  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP C 297   O3B                                                    
REMARK 620 2 ADP C 297   O1A  83.4                                              
REMARK 620 3 ASN C 132   OD1 169.6  86.3                                        
REMARK 620 4 ASP C 145   OD2  88.4  80.1  91.4                                  
REMARK 620 5 HOH C 352   O    89.0  92.3  89.9 172.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             MGF A 300  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR K   0   OG1                                                    
REMARK 620 2 MGF A 300   F1   73.6                                              
REMARK 620 3 MGF A 300   F2  107.2 121.3                                        
REMARK 620 4 MGF A 300   F3   88.1 119.0 119.7                                  
REMARK 620 5 ADP A 297   O3B 163.2  89.6  82.2  99.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             MGF C 300  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR J   0   OG1                                                    
REMARK 620 2 MGF C 300   F1   83.0                                              
REMARK 620 3 MGF C 300   F2  104.0 120.6                                        
REMARK 620 4 MGF C 300   F3   82.7 120.3 119.1                                  
REMARK 620 5 ADP C 297   O3B 174.0  91.0  79.4 100.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 297                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 298                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 299                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGF A 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 8                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 16                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 297                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 298                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 299                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGF C 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 7                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 13                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 15                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3QHW   RELATED DB: PDB                                   
REMARK 900 SAME COMPLEX AT PH 8.25                                              
DBREF  3QHR A    1   296  UNP    P24941   CDK2_HUMAN       1    296             
DBREF  3QHR B  173   432  UNP    P51943   CCNA2_MOUSE    163    422             
DBREF  3QHR C    1   296  UNP    P24941   CDK2_HUMAN       1    296             
DBREF  3QHR D  173   432  UNP    P51943   CCNA2_MOUSE    163    422             
DBREF  3QHR J   -2     7  PDB    3QHR     3QHR            -2      7             
DBREF  3QHR K   -2     7  PDB    3QHR     3QHR            -2      7             
DBREF  3QHR L   -2     7  PDB    3QHR     3QHR            -2      7             
DBREF  3QHR M   -2     7  PDB    3QHR     3QHR            -2      7             
SEQADV 3QHR GLY A   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 3QHR HIS A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 3QHR SER B  172  UNP  P51943              EXPRESSION TAG                 
SEQADV 3QHR GLY C   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 3QHR HIS C    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 3QHR SER D  172  UNP  P51943              EXPRESSION TAG                 
SEQRES   1 A  298  GLY HIS MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY          
SEQRES   2 A  298  GLU GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS          
SEQRES   3 A  298  LEU THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU          
SEQRES   4 A  298  ASP THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG          
SEQRES   5 A  298  GLU ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE          
SEQRES   6 A  298  VAL LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU          
SEQRES   7 A  298  TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS          
SEQRES   8 A  298  PHE MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO          
SEQRES   9 A  298  LEU ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU          
SEQRES  10 A  298  ALA PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU          
SEQRES  11 A  298  LYS PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE          
SEQRES  12 A  298  LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL          
SEQRES  13 A  298  PRO VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP          
SEQRES  14 A  298  TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR          
SEQRES  15 A  298  SER THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE          
SEQRES  16 A  298  ALA GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP          
SEQRES  17 A  298  SER GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU          
SEQRES  18 A  298  GLY THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER          
SEQRES  19 A  298  MET PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG          
SEQRES  20 A  298  GLN ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP          
SEQRES  21 A  298  GLY ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO          
SEQRES  22 A  298  ASN LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO          
SEQRES  23 A  298  PHE PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU              
SEQRES   1 B  261  SER ASN GLU VAL PRO ASP TYR GLN GLU ASP ILE HIS THR          
SEQRES   2 B  261  TYR LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS VAL          
SEQRES   3 B  261  GLY TYR MET LYS ARG GLN PRO ASP ILE THR ASN SER MET          
SEQRES   4 B  261  ARG ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU          
SEQRES   5 B  261  GLU TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA VAL          
SEQRES   6 B  261  ASN TYR ILE ASP ARG PHE LEU SER SER MET SER VAL LEU          
SEQRES   7 B  261  ARG GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET LEU          
SEQRES   8 B  261  LEU ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL          
SEQRES   9 B  261  ALA GLU PHE VAL TYR ILE THR ASP ASP THR TYR SER LYS          
SEQRES  10 B  261  LYS GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS VAL          
SEQRES  11 B  261  LEU ALA PHE ASP LEU ALA ALA PRO THR VAL ASN GLN PHE          
SEQRES  12 B  261  LEU THR GLN TYR PHE LEU HIS LEU GLN PRO ALA ASN CYS          
SEQRES  13 B  261  LYS VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU SER          
SEQRES  14 B  261  LEU ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO SER          
SEQRES  15 B  261  LEU ILE ALA GLY ALA ALA PHE HIS LEU ALA LEU TYR THR          
SEQRES  16 B  261  VAL THR GLY GLN SER TRP PRO GLU SER LEU ALA GLN GLN          
SEQRES  17 B  261  THR GLY TYR THR LEU GLU SER LEU LYS PRO CYS LEU VAL          
SEQRES  18 B  261  ASP LEU HIS GLN THR TYR LEU LYS ALA PRO GLN HIS ALA          
SEQRES  19 B  261  GLN GLN SER ILE ARG GLU LYS TYR LYS HIS SER LYS TYR          
SEQRES  20 B  261  HIS SER VAL SER LEU LEU ASN PRO PRO GLU THR LEU SER          
SEQRES  21 B  261  VAL                                                          
SEQRES   1 C  298  GLY HIS MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY          
SEQRES   2 C  298  GLU GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS          
SEQRES   3 C  298  LEU THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU          
SEQRES   4 C  298  ASP THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG          
SEQRES   5 C  298  GLU ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE          
SEQRES   6 C  298  VAL LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU          
SEQRES   7 C  298  TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS          
SEQRES   8 C  298  PHE MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO          
SEQRES   9 C  298  LEU ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU          
SEQRES  10 C  298  ALA PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU          
SEQRES  11 C  298  LYS PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE          
SEQRES  12 C  298  LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL          
SEQRES  13 C  298  PRO VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP          
SEQRES  14 C  298  TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR          
SEQRES  15 C  298  SER THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE          
SEQRES  16 C  298  ALA GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP          
SEQRES  17 C  298  SER GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU          
SEQRES  18 C  298  GLY THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER          
SEQRES  19 C  298  MET PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG          
SEQRES  20 C  298  GLN ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP          
SEQRES  21 C  298  GLY ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO          
SEQRES  22 C  298  ASN LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO          
SEQRES  23 C  298  PHE PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU              
SEQRES   1 D  261  SER ASN GLU VAL PRO ASP TYR GLN GLU ASP ILE HIS THR          
SEQRES   2 D  261  TYR LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS VAL          
SEQRES   3 D  261  GLY TYR MET LYS ARG GLN PRO ASP ILE THR ASN SER MET          
SEQRES   4 D  261  ARG ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU          
SEQRES   5 D  261  GLU TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA VAL          
SEQRES   6 D  261  ASN TYR ILE ASP ARG PHE LEU SER SER MET SER VAL LEU          
SEQRES   7 D  261  ARG GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET LEU          
SEQRES   8 D  261  LEU ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL          
SEQRES   9 D  261  ALA GLU PHE VAL TYR ILE THR ASP ASP THR TYR SER LYS          
SEQRES  10 D  261  LYS GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS VAL          
SEQRES  11 D  261  LEU ALA PHE ASP LEU ALA ALA PRO THR VAL ASN GLN PHE          
SEQRES  12 D  261  LEU THR GLN TYR PHE LEU HIS LEU GLN PRO ALA ASN CYS          
SEQRES  13 D  261  LYS VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU SER          
SEQRES  14 D  261  LEU ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO SER          
SEQRES  15 D  261  LEU ILE ALA GLY ALA ALA PHE HIS LEU ALA LEU TYR THR          
SEQRES  16 D  261  VAL THR GLY GLN SER TRP PRO GLU SER LEU ALA GLN GLN          
SEQRES  17 D  261  THR GLY TYR THR LEU GLU SER LEU LYS PRO CYS LEU VAL          
SEQRES  18 D  261  ASP LEU HIS GLN THR TYR LEU LYS ALA PRO GLN HIS ALA          
SEQRES  19 D  261  GLN GLN SER ILE ARG GLU LYS TYR LYS HIS SER LYS TYR          
SEQRES  20 D  261  HIS SER VAL SER LEU LEU ASN PRO PRO GLU THR LEU SER          
SEQRES  21 D  261  VAL                                                          
SEQRES   1 J   10  PRO LYS THR PRO LYS LYS ALA LYS LYS LEU                      
SEQRES   1 K   10  PRO LYS THR PRO LYS LYS ALA LYS LYS LEU                      
SEQRES   1 L   10  PRO LYS THR PRO LYS LYS ALA LYS LYS LEU                      
SEQRES   1 M   10  PRO LYS THR PRO LYS LYS ALA LYS LYS LEU                      
MODRES 3QHR TPO A  160  THR  PHOSPHOTHREONINE                                   
MODRES 3QHR TPO C  160  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET    ADP  A 297      27                                                       
HET     MG  A 298       1                                                       
HET     MG  A 299       1                                                       
HET    MGF  A 300       4                                                       
HET     CL  A 301       1                                                       
HET    GOL  A 302       6                                                       
HET    GOL  A 303       6                                                       
HET    GOL  A 304       6                                                       
HET    GOL  A 305       6                                                       
HET    GOL  B   1       6                                                       
HET    GOL  B   3       6                                                       
HET    GOL  B   6       6                                                       
HET    GOL  B   8       6                                                       
HET    GOL  B  16       6                                                       
HET    ADP  C 297      27                                                       
HET     MG  C 298       1                                                       
HET     MG  C 299       1                                                       
HET    MGF  C 300       4                                                       
HET     CL  C 301       1                                                       
HET    GOL  C 302       6                                                       
HET    GOL  C 303       6                                                       
HET    GOL  D   2       6                                                       
HET    GOL  D   5       6                                                       
HET    GOL  D   7       6                                                       
HET    GOL  D  13       6                                                       
HET    GOL  D  15       6                                                       
HET    GOL  K  12       6                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     MGF TRIFLUOROMAGNESATE                                               
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   9  ADP    2(C10 H15 N5 O10 P2)                                         
FORMUL  10   MG    4(MG 2+)                                                     
FORMUL  12  MGF    2(F3 MG 1-)                                                  
FORMUL  13   CL    2(CL 1-)                                                     
FORMUL  14  GOL    17(C3 H8 O3)                                                 
FORMUL  36  HOH   *601(H2 O)                                                    
HELIX    1   1 HIS A    0  GLU A    2  5                                   3    
HELIX    2   2 PRO A   45  GLU A   57  1                                  13    
HELIX    3   3 LEU A   87  SER A   94  1                                   8    
HELIX    4   4 PRO A  100  HIS A  121  1                                  22    
HELIX    5   5 LYS A  129  GLN A  131  5                                   3    
HELIX    6   6 THR A  165  ARG A  169  5                                   5    
HELIX    7   7 ALA A  170  LEU A  175  1                                   6    
HELIX    8   8 THR A  182  ARG A  199  1                                  18    
HELIX    9   9 SER A  207  GLY A  220  1                                  14    
HELIX   10  10 GLY A  229  MET A  233  5                                   5    
HELIX   11  11 ASP A  247  VAL A  252  1                                   6    
HELIX   12  12 ASP A  256  LEU A  267  1                                  12    
HELIX   13  13 SER A  276  LEU A  281  1                                   6    
HELIX   14  14 ALA A  282  GLN A  287  5                                   6    
HELIX   15  15 VAL B  175  VAL B  191  1                                  17    
HELIX   16  16 GLY B  198  GLN B  203  5                                   6    
HELIX   17  17 THR B  207  LYS B  226  1                                  20    
HELIX   18  18 GLN B  228  SER B  244  1                                  17    
HELIX   19  19 LEU B  249  GLU B  269  1                                  21    
HELIX   20  20 GLU B  274  THR B  282  1                                   9    
HELIX   21  21 SER B  287  ALA B  303  1                                  17    
HELIX   22  22 THR B  310  LEU B  320  1                                  11    
HELIX   23  23 ASN B  326  SER B  340  1                                  15    
HELIX   24  24 ASP B  343  LEU B  348  1                                   6    
HELIX   25  25 LEU B  351  GLY B  369  1                                  19    
HELIX   26  26 PRO B  373  GLY B  381  1                                   9    
HELIX   27  27 THR B  383  LYS B  400  1                                  18    
HELIX   28  28 GLN B  407  TYR B  413  1                                   7    
HELIX   29  29 LYS B  414  HIS B  419  5                                   6    
HELIX   30  30 SER B  420  LEU B  424  5                                   5    
HELIX   31  31 HIS C    0  GLU C    2  5                                   3    
HELIX   32  32 PRO C   45  GLU C   57  1                                  13    
HELIX   33  33 LEU C   87  SER C   94  1                                   8    
HELIX   34  34 PRO C  100  HIS C  121  1                                  22    
HELIX   35  35 LYS C  129  GLN C  131  5                                   3    
HELIX   36  36 THR C  165  ARG C  169  5                                   5    
HELIX   37  37 ALA C  170  LEU C  175  1                                   6    
HELIX   38  38 THR C  182  ARG C  199  1                                  18    
HELIX   39  39 SER C  207  GLY C  220  1                                  14    
HELIX   40  40 GLY C  229  MET C  233  5                                   5    
HELIX   41  41 ASP C  247  VAL C  252  1                                   6    
HELIX   42  42 ASP C  256  LEU C  267  1                                  12    
HELIX   43  43 SER C  276  LEU C  281  1                                   6    
HELIX   44  44 ALA C  282  GLN C  287  5                                   6    
HELIX   45  45 TYR D  178  VAL D  191  1                                  14    
HELIX   46  46 GLY D  198  GLN D  203  5                                   6    
HELIX   47  47 THR D  207  TYR D  225  1                                  19    
HELIX   48  48 GLN D  228  SER D  244  1                                  17    
HELIX   49  49 LEU D  249  GLU D  269  1                                  21    
HELIX   50  50 GLU D  274  THR D  282  1                                   9    
HELIX   51  51 SER D  287  ALA D  303  1                                  17    
HELIX   52  52 THR D  310  LEU D  320  1                                  11    
HELIX   53  53 ASN D  326  ASP D  343  1                                  18    
HELIX   54  54 ASP D  343  LEU D  348  1                                   6    
HELIX   55  55 LEU D  351  GLY D  369  1                                  19    
HELIX   56  56 PRO D  373  GLY D  381  1                                   9    
HELIX   57  57 THR D  383  LYS D  400  1                                  18    
HELIX   58  58 GLN D  407  TYR D  413  1                                   7    
HELIX   59  59 LYS D  414  HIS D  419  5                                   6    
HELIX   60  60 SER D  420  LEU D  424  5                                   5    
SHEET    1   A 5 PHE A   4  GLU A  12  0                                        
SHEET    2   A 5 VAL A  17  ASN A  23 -1  O  LYS A  20   N  VAL A   7           
SHEET    3   A 5 VAL A  29  ARG A  36 -1  O  LYS A  34   N  VAL A  17           
SHEET    4   A 5 LYS A  75  GLU A  81 -1  O  PHE A  80   N  ALA A  31           
SHEET    5   A 5 LEU A  66  HIS A  71 -1  N  LEU A  67   O  VAL A  79           
SHEET    1   B 3 GLN A  85  ASP A  86  0                                        
SHEET    2   B 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3   B 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1   C 2 VAL A 123  LEU A 124  0                                        
SHEET    2   C 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SHEET    1   D 5 PHE C   4  GLU C  12  0                                        
SHEET    2   D 5 VAL C  17  ASN C  23 -1  O  ARG C  22   N  GLN C   5           
SHEET    3   D 5 VAL C  29  ARG C  36 -1  O  LYS C  34   N  VAL C  17           
SHEET    4   D 5 LYS C  75  GLU C  81 -1  O  LEU C  78   N  LYS C  33           
SHEET    5   D 5 LEU C  66  HIS C  71 -1  N  LEU C  67   O  VAL C  79           
SHEET    1   E 3 GLN C  85  ASP C  86  0                                        
SHEET    2   E 3 LEU C 133  ILE C 135 -1  O  ILE C 135   N  GLN C  85           
SHEET    3   E 3 ILE C 141  LEU C 143 -1  O  LYS C 142   N  LEU C 134           
SHEET    1   F 2 VAL C 123  LEU C 124  0                                        
SHEET    2   F 2 ARG C 150  ALA C 151 -1  O  ARG C 150   N  LEU C 124           
LINK         C   TYR A 159                 N   TPO A 160     1555   1555  1.34  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.33  
LINK         C   TYR C 159                 N   TPO C 160     1555   1555  1.33  
LINK         C   TPO C 160                 N   HIS C 161     1555   1555  1.33  
LINK         OD2 ASP C 145                MG    MG C 298     1555   1555  2.10  
LINK         OD1 ASN A 132                MG    MG A 299     1555   1555  2.13  
LINK         OD2 ASP A 145                MG    MG A 298     1555   1555  2.14  
LINK         O2B ADP C 297                MG    MG C 298     1555   1555  2.15  
LINK         O3B ADP C 297                MG    MG C 299     1555   1555  2.19  
LINK         O1A ADP C 297                MG    MG C 299     1555   1555  2.20  
LINK         OD1 ASN C 132                MG    MG C 299     1555   1555  2.23  
LINK         O3B ADP A 297                MG    MG A 299     1555   1555  2.24  
LINK         O1A ADP A 297                MG    MG A 299     1555   1555  2.28  
LINK         O2B ADP A 297                MG    MG A 298     1555   1555  2.28  
LINK         OD1 ASP A 145                MG    MG A 298     1555   1555  2.29  
LINK         OD2 ASP C 145                MG    MG C 299     1555   1555  2.31  
LINK         OD1 ASP C 145                MG    MG C 298     1555   1555  2.39  
LINK         OG1 THR K   0                MG   MGF A 300     1555   1555  2.50  
LINK         OD2 ASP A 145                MG    MG A 299     1555   1555  2.50  
LINK         OG1 THR J   0                MG   MGF C 300     1555   1555  2.59  
LINK         O3B ADP C 297                MG   MGF C 300     1555   1555  2.59  
LINK         O3B ADP A 297                MG   MGF A 300     1555   1555  2.76  
LINK        MG    MG A 299                 O   HOH A 341     1555   1555  2.00  
LINK        MG    MG C 299                 O   HOH C 352     1555   1555  2.03  
LINK        MG    MG A 298                 O   HOH A 333     1555   1555  2.07  
LINK        MG    MG C 298                 O   HOH C 551     1555   1555  2.15  
LINK        MG    MG A 298                 O   HOH A 306     1555   1555  2.41  
LINK        MG    MG C 298                 O   HOH C 304     1555   1555  2.71  
CISPEP   1 VAL A  154    PRO A  155          0        -4.16                     
CISPEP   2 GLN B  323    PRO B  324          0        -5.20                     
CISPEP   3 ASP B  345    PRO B  346          0         2.29                     
CISPEP   4 VAL C  154    PRO C  155          0        -3.12                     
CISPEP   5 GLN D  323    PRO D  324          0        -4.43                     
CISPEP   6 ASP D  345    PRO D  346          0         1.95                     
SITE     1 AC1 21 ILE A  10  GLY A  11  GLY A  13  THR A  14                    
SITE     2 AC1 21 TYR A  15  GLY A  16  ALA A  31  LYS A  33                    
SITE     3 AC1 21 GLU A  81  LEU A  83  ASP A  86  GLN A 131                    
SITE     4 AC1 21 ASN A 132  LEU A 134  ASP A 145   MG A 298                    
SITE     5 AC1 21  MG A 299  MGF A 300  HOH A 307  HOH A 341                    
SITE     6 AC1 21 HOH A 574                                                     
SITE     1 AC2  6 TYR A  15  ASP A 145  ADP A 297  MGF A 300                    
SITE     2 AC2  6 HOH A 306  HOH A 333                                          
SITE     1 AC3  5 ASN A 132  ASP A 145  ADP A 297  MGF A 300                    
SITE     2 AC3  5 HOH A 341                                                     
SITE     1 AC4 14 GLY A  13  THR A  14  TYR A  15  ASP A 127                    
SITE     2 AC4 14 LYS A 129  ASN A 132  ASP A 145  ADP A 297                    
SITE     3 AC4 14  MG A 298   MG A 299  HOH A 306  HOH A 333                    
SITE     4 AC4 14 HOH A 654  THR K   0                                          
SITE     1 AC5  3 PRO A 130  GLN A 131  HOH A 360                               
SITE     1 AC6  6 LYS A 105  ASP A 256  ASP A 258  PRO A 284                    
SITE     2 AC6  6 GLN A 287  ASP A 288                                          
SITE     1 AC7  7 THR A 158  TYR A 159  TPO A 160  HIS A 161                    
SITE     2 AC7  7 GLU A 162  HOH A 559  TYR B 271                               
SITE     1 AC8  7 GLY A  -1  PHE A   4  ASN A  23  GLU A  28                    
SITE     2 AC8  7 ASP A  68  GOL A 305  HOH A 448                               
SITE     1 AC9  4 GLY A  -1  ASP A  68  GOL A 304  LYS D 300                    
SITE     1 BC1  6 HIS B 233  ASN B 237  PRO B 309  THR B 310                    
SITE     2 BC1  6 VAL B 311  HOH B 452                                          
SITE     1 BC2  6 TYR B 199  ARG B 202  GLN B 203  LEU B 243                    
SITE     2 BC2  6 SER B 244  SER B 247                                          
SITE     1 BC3  8 HOH B  91  SER B 209  ALA B 212  ASP B 343                    
SITE     2 BC3  8 HIS B 404  GLN B 406  HOH B 441  HOH B 518                    
SITE     1 BC4  3 THR B 380  HOH B 459  HOH B 502                               
SITE     1 BC5  8 GLY B 251  LYS B 252  THR B 285  TYR B 286                    
SITE     2 BC5  8 GLN B 290  HOH B 476  HOH B 483  LYS L   6                    
SITE     1 BC6 24 ILE C  10  GLY C  11  GLY C  13  THR C  14                    
SITE     2 BC6 24 TYR C  15  GLY C  16  ALA C  31  LYS C  33                    
SITE     3 BC6 24 GLU C  81  LEU C  83  ASP C  86  LYS C  89                    
SITE     4 BC6 24 GLN C 131  ASN C 132  LEU C 134  ASP C 145                    
SITE     5 BC6 24  MG C 298   MG C 299  MGF C 300  HOH C 308                    
SITE     6 BC6 24 HOH C 352  HOH C 551  HOH C 560  HOH C 561                    
SITE     1 BC7  6 TYR C  15  ASP C 145  ADP C 297  MGF C 300                    
SITE     2 BC7  6 HOH C 304  HOH C 551                                          
SITE     1 BC8  5 ASN C 132  ASP C 145  ADP C 297  MGF C 300                    
SITE     2 BC8  5 HOH C 352                                                     
SITE     1 BC9 12 GLY C  13  THR C  14  TYR C  15  ASP C 127                    
SITE     2 BC9 12 LYS C 129  ASN C 132  ASP C 145  ADP C 297                    
SITE     3 BC9 12  MG C 298   MG C 299  THR J   0  HOH J 655                    
SITE     1 CC1  2 PRO C 130  GLN C 131                                          
SITE     1 CC2  7 LYS C  88  MET C  91  ASP C  92  GLU C 195                    
SITE     2 CC2  7 ARG C 199  ARG C 200  ALA C 201                               
SITE     1 CC3  4 LYS C  56  LEU C  66  VAL C  69  HOH C 627                    
SITE     1 CC4  2 GLN D 379  THR D 380                                          
SITE     1 CC5  7 HIS D 233  ASN D 237  PRO D 309  THR D 310                    
SITE     2 CC5  7 VAL D 311  LEU D 341  HOH D 567                               
SITE     1 CC6  5 MET D 200  GLN D 203  ILE D 206  THR D 207                    
SITE     2 CC6  5 ASN D 208                                                     
SITE     1 CC7  3 LYS D 252  GLN D 290  LYS M   6                               
SITE     1 CC8  6 TYR D 199  ARG D 202  LEU D 243  SER D 244                    
SITE     2 CC8  6 MET D 246  SER D 247                                          
CRYST1   70.690  163.910   73.280  90.00 107.38  90.00 P 1 21 1      8          
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      0.014146  0.000000  0.004428        0.00000                         
SCALE2      0.000000  0.006101  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014299        0.00000                         
MTRIX1   1  0.825892  0.020226  0.563465       11.51420    1                    
MTRIX2   1  0.022007 -0.999751  0.003630      -51.02090    1                    
MTRIX3   1  0.563398  0.009402 -0.826132      -34.90290    1                    
MTRIX1   2  0.826285  0.033518  0.562254       11.50480    1                    
MTRIX2   2  0.036510 -0.999316  0.005918      -51.05680    1                    
MTRIX3   2  0.562068  0.015638 -0.826943      -34.91910    1                    
MTRIX1   3  0.814910  0.039063  0.578269       11.70750    1                    
MTRIX2   3  0.038742 -0.999166  0.012900      -50.97060    1                    
MTRIX3   3  0.578291  0.011891 -0.815744      -34.95580    1                    
MTRIX1   4  0.821214  0.003820  0.570607       11.75080    1                    
MTRIX2   4  0.030488 -0.998843 -0.037191      -52.70210    1                    
MTRIX3   4  0.569805  0.047938 -0.820381      -34.49120    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system