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Database: PDB
Entry: 3QHW
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HEADER    TRANSFERASE/PROTEIN BINDING             26-JAN-11   3QHW              
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 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  10 ORGANISM_COMMON: MOUSE;                                              
SOURCE  11 ORGANISM_TAXID: 10090;                                               
SOURCE  12 GENE: CCNA2, CCNA, CYCA;                                             
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 SYNTHETIC: YES;                                                      
SOURCE  17 OTHER_DETAILS: OPTIMAL CDK2 KINASE SUBSTRATE                         
KEYWDS    KINASE CATALYTIC DOMAIN, PROTEIN KINASE, CYCLIN, PHOSPHORYLATED THR-  
KEYWDS   2 160, PHOSPHORYLATED ON THR-160, TRANSFERASE-PROTEIN BINDING COMPLEX  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.YOUNG,D.M.JACOBSEN,Z.Q.BAO                                        
REVDAT   1   25-MAY-11 3QHW    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.    1.91 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) : 1.91                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.73                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 123234                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.950                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2401                            
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 39.7341 -  4.9083    1.00     7205   143  0.1966 0.2104        
REMARK   3     2  4.9083 -  3.8969    1.00     7154   143  0.1495 0.1580        
REMARK   3     3  3.8969 -  3.4046    1.00     7136   141  0.1683 0.1999        
REMARK   3     4  3.4046 -  3.0935    1.00     7121   141  0.1674 0.2248        
REMARK   3     5  3.0935 -  2.8718    1.00     7134   144  0.1616 0.2069        
REMARK   3     6  2.8718 -  2.7026    1.00     7106   141  0.1535 0.1893        
REMARK   3     7  2.7026 -  2.5672    1.00     7151   137  0.1692 0.2129        
REMARK   3     8  2.5672 -  2.4555    1.00     7079   144  0.1795 0.2091        
REMARK   3     9  2.4555 -  2.3610    1.00     7082   145  0.1909 0.2230        
REMARK   3    10  2.3610 -  2.2795    1.00     7115   132  0.1981 0.2622        
REMARK   3    11  2.2795 -  2.2082    1.00     7129   148  0.2083 0.2496        
REMARK   3    12  2.2082 -  2.1451    1.00     7071   144  0.2240 0.2637        
REMARK   3    13  2.1451 -  2.0887    1.00     7089   143  0.2398 0.2725        
REMARK   3    14  2.0887 -  2.0377    1.00     7120   133  0.2639 0.3149        
REMARK   3    15  2.0377 -  1.9914    1.00     7126   138  0.3033 0.3202        
REMARK   3    16  1.9914 -  1.9490    1.00     7122   124  0.3361 0.3485        
REMARK   3    17  1.9490 -  1.9100    0.97     6893   160  0.3755 0.4115        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.95                                          
REMARK   3   K_SOL              : 0.38                                          
REMARK   3   B_SOL              : 61.71                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.660            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.340           
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) : 9.91220                                              
REMARK   3    B22 (A**2) : -6.73530                                             
REMARK   3    B33 (A**2) : -3.17690                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 8.05380                                              
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      :  0.010           9587                                  
REMARK   3   ANGLE     :  1.266          13016                                  
REMARK   3   CHIRALITY :  0.091           1475                                  
REMARK   3   PLANARITY :  0.007           1624                                  
REMARK   3   DIHEDRAL  : 13.923           3594                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 21                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 1:21)                               
REMARK   3    ORIGIN FOR THE GROUP (A): -19.4139 -66.1019 -68.8677              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8169 T22:   0.2512                                     
REMARK   3      T33:   0.4758 T12:  -0.0240                                     
REMARK   3      T13:  -0.2418 T23:   0.0312                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3836 L22:   5.5355                                     
REMARK   3      L33:   2.4044 L12:  -0.6287                                     
REMARK   3      L13:   0.3188 L23:  -3.6396                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1951 S12:  -0.2080 S13:  -0.3133                       
REMARK   3      S21:   0.9515 S22:   0.2880 S23:   0.9299                       
REMARK   3      S31:   1.0157 S32:  -0.3770 S33:  -0.3827                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 22:37)                              
REMARK   3    ORIGIN FOR THE GROUP (A): -16.7385 -61.1983 -66.2717              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3987 T22:   0.3176                                     
REMARK   3      T33:   0.2323 T12:  -0.0315                                     
REMARK   3      T13:  -0.1191 T23:   0.0026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3469 L22:   3.9188                                     
REMARK   3      L33:   8.4760 L12:  -0.6980                                     
REMARK   3      L13:  -3.0050 L23:   0.9653                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2594 S12:   0.1190 S13:  -0.0182                       
REMARK   3      S21:  -0.9704 S22:   0.2663 S23:   0.2126                       
REMARK   3      S31:   0.6456 S32:  -0.9257 S33:  -0.1137                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 38:46)                              
REMARK   3    ORIGIN FOR THE GROUP (A): -24.2988 -74.7124 -52.6240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5166 T22:   0.6797                                     
REMARK   3      T33:   0.4896 T12:  -0.0658                                     
REMARK   3      T13:  -0.1975 T23:  -0.0814                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5937 L22:   2.0021                                     
REMARK   3      L33:   2.0015 L12:   2.6120                                     
REMARK   3      L13:  -5.0969 L23:  -4.0957                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2398 S12:   1.3640 S13:  -0.1228                       
REMARK   3      S21:  -1.6068 S22:   0.0356 S23:   2.0565                       
REMARK   3      S31:   0.1570 S32:  -2.3992 S33:  -0.1096                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 47:160)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.6866 -74.5648 -64.9151              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2788 T22:   0.1229                                     
REMARK   3      T33:   0.1419 T12:  -0.0313                                     
REMARK   3      T13:  -0.0210 T23:  -0.0020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5982 L22:   2.3252                                     
REMARK   3      L33:   4.1859 L12:  -0.3805                                     
REMARK   3      L13:  -1.0585 L23:   0.4663                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0468 S12:   0.1200 S13:   0.0386                       
REMARK   3      S21:  -0.3260 S22:  -0.0336 S23:   0.0680                       
REMARK   3      S31:  -0.1514 S32:  -0.1060 S33:  -0.0137                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 161:296)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   1.2856 -93.2084 -68.6506              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3065 T22:   0.1665                                     
REMARK   3      T33:   0.1591 T12:   0.0090                                     
REMARK   3      T13:   0.0263 T23:  -0.0304                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5925 L22:   4.3440                                     
REMARK   3      L33:   1.9164 L12:   1.2706                                     
REMARK   3      L13:  -0.0089 L23:  -0.0219                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0014 S12:   0.0671 S13:  -0.1655                       
REMARK   3      S21:  -0.2765 S22:   0.0318 S23:  -0.0792                       
REMARK   3      S31:   0.0969 S32:   0.1339 S33:  -0.0444                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 175:192)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   7.3609 -75.2093 -47.7656              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2227 T22:   0.2804                                     
REMARK   3      T33:   0.2272 T12:   0.0074                                     
REMARK   3      T13:   0.0408 T23:  -0.0664                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2904 L22:   5.8190                                     
REMARK   3      L33:   3.2524 L12:  -1.7818                                     
REMARK   3      L13:  -1.4723 L23:   3.5041                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1521 S12:   0.6709 S13:  -0.4848                       
REMARK   3      S21:  -0.3726 S22:  -0.0361 S23:  -0.1972                       
REMARK   3      S31:   0.3532 S32:   0.4002 S33:  -0.0315                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 193:308)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -15.8320 -71.8321 -36.8843              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1280 T22:   0.1146                                     
REMARK   3      T33:   0.1463 T12:   0.0172                                     
REMARK   3      T13:  -0.0038 T23:   0.0184                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3303 L22:   3.5961                                     
REMARK   3      L33:   2.9016 L12:  -0.2377                                     
REMARK   3      L13:  -0.9806 L23:   0.3602                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1250 S12:  -0.0286 S13:  -0.0835                       
REMARK   3      S21:   0.1888 S22:   0.0814 S23:   0.2031                       
REMARK   3      S31:   0.0931 S32:  -0.0102 S33:   0.0322                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 309:402)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   6.3370 -80.5956 -30.4887              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1814 T22:   0.2305                                     
REMARK   3      T33:   0.1915 T12:   0.0727                                     
REMARK   3      T13:  -0.0348 T23:  -0.0021                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1216 L22:   3.5603                                     
REMARK   3      L33:   3.2170 L12:   0.4952                                     
REMARK   3      L13:  -0.3757 L23:  -1.2199                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2034 S12:  -0.3373 S13:  -0.2249                       
REMARK   3      S21:   0.1818 S22:   0.1361 S23:  -0.3017                       
REMARK   3      S31:   0.1438 S32:   0.2823 S33:   0.0299                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 403:432)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.9902 -87.2437 -22.7798              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4176 T22:   0.2816                                     
REMARK   3      T33:   0.2099 T12:   0.0957                                     
REMARK   3      T13:   0.0821 T23:   0.1492                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0235 L22:   3.8304                                     
REMARK   3      L33:   7.6252 L12:  -0.5962                                     
REMARK   3      L13:   0.3824 L23:   1.5677                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2864 S12:  -0.3393 S13:  -0.7049                       
REMARK   3      S21:   0.4545 S22:   0.2166 S23:  -0.0154                       
REMARK   3      S31:   0.2434 S32:   0.4894 S33:   0.0970                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 1:21)                               
REMARK   3    ORIGIN FOR THE GROUP (A): -28.5360 -43.3507 -39.7479              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2784 T22:   0.2027                                     
REMARK   3      T33:   0.5320 T12:   0.0840                                     
REMARK   3      T13:   0.0752 T23:   0.0304                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3296 L22:   4.5329                                     
REMARK   3      L33:   4.0515 L12:   0.9726                                     
REMARK   3      L13:   0.8754 L23:  -2.9746                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2114 S12:   0.2736 S13:   0.3416                       
REMARK   3      S21:  -0.6286 S22:  -0.1470 S23:   0.7412                       
REMARK   3      S31:  -0.1578 S32:  -0.3343 S33:  -0.0439                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 22:37)                              
REMARK   3    ORIGIN FOR THE GROUP (A): -25.2817 -49.7506 -40.5400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1909 T22:   0.3413                                     
REMARK   3      T33:   0.3423 T12:   0.0886                                     
REMARK   3      T13:   0.0680 T23:   0.0508                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8034 L22:   6.4515                                     
REMARK   3      L33:   5.0445 L12:  -0.3316                                     
REMARK   3      L13:   0.6733 L23:   2.1911                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3775 S12:   0.6722 S13:   0.1309                       
REMARK   3      S21:   0.2035 S22:  -0.1057 S23:   0.7540                       
REMARK   3      S31:  -0.4608 S32:  -0.3503 S33:  -0.2970                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 38:46)                              
REMARK   3    ORIGIN FOR THE GROUP (A): -23.8170 -36.9576 -55.5459              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6237 T22:   0.6374                                     
REMARK   3      T33:   0.7711 T12:   0.1970                                     
REMARK   3      T13:  -0.0337 T23:   0.0944                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.4350 L22:   2.0033                                     
REMARK   3      L33:   2.0017 L12:  -3.0059                                     
REMARK   3      L13:  -3.1149 L23:  -6.7036                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0227 S12:   0.1243 S13:   0.1836                       
REMARK   3      S21:  -0.5138 S22:   0.4219 S23:   2.7026                       
REMARK   3      S31:  -0.5103 S32:  -2.5396 S33:  -0.3174                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 47:160)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -14.3795 -36.8911 -34.4102              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2027 T22:   0.1119                                     
REMARK   3      T33:   0.1616 T12:   0.0497                                     
REMARK   3      T13:   0.0354 T23:   0.0251                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3138 L22:   2.9817                                     
REMARK   3      L33:   4.0746 L12:   0.0912                                     
REMARK   3      L13:   0.0658 L23:   0.5666                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0036 S12:   0.0143 S13:  -0.0421                       
REMARK   3      S21:   0.0187 S22:  -0.0526 S23:   0.1756                       
REMARK   3      S31:   0.2423 S32:   0.0049 S33:   0.0544                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 161:296)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -11.7811 -18.2013 -28.0451              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1525 T22:   0.1783                                     
REMARK   3      T33:   0.1839 T12:  -0.0145                                     
REMARK   3      T13:   0.0279 T23:  -0.0313                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6220 L22:   5.4513                                     
REMARK   3      L33:   2.5278 L12:  -1.4210                                     
REMARK   3      L13:   0.1763 L23:  -1.1508                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0286 S12:  -0.1441 S13:   0.2711                       
REMARK   3      S21:   0.0891 S22:  -0.0482 S23:  -0.0585                       
REMARK   3      S31:   0.0625 S32:   0.1269 S33:   0.0102                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 175:193)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   5.0244 -36.1478 -42.3559              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2770 T22:   0.3597                                     
REMARK   3      T33:   0.2042 T12:   0.0997                                     
REMARK   3      T13:   0.0158 T23:  -0.0373                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2734 L22:   7.1148                                     
REMARK   3      L33:   7.6746 L12:   0.5732                                     
REMARK   3      L13:  -1.0580 L23:   5.6210                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0989 S12:  -0.8938 S13:   0.5889                       
REMARK   3      S21:   0.0162 S22:  -0.2296 S23:   0.3287                       
REMARK   3      S31:  -0.4680 S32:   0.3396 S33:   0.1357                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 194:201)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   4.4185 -49.4201 -62.5398              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4322 T22:   0.3628                                     
REMARK   3      T33:   0.3360 T12:   0.0560                                     
REMARK   3      T13:   0.1005 T23:  -0.0559                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5816 L22:   9.6072                                     
REMARK   3      L33:   3.3747 L12:  -4.7330                                     
REMARK   3      L13:  -4.2897 L23:   1.5146                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3267 S12:  -0.2856 S13:  -0.0981                       
REMARK   3      S21:   0.0087 S22:   0.6592 S23:  -0.8513                       
REMARK   3      S31:   0.8442 S32:   1.3758 S33:  -0.9382                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 202:310)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.7645 -38.7099 -63.9032              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3524 T22:   0.1652                                     
REMARK   3      T33:   0.1805 T12:   0.0203                                     
REMARK   3      T13:   0.0171 T23:   0.0121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8824 L22:   2.3603                                     
REMARK   3      L33:   3.2290 L12:   0.3132                                     
REMARK   3      L13:   0.5563 L23:   0.3114                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0975 S12:   0.0292 S13:  -0.0130                       
REMARK   3      S21:  -0.3805 S22:   0.0996 S23:   0.0871                       
REMARK   3      S31:  -0.2351 S32:  -0.0092 S33:  -0.0004                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 311:402)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  14.0819 -30.1277 -56.9870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2734 T22:   0.3798                                     
REMARK   3      T33:   0.2073 T12:  -0.0521                                     
REMARK   3      T13:   0.0653 T23:  -0.0467                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1904 L22:   3.0710                                     
REMARK   3      L33:   4.8978 L12:  -0.0910                                     
REMARK   3      L13:  -0.0071 L23:  -0.9503                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1951 S12:   0.0347 S13:   0.0480                       
REMARK   3      S21:  -0.0798 S22:   0.1923 S23:  -0.3507                       
REMARK   3      S31:  -0.4120 S32:   0.8458 S33:  -0.0003                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 403:432)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  10.2438 -23.7405 -68.5332              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6733 T22:   0.4464                                     
REMARK   3      T33:   0.2587 T12:  -0.2101                                     
REMARK   3      T13:   0.0885 T23:   0.0638                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2671 L22:   3.1075                                     
REMARK   3      L33:   7.4177 L12:  -0.9964                                     
REMARK   3      L13:  -1.8780 L23:   4.1755                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3399 S12:   0.0663 S13:   0.5262                       
REMARK   3      S21:  -0.5054 S22:   0.2720 S23:  -0.3889                       
REMARK   3      S31:  -0.8714 S32:   0.9208 S33:  -0.1049                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: (CHAIN A AND RESID 297)                                
REMARK   3    ORIGIN FOR THE GROUP (A): -12.8180 -73.3585 -68.7642              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7626 T22:   0.5216                                     
REMARK   3      T33:   0.6993 T12:   0.0045                                     
REMARK   3      T13:   0.0249 T23:   0.2135                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8559 L22:   7.3271                                     
REMARK   3      L33:   3.4652 L12:  -4.3683                                     
REMARK   3      L13:   1.4344 L23:   1.9241                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3076 S12:  -0.4022 S13:  -0.4814                       
REMARK   3      S21:   1.0002 S22:  -0.5857 S23:   0.3636                       
REMARK   3      S31:   0.1515 S32:  -0.0264 S33:   0.8653                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 297)                                
REMARK   3    ORIGIN FOR THE GROUP (A): -23.2836 -38.2197 -35.7367              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1616 T22:   0.4492                                     
REMARK   3      T33:   0.7008 T12:  -0.2062                                     
REMARK   3      T13:  -0.0791 T23:   0.1384                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.3912 L22:   6.7030                                     
REMARK   3      L33:   0.8904 L12:  -5.2940                                     
REMARK   3      L13:  -2.5190 L23:   2.3134                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4100 S12:   0.6247 S13:   0.9832                       
REMARK   3      S21:  -1.0784 S22:  -0.2318 S23:   0.0142                       
REMARK   3      S31:  -0.3504 S32:  -0.1196 S33:  -0.1810                       
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 -1:296 ) and not        
REMARK   3                          (resseq 10:18) and not (resseq 129 or       
REMARK   3                          resseq 127 or resseq 145 or resseq 132 or   
REMARK   3                          resseq 160)                                 
REMARK   3     SELECTION          : chain C                                     
REMARK   3     ATOM PAIRS NUMBER  : 2282                                        
REMARK   3     RMSD               : 0.072                                       
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               : 0.154                                       
REMARK   3   NCS GROUP : 3                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain J and (resseq -2:7) and not (resseq   
REMARK   3                          0:1)                                        
REMARK   3     SELECTION          : chain K                                     
REMARK   3     ATOM PAIRS NUMBER  : 65                                          
REMARK   3     RMSD               : 0.552                                       
REMARK   3   NCS GROUP : 4                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain L and (resseq 4:7 )                   
REMARK   3     SELECTION          : chain M                                     
REMARK   3     ATOM PAIRS NUMBER  : 31                                          
REMARK   3     RMSD               : 0.035                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3QHW 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 RCSB063665.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-JUL-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.25                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872                            
REMARK 200  MONOCHROMATOR                  : KOHZU                              
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   : 123388                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.908                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.740                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.14000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.91                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.01                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.01400                            
REMARK 200  R SYM FOR SHELL            (I) : 1.41300                            
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 MODEL                                    
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% W/V POLY(ACRYLIC ACID SODIUM SALT)   
REMARK 280  5100, 20MM MGCL2, 100MM HEPES PH 8.25, 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       81.72500            
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: 7260 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, J, L                            
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: 7170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, K, M                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO L    -2                                                      
REMARK 465     LYS L    -1                                                      
REMARK 465     THR L     0                                                      
REMARK 465     PRO L     1                                                      
REMARK 465     LYS L     2                                                      
REMARK 465     LYS L     3                                                      
REMARK 465     PRO M    -2                                                      
REMARK 465     LYS M    -1                                                      
REMARK 465     THR M     0                                                      
REMARK 465     PRO M     1                                                      
REMARK 465     LYS M     2                                                      
REMARK 465     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    ASP A 127       37.82   -142.12                                   
REMARK 500    ASP A 145       75.18     54.44                                   
REMARK 500    VAL A 163      -86.88   -117.61                                   
REMARK 500    SER A 181     -157.91   -155.06                                   
REMARK 500    PHE B 304       19.31     58.52                                   
REMARK 500    VAL C   7      -61.40    -98.55                                   
REMARK 500    ASP C 127       39.77   -142.52                                   
REMARK 500    ASP C 145       71.73     57.50                                   
REMARK 500    VAL C 163      -80.28   -123.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    TYR A  15        23.2      L          L   OUTSIDE RANGE           
REMARK 500    ASN C  62        24.8      L          L   OUTSIDE RANGE           
REMARK 500    VAL C 163        23.4      L          L   OUTSIDE RANGE           
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 A 375        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH A 578        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH A 607        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH B 533        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH C 337        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH C 524        DISTANCE =  5.43 ANGSTROMS                       
REMARK 525    HOH C 583        DISTANCE =  5.14 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 ASN C 132   OD1                                                    
REMARK 620 2 ASP C 145   OD2  87.2                                              
REMARK 620 3 ADP C 297   O2A  95.4  93.8                                        
REMARK 620 4 ADP C 297   O3B 169.6  95.2  74.4                                  
REMARK 620 5 HOH C 464   O    96.0 176.0  83.5  81.2                            
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 ASN A 132   OD1                                                    
REMARK 620 2 ADP A 297   O1A  94.3                                              
REMARK 620 3 ASP A 145   OD2  88.8  83.3                                        
REMARK 620 4 ADP A 297   O1B 176.5  82.2  91.4                                  
REMARK 620 5 HOH A 445   O    96.8  93.6 173.8  82.8                            
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 ASP C 145   OD1                                                    
REMARK 620 2 ASP C 145   OD2  57.4                                              
REMARK 620 3 ADP C 297   O1B  89.3  98.0                                        
REMARK 620 4 HOH C 731   O   113.0 170.4  80.0                                  
REMARK 620 5 HOH C 302   O    91.0  76.3 173.0 106.4                            
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 ADP A 297   O2B                                                    
REMARK 620 2 ASP A 145   OD1  92.0                                              
REMARK 620 3 ASP A 145   OD2  79.8  52.2                                        
REMARK 620 4 HOH A 730   O   105.6 108.5 160.6                                  
REMARK 620 5 HOH A 302   O   152.0  75.5  72.8 102.2                            
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 K   0   OG1                                                    
REMARK 620 2 MGF C 300   F1   82.3                                              
REMARK 620 3 MGF C 300   F2   97.0 120.6                                        
REMARK 620 4 MGF C 300   F3   89.5 116.9 122.5                                  
REMARK 620 5 ADP C 297   O3B 164.2  82.0  91.9  96.7                            
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 J   0   OG1                                                    
REMARK 620 2 MGF A 300   F1   90.4                                              
REMARK 620 3 MGF A 300   F2   91.7 122.8                                        
REMARK 620 4 MGF A 300   F3   86.3 115.4 121.8                                  
REMARK 620 5 ADP A 297   O1B 173.0  82.7  93.0  95.7                            
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 DTU B 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 297                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 298                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 299                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGF C 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTU D 4                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3QHR   RELATED DB: PDB                                   
REMARK 900 SAME COMPLEX AT PH 8.0                                               
DBREF  3QHW A    1   296  UNP    P24941   CDK2_HUMAN       1    296             
DBREF  3QHW B  173   432  UNP    P51943   CCNA2_MOUSE    163    422             
DBREF  3QHW C    1   296  UNP    P24941   CDK2_HUMAN       1    296             
DBREF  3QHW D  173   432  UNP    P51943   CCNA2_MOUSE    163    422             
DBREF  3QHW J   -2     7  PDB    3QHW     3QHW             1     10             
DBREF  3QHW K   -2     7  PDB    3QHW     3QHW             1     10             
DBREF  3QHW L   -2     7  PDB    3QHW     3QHW             1     10             
DBREF  3QHW M   -2     7  PDB    3QHW     3QHW             1     10             
SEQADV 3QHW GLY A   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 3QHW HIS A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 3QHW SER B  172  UNP  P51943              EXPRESSION TAG                 
SEQADV 3QHW GLY C   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 3QHW HIS C    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 3QHW 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 3QHW TPO A  160  THR  PHOSPHOTHREONINE                                   
MODRES 3QHW 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    DTU  B   3       8                                                       
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    DTU  D   4       8                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     MGF TRIFLUOROMAGNESATE                                               
HETNAM      CL CHLORIDE ION                                                     
HETNAM     DTU (2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL                            
HETSYN     TPO PHOSPHONOTHREONINE                                               
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  DTU    2(C4 H10 O2 S2)                                              
FORMUL  21  HOH   *793(H2 O)                                                    
HELIX    1   1 HIS A    0  GLU A    2  5                                   3    
HELIX    2   2 PRO A   45  LEU A   58  1                                  14    
HELIX    3   3 LEU A   87  ALA A   95  1                                   9    
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  ALA A  282  1                                   7    
HELIX   14  14 HIS A  283  GLN A  287  5                                   5    
HELIX   15  15 VAL B  175  CYS B  193  1                                  19    
HELIX   16  16 GLY B  198  GLN B  203  5                                   6    
HELIX   17  17 THR B  207  TYR B  225  1                                  19    
HELIX   18  18 GLN B  228  MET B  246  1                                  19    
HELIX   19  19 LEU B  249  GLY B  251  5                                   3    
HELIX   20  20 LYS B  252  GLU B  269  1                                  18    
HELIX   21  21 GLU B  274  THR B  282  1                                   9    
HELIX   22  22 SER B  287  LEU B  302  1                                  16    
HELIX   23  23 THR B  310  PHE B  319  1                                  10    
HELIX   24  24 LEU B  320  LEU B  322  5                                   3    
HELIX   25  25 ASN B  326  ASP B  343  1                                  18    
HELIX   26  26 ASP B  343  LEU B  348  1                                   6    
HELIX   27  27 LEU B  351  GLY B  369  1                                  19    
HELIX   28  28 PRO B  373  GLY B  381  1                                   9    
HELIX   29  29 THR B  383  ALA B  401  1                                  19    
HELIX   30  30 PRO B  402  HIS B  404  5                                   3    
HELIX   31  31 GLN B  407  TYR B  413  1                                   7    
HELIX   32  32 LYS B  414  HIS B  419  5                                   6    
HELIX   33  33 SER B  420  LEU B  424  5                                   5    
HELIX   34  34 HIS C    0  GLU C    2  5                                   3    
HELIX   35  35 PRO C   45  LEU C   58  1                                  14    
HELIX   36  36 LEU C   87  ALA C   95  1                                   9    
HELIX   37  37 PRO C  100  HIS C  121  1                                  22    
HELIX   38  38 LYS C  129  GLN C  131  5                                   3    
HELIX   39  39 ASP C  145  ALA C  149  5                                   5    
HELIX   40  40 THR C  165  ARG C  169  5                                   5    
HELIX   41  41 ALA C  170  LEU C  175  1                                   6    
HELIX   42  42 THR C  182  ARG C  199  1                                  18    
HELIX   43  43 SER C  207  GLY C  220  1                                  14    
HELIX   44  44 GLY C  229  MET C  233  5                                   5    
HELIX   45  45 ASP C  247  VAL C  252  1                                   6    
HELIX   46  46 ASP C  256  LEU C  267  1                                  12    
HELIX   47  47 SER C  276  ALA C  282  1                                   7    
HELIX   48  48 HIS C  283  GLN C  287  5                                   5    
HELIX   49  49 TYR D  178  CYS D  193  1                                  16    
HELIX   50  50 GLY D  198  GLN D  203  5                                   6    
HELIX   51  51 THR D  207  TYR D  225  1                                  19    
HELIX   52  52 GLN D  228  MET D  246  1                                  19    
HELIX   53  53 LEU D  249  GLY D  251  5                                   3    
HELIX   54  54 LYS D  252  GLU D  269  1                                  18    
HELIX   55  55 GLU D  274  THR D  282  1                                   9    
HELIX   56  56 SER D  287  LEU D  302  1                                  16    
HELIX   57  57 THR D  310  LEU D  320  1                                  11    
HELIX   58  58 ASN D  326  ASP D  343  1                                  18    
HELIX   59  59 ASP D  343  LEU D  348  1                                   6    
HELIX   60  60 LEU D  351  GLY D  369  1                                  19    
HELIX   61  61 PRO D  373  GLY D  381  1                                   9    
HELIX   62  62 THR D  383  ALA D  401  1                                  19    
HELIX   63  63 PRO D  402  HIS D  404  5                                   3    
HELIX   64  64 GLN D  407  TYR D  413  1                                   7    
HELIX   65  65 LYS D  414  HIS D  419  5                                   6    
HELIX   66  66 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  GLU A   8           
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  LEU A  76   N  ILE A  35           
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  LYS C  20   N  GLU C   8           
SHEET    3   D 5 VAL C  29  ARG C  36 -1  O  LEU C  32   N  TYR C  19           
SHEET    4   D 5 LYS C  75  GLU C  81 -1  O  LEU C  76   N  ILE C  35           
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  1.33  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.32  
LINK         C   TYR C 159                 N   TPO C 160     1555   1555  1.33  
LINK         C   TPO C 160                 N   HIS C 161     1555   1555  1.32  
LINK         S4  DTU B   3                 SG  CYS B 193     1555   1555  2.38  
LINK         S4  DTU D   4                 SG  CYS D 193     1555   1555  2.39  
LINK         OD1 ASN C 132                MG    MG C 298     1555   1555  1.93  
LINK         OD1 ASN A 132                MG    MG A 298     1555   1555  2.06  
LINK         O1A ADP A 297                MG    MG A 298     1555   1555  2.15  
LINK         OD2 ASP A 145                MG    MG A 298     1555   1555  2.16  
LINK         OD1 ASP C 145                MG    MG C 299     1555   1555  2.17  
LINK         O2B ADP A 297                MG    MG A 299     1555   1555  2.22  
LINK         OD2 ASP C 145                MG    MG C 298     1555   1555  2.24  
LINK         O2A ADP C 297                MG    MG C 298     1555   1555  2.26  
LINK         O3B ADP C 297                MG    MG C 298     1555   1555  2.35  
LINK         O1B ADP A 297                MG    MG A 298     1555   1555  2.36  
LINK         OD2 ASP C 145                MG    MG C 299     1555   1555  2.39  
LINK         OD1 ASP A 145                MG    MG A 299     1555   1555  2.42  
LINK         OG1 THR K   0                MG   MGF C 300     1555   1555  2.51  
LINK         O1B ADP C 297                MG    MG C 299     1555   1555  2.58  
LINK         OG1 THR J   0                MG   MGF A 300     1555   1555  2.58  
LINK         OD2 ASP A 145                MG    MG A 299     1555   1555  2.59  
LINK         O3B ADP C 297                MG   MGF C 300     1555   1555  2.61  
LINK         O1B ADP A 297                MG   MGF A 300     1555   1555  2.70  
LINK        MG    MG C 299                 O   HOH C 731     1555   1555  2.06  
LINK        MG    MG C 298                 O   HOH C 464     1555   1555  2.06  
LINK        MG    MG A 299                 O   HOH A 730     1555   1555  2.07  
LINK        MG    MG A 298                 O   HOH A 445     1555   1555  2.18  
LINK        MG    MG C 299                 O   HOH C 302     1555   1555  2.25  
LINK        MG    MG A 299                 O   HOH A 302     1555   1555  2.53  
CISPEP   1 VAL A  154    PRO A  155          0        -4.57                     
CISPEP   2 GLN B  323    PRO B  324          0        -6.00                     
CISPEP   3 ASP B  345    PRO B  346          0        -0.11                     
CISPEP   4 VAL C  154    PRO C  155          0         1.84                     
CISPEP   5 GLN D  323    PRO D  324          0        -6.52                     
CISPEP   6 ASP D  345    PRO D  346          0        -1.70                     
SITE     1 AC1 23 ILE A  10  GLY A  11  GLY A  13  TYR A  15                    
SITE     2 AC1 23 GLY A  16  VAL A  18  ALA A  31  LYS A  33                    
SITE     3 AC1 23 GLU A  81  LEU A  83  ASP A  86  LYS A  89                    
SITE     4 AC1 23 GLN A 131  ASN A 132  LEU A 134  ASP A 145                    
SITE     5 AC1 23  MG A 298   MG A 299  MGF A 300  HOH A 336                    
SITE     6 AC1 23 HOH A 348  HOH A 351  HOH A 445                               
SITE     1 AC2  5 ASN A 132  ASP A 145  ADP A 297  MGF A 300                    
SITE     2 AC2  5 HOH A 445                                                     
SITE     1 AC3  5 ASP A 145  ADP A 297  MGF A 300  HOH A 302                    
SITE     2 AC3  5 HOH A 730                                                     
SITE     1 AC4 13 GLY A  13  THR A  14  TYR A  15  ASP A 127                    
SITE     2 AC4 13 LYS A 129  ASN A 132  ASP A 145  ADP A 297                    
SITE     3 AC4 13  MG A 298   MG A 299  HOH A 302  HOH A 445                    
SITE     4 AC4 13 THR J   0                                                     
SITE     1 AC5  2 PRO A 130  GLN A 131                                          
SITE     1 AC6  5 MET B 189  CYS B 193  ARG B 241  ASP B 305                    
SITE     2 AC6  5 HOH B 444                                                     
SITE     1 AC7 23 ILE C  10  GLY C  13  TYR C  15  GLY C  16                    
SITE     2 AC7 23 VAL C  18  ALA C  31  LYS C  33  GLU C  81                    
SITE     3 AC7 23 LEU C  83  ASP C  86  LYS C  89  GLN C 131                    
SITE     4 AC7 23 ASN C 132  LEU C 134  ASP C 145   MG C 298                    
SITE     5 AC7 23  MG C 299  MGF C 300  HOH C 332  HOH C 346                    
SITE     6 AC7 23 HOH C 373  HOH C 464  HOH C 731                               
SITE     1 AC8  5 ASN C 132  ASP C 145  ADP C 297  MGF C 300                    
SITE     2 AC8  5 HOH C 464                                                     
SITE     1 AC9  5 ASP C 145  ADP C 297  MGF C 300  HOH C 302                    
SITE     2 AC9  5 HOH C 731                                                     
SITE     1 BC1 15 GLY C  13  THR C  14  TYR C  15  ASP C 127                    
SITE     2 BC1 15 LYS C 129  ASN C 132  ASP C 145  ADP C 297                    
SITE     3 BC1 15  MG C 298   MG C 299  HOH C 302  HOH C 464                    
SITE     4 BC1 15 HOH C 678  HOH C 731  THR K   0                               
SITE     1 BC2  3 PRO C 130  GLN C 131  HOH C 345                               
SITE     1 BC3  6 HOH D 139  MET D 189  CYS D 193  ARG D 241                    
SITE     2 BC3  6 ASP D 305  HOH D 443                                          
CRYST1   71.025  163.450   73.390  90.00 107.08  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      0.014080  0.000000  0.004326        0.00000                         
SCALE2      0.000000  0.006118  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014255        0.00000                         
MTRIX1   1  0.830725  0.014354  0.556498       26.94340    1                    
MTRIX2   1  0.014899 -0.999883  0.003551     -111.11600    1                    
MTRIX3   1  0.556484  0.005342 -0.830841      -85.30440    1                    
MTRIX1   2  0.830817  0.020690  0.556161       27.10060    1                    
MTRIX2   2  0.022324 -0.999743  0.003843     -110.92400    1                    
MTRIX3   2  0.556098  0.009222 -0.831066      -85.20060    1                    
MTRIX1   3  0.829614 -0.007753  0.558283       26.36950    1                    
MTRIX2   3 -0.008594 -0.999962 -0.001117     -111.71200    1                    
MTRIX3   3  0.558271 -0.003871 -0.829650      -85.39630    1                    
MTRIX1   4  0.824094  0.019955  0.566102       27.90960    1                    
MTRIX2   4  0.026147 -0.999654 -0.002826     -111.32200    1                    
MTRIX3   4  0.565849  0.017131 -0.824331      -84.24130    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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