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Database: PDB
Entry: 4I3Z
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HEADER    TRANSFERASE/CELL CYCLE                  27-NOV-12   4I3Z              
TITLE     STRUCTURE OF PCDK2/CYCLINA BOUND TO ADP AND 2 MAGNESIUM IONS          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 2;                                 
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: CELL DIVISION PROTEIN KINASE 2, P33 PROTEIN KINASE;         
COMPND   5 EC: 2.7.11.22;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CYCLIN-A2;                                                 
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: UNP RESIDUES 105-421;                                      
COMPND  11 SYNONYM: CYCLIN-A;                                                   
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CDK2, CDKN2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  13 ORGANISM_COMMON: MOUSE;                                              
SOURCE  14 ORGANISM_TAXID: 10090;                                               
SOURCE  15 GENE: CCNA, CCNA2, CYCA;                                             
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    ADP AND MAGNESIUM BINDING, T160 PHOSPHORYLATION, TRANSFERASE-CELL     
KEYWDS   2 CYCLE COMPLEX                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.M.JACOBSEN,Z.-Q.BAO,P.J.O'BRIEN,C.L.BROOKS,M.A.YOUNG                
REVDAT   2   15-NOV-17 4I3Z    1       REMARK                                   
REVDAT   1   26-DEC-12 4I3Z    0                                                
JRNL        AUTH   D.M.JACOBSEN,Z.-Q.BAO,P.J.O'BRIEN,C.L.BROOKS,M.A.YOUNG       
JRNL        TITL   PRICE TO BE PAID FOR TWO-METAL CATALYSIS: MAGNESIUM IONS     
JRNL        TITL 2 THAT ACCELERATE CHEMISTRY UNAVOIDABLY LIMIT PRODUCT RELEASE  
JRNL        TITL 3 FROM A PROTEIN KINASE                                        
JRNL        REF    J.AM.CHEM.SOC.                V. 134 15357 2012              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   22891849                                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.79                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 98383                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4895                            
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 42.7995 -  6.3631    0.99     3190   187  0.2068 0.2222        
REMARK   3     2  6.3631 -  5.0532    1.00     3183   160  0.2005 0.2193        
REMARK   3     3  5.0532 -  4.4152    1.00     3188   155  0.1632 0.1824        
REMARK   3     4  4.4152 -  4.0118    1.00     3174   165  0.1654 0.1833        
REMARK   3     5  4.0118 -  3.7244    1.00     3185   139  0.1681 0.1921        
REMARK   3     6  3.7244 -  3.5049    1.00     3179   155  0.1686 0.1852        
REMARK   3     7  3.5049 -  3.3295    1.00     3158   178  0.1631 0.2002        
REMARK   3     8  3.3295 -  3.1846    1.00     3146   185  0.1748 0.2387        
REMARK   3     9  3.1846 -  3.0620    1.00     3127   193  0.1728 0.2188        
REMARK   3    10  3.0620 -  2.9564    1.00     3161   164  0.1740 0.1978        
REMARK   3    11  2.9564 -  2.8640    1.00     3176   170  0.1765 0.2071        
REMARK   3    12  2.8640 -  2.7821    1.00     3170   170  0.1765 0.2226        
REMARK   3    13  2.7821 -  2.7089    1.00     3114   164  0.1783 0.2280        
REMARK   3    14  2.7089 -  2.6428    0.99     3133   172  0.1904 0.2258        
REMARK   3    15  2.6428 -  2.5828    0.99     3156   163  0.2014 0.2556        
REMARK   3    16  2.5828 -  2.5278    0.99     3116   139  0.2021 0.2310        
REMARK   3    17  2.5278 -  2.4772    0.98     3128   171  0.2149 0.2758        
REMARK   3    18  2.4772 -  2.4305    0.98     3050   178  0.2236 0.2900        
REMARK   3    19  2.4305 -  2.3871    0.97     3054   157  0.2171 0.2514        
REMARK   3    20  2.3871 -  2.3466    0.97     3084   145  0.2251 0.2773        
REMARK   3    21  2.3466 -  2.3088    0.97     3030   178  0.2288 0.2580        
REMARK   3    22  2.3088 -  2.2733    0.97     3042   178  0.2450 0.2874        
REMARK   3    23  2.2733 -  2.2398    0.97     3065   159  0.2533 0.2824        
REMARK   3    24  2.2398 -  2.2083    0.97     3067   152  0.2681 0.3015        
REMARK   3    25  2.2083 -  2.1784    0.97     3082   163  0.2759 0.2935        
REMARK   3    26  2.1784 -  2.1502    0.97     3020   147  0.2713 0.2985        
REMARK   3    27  2.1502 -  2.1233    0.97     3099   157  0.2899 0.3113        
REMARK   3    28  2.1233 -  2.0977    0.97     3039   142  0.2998 0.2937        
REMARK   3    29  2.0977 -  2.0733    0.97     3080   154  0.3151 0.3312        
REMARK   3    30  2.0733 -  2.0500    0.97     3092   155  0.3341 0.3578        
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              : 0.40                                          
REMARK   3   B_SOL              : 59.54                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.680           
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) : 12.19110                                             
REMARK   3    B22 (A**2) : -7.88620                                             
REMARK   3    B33 (A**2) : -4.30490                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 7.72940                                              
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      :  0.008           9229                                  
REMARK   3   ANGLE     :  0.887          12535                                  
REMARK   3   CHIRALITY :  0.061           1414                                  
REMARK   3   PLANARITY :  0.004           1564                                  
REMARK   3   DIHEDRAL  : 14.949           3434                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 26                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 1:23)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.1249 -48.7782  -4.1773              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2623 T22:   0.1429                                     
REMARK   3      T33:   0.5490 T12:   0.0259                                     
REMARK   3      T13:   0.1213 T23:  -0.0010                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8906 L22:   2.9723                                     
REMARK   3      L33:   1.5729 L12:  -0.8477                                     
REMARK   3      L13:   0.8389 L23:  -1.3270                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4516 S12:  -0.0595 S13:  -0.1194                       
REMARK   3      S21:  -0.4725 S22:   0.0656 S23:   0.1093                       
REMARK   3      S31:  -0.0258 S32:  -0.0040 S33:   0.1051                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 24:45)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0158 -46.7445 -10.9981              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2001 T22:   0.2058                                     
REMARK   3      T33:   0.2791 T12:   0.0573                                     
REMARK   3      T13:   0.0171 T23:   0.0381                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1063 L22:   0.1928                                     
REMARK   3      L33:   0.2608 L12:   0.1405                                     
REMARK   3      L13:  -0.0300 L23:  -0.0464                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1701 S12:   0.1331 S13:   0.0092                       
REMARK   3      S21:   0.0477 S22:   0.1088 S23:   0.2288                       
REMARK   3      S31:  -0.0590 S32:  -0.0529 S33:  -0.1531                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 46:158)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.1942 -38.7653   0.9224              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1807 T22:   0.1460                                     
REMARK   3      T33:   0.1554 T12:   0.0151                                     
REMARK   3      T13:   0.0195 T23:  -0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6697 L22:   0.8568                                     
REMARK   3      L33:   0.7179 L12:  -0.2227                                     
REMARK   3      L13:   0.2119 L23:   0.1422                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0621 S12:  -0.0313 S13:  -0.0492                       
REMARK   3      S21:   0.0323 S22:   0.0348 S23:   0.0877                       
REMARK   3      S31:   0.1450 S32:   0.1343 S33:   0.0246                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 159:198)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  11.2184 -23.1122  -0.0241              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2208 T22:   0.1789                                     
REMARK   3      T33:   0.2017 T12:   0.0124                                     
REMARK   3      T13:  -0.0030 T23:  -0.0003                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4295 L22:   0.6714                                     
REMARK   3      L33:   0.2494 L12:  -0.2381                                     
REMARK   3      L13:  -0.2564 L23:  -0.1272                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0059 S12:   0.0718 S13:   0.0068                       
REMARK   3      S21:  -0.3213 S22:  -0.0958 S23:   0.0590                       
REMARK   3      S31:   0.0527 S32:   0.1037 S33:  -0.0222                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 199:219)                         
REMARK   3    ORIGIN FOR THE GROUP (A):   3.9870 -15.4944   6.3919              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0252 T22:   0.2093                                     
REMARK   3      T33:   0.3750 T12:  -0.0122                                     
REMARK   3      T13:  -0.0090 T23:  -0.0245                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0992 L22:   0.2934                                     
REMARK   3      L33:   0.1363 L12:   0.0866                                     
REMARK   3      L13:   0.0681 L23:  -0.0576                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0539 S12:  -0.0772 S13:   0.1283                       
REMARK   3      S21:   0.0294 S22:  -0.0571 S23:   0.3126                       
REMARK   3      S31:  -0.0186 S32:   0.1119 S33:   0.0143                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 220:266)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  14.6260 -12.6986   8.7483              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2033 T22:   0.2147                                     
REMARK   3      T33:   0.3056 T12:  -0.0258                                     
REMARK   3      T13:   0.0351 T23:  -0.0655                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1973 L22:   0.3738                                     
REMARK   3      L33:   0.5296 L12:  -0.2586                                     
REMARK   3      L13:  -0.0991 L23:   0.0997                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0296 S12:  -0.3610 S13:   0.5269                       
REMARK   3      S21:   0.2362 S22:   0.0683 S23:  -0.1799                       
REMARK   3      S31:  -0.1257 S32:   0.1548 S33:  -0.0282                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 267:296)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  18.8053 -29.5058  12.5171              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2285 T22:   0.3062                                     
REMARK   3      T33:   0.1683 T12:   0.0315                                     
REMARK   3      T13:  -0.0146 T23:  -0.0161                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5189 L22:   0.4581                                     
REMARK   3      L33:   0.2559 L12:  -0.2612                                     
REMARK   3      L13:  -0.0989 L23:   0.2894                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1207 S12:  -0.1896 S13:   0.1461                       
REMARK   3      S21:   0.3286 S22:   0.0804 S23:  -0.0963                       
REMARK   3      S31:   0.2216 S32:   0.1275 S33:  -0.0365                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 175:192)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  29.8482 -37.3734  -6.6848              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2597 T22:   0.3904                                     
REMARK   3      T33:   0.1945 T12:  -0.0023                                     
REMARK   3      T13:   0.0765 T23:  -0.0768                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1409 L22:   0.9730                                     
REMARK   3      L33:   0.3550 L12:  -0.0916                                     
REMARK   3      L13:  -0.0114 L23:  -0.1780                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0919 S12:  -0.4158 S13:   0.0128                       
REMARK   3      S21:  -0.0291 S22:  -0.3498 S23:   0.2046                       
REMARK   3      S31:   0.1733 S32:   0.6014 S33:   0.0384                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 193:207)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  27.1645 -51.5408 -30.2240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4319 T22:   0.3164                                     
REMARK   3      T33:   0.3117 T12:   0.0652                                     
REMARK   3      T13:   0.0655 T23:  -0.0486                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4194 L22:   0.5171                                     
REMARK   3      L33:   0.0254 L12:  -0.2285                                     
REMARK   3      L13:  -0.0790 L23:  -0.0218                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0208 S12:  -0.0994 S13:   0.0493                       
REMARK   3      S21:  -0.1965 S22:   0.1511 S23:  -0.1674                       
REMARK   3      S31:  -0.1562 S32:   0.2112 S33:  -0.0396                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 208:268)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  19.1756 -39.1516 -29.3672              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2729 T22:   0.1360                                     
REMARK   3      T33:   0.1111 T12:  -0.0133                                     
REMARK   3      T13:   0.0236 T23:  -0.0050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2280 L22:   0.2969                                     
REMARK   3      L33:   0.5226 L12:  -0.0023                                     
REMARK   3      L13:   0.2779 L23:   0.0520                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0232 S12:   0.0193 S13:   0.0146                       
REMARK   3      S21:  -0.3712 S22:   0.1022 S23:  -0.0896                       
REMARK   3      S31:  -0.2795 S32:   0.1880 S33:  -0.0303                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 269:310)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  10.1472 -39.8471 -26.9653              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3018 T22:   0.1708                                     
REMARK   3      T33:   0.1866 T12:   0.0204                                     
REMARK   3      T13:  -0.0595 T23:   0.0056                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4773 L22:   0.6419                                     
REMARK   3      L33:   0.1323 L12:  -0.0090                                     
REMARK   3      L13:  -0.1066 L23:   0.0530                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0502 S12:  -0.0983 S13:  -0.0729                       
REMARK   3      S21:  -0.3794 S22:   0.0218 S23:   0.0841                       
REMARK   3      S31:  -0.0247 S32:  -0.1086 S33:  -0.0144                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 311:399)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  38.7849 -31.5451 -21.2347              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2329 T22:   0.4662                                     
REMARK   3      T33:   0.2052 T12:  -0.0723                                     
REMARK   3      T13:   0.0960 T23:  -0.1033                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3133 L22:   0.2849                                     
REMARK   3      L33:   0.4467 L12:  -0.1392                                     
REMARK   3      L13:  -0.0036 L23:  -0.0425                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2564 S12:  -0.0044 S13:  -0.0031                       
REMARK   3      S21:  -0.1745 S22:   0.2874 S23:  -0.0419                       
REMARK   3      S31:  -0.2340 S32:   0.7144 S33:  -0.1521                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 400:431)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  34.8192 -25.5295 -34.0492              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5144 T22:   0.3921                                     
REMARK   3      T33:   0.2177 T12:  -0.1861                                     
REMARK   3      T13:   0.1457 T23:  -0.0564                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0666 L22:   0.4057                                     
REMARK   3      L33:   0.1859 L12:   0.1523                                     
REMARK   3      L13:  -0.0070 L23:  -0.1340                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2402 S12:   0.3381 S13:   0.0293                       
REMARK   3      S21:  -0.3561 S22:   0.2161 S23:  -0.0768                       
REMARK   3      S31:  -0.2530 S32:   0.4770 S33:  -0.1595                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 1:23)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  16.3462  15.8173 -36.1487              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6929 T22:   0.1484                                     
REMARK   3      T33:   0.3269 T12:   0.0092                                     
REMARK   3      T13:  -0.1764 T23:   0.0272                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1745 L22:   0.5732                                     
REMARK   3      L33:   0.3329 L12:  -0.7675                                     
REMARK   3      L13:  -0.4790 L23:   0.2276                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1159 S12:  -0.0863 S13:   0.2268                       
REMARK   3      S21:  -0.2570 S22:   0.0429 S23:  -0.3330                       
REMARK   3      S31:   0.3287 S32:  -0.0370 S33:   0.0151                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 24:45)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  16.6612  13.8463 -44.1277              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3012 T22:   0.1848                                     
REMARK   3      T33:   0.2492 T12:   0.0574                                     
REMARK   3      T13:  -0.0908 T23:   0.0302                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1075 L22:   0.3193                                     
REMARK   3      L33:   0.0100 L12:   0.1980                                     
REMARK   3      L13:  -0.0366 L23:  -0.0590                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0786 S12:   0.0464 S13:   0.0950                       
REMARK   3      S21:   0.2911 S22:  -0.0974 S23:  -0.1164                       
REMARK   3      S31:   0.0794 S32:   0.0162 S33:   0.0161                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 46:158)                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.4229   6.1143 -39.9729              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3148 T22:   0.1355                                     
REMARK   3      T33:   0.1175 T12:   0.0015                                     
REMARK   3      T13:  -0.0116 T23:   0.0102                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7414 L22:   0.6692                                     
REMARK   3      L33:   0.4318 L12:   0.1913                                     
REMARK   3      L13:   0.0083 L23:  -0.1644                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0271 S12:  -0.0341 S13:   0.0101                       
REMARK   3      S21:   0.3535 S22:   0.0217 S23:   0.0188                       
REMARK   3      S31:  -0.1773 S32:  -0.0847 S33:  -0.0115                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 159:198)                         
REMARK   3    ORIGIN FOR THE GROUP (A):   0.7911  -9.5292 -41.4764              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3653 T22:   0.1912                                     
REMARK   3      T33:   0.2395 T12:   0.0164                                     
REMARK   3      T13:   0.0528 T23:   0.0171                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1350 L22:   0.5328                                     
REMARK   3      L33:   0.1110 L12:  -0.1843                                     
REMARK   3      L13:   0.1450 L23:  -0.1332                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0665 S12:   0.0670 S13:   0.0225                       
REMARK   3      S21:   0.1365 S22:  -0.0808 S23:  -0.2914                       
REMARK   3      S31:  -0.1426 S32:   0.0638 S33:   0.0020                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 199:219)                         
REMARK   3    ORIGIN FOR THE GROUP (A):   3.0891 -17.2674 -32.1850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4376 T22:   0.1929                                     
REMARK   3      T33:   0.2969 T12:   0.0180                                     
REMARK   3      T13:  -0.0321 T23:   0.0060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2167 L22:   0.4997                                     
REMARK   3      L33:   0.0542 L12:   0.2177                                     
REMARK   3      L13:   0.0608 L23:  -0.0411                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0441 S12:  -0.1061 S13:  -0.0854                       
REMARK   3      S21:   0.3695 S22:   0.0010 S23:  -0.3583                       
REMARK   3      S31:   0.0395 S32:  -0.0246 S33:   0.0091                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 220:266)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.1219 -19.8477 -36.1477              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4756 T22:   0.2170                                     
REMARK   3      T33:   0.2702 T12:  -0.0269                                     
REMARK   3      T13:   0.0957 T23:   0.0586                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7408 L22:   0.0323                                     
REMARK   3      L33:   0.4124 L12:  -0.0797                                     
REMARK   3      L13:   0.2822 L23:  -0.0008                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0859 S12:  -0.1564 S13:  -0.4265                       
REMARK   3      S21:   0.3769 S22:   0.0605 S23:   0.2991                       
REMARK   3      S31:   0.3530 S32:  -0.1182 S33:   0.0561                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 267:296)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -12.3638  -2.9341 -35.2118              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3906 T22:   0.2663                                     
REMARK   3      T33:   0.2487 T12:   0.0114                                     
REMARK   3      T13:   0.1343 T23:   0.0138                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2304 L22:   0.3586                                     
REMARK   3      L33:   0.4248 L12:  -0.1018                                     
REMARK   3      L13:   0.0881 L23:   0.1671                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0987 S12:  -0.0943 S13:   0.0306                       
REMARK   3      S21:   0.4725 S22:   0.0332 S23:   0.2732                       
REMARK   3      S31:   0.0058 S32:  -0.1118 S33:  -0.0017                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 175:192)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -10.7312   5.3445 -57.2539              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1736 T22:   0.2427                                     
REMARK   3      T33:   0.1653 T12:  -0.0484                                     
REMARK   3      T13:   0.0693 T23:   0.0448                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0907 L22:   0.3020                                     
REMARK   3      L33:   0.7937 L12:   0.0686                                     
REMARK   3      L13:  -0.0670 L23:  -0.3949                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0056 S12:  -0.3475 S13:  -0.0301                       
REMARK   3      S21:   0.3020 S22:  -0.1810 S23:   0.0874                       
REMARK   3      S31:  -0.1728 S32:  -0.2143 S33:  -0.0531                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 193:207)                         
REMARK   3    ORIGIN FOR THE GROUP (A):   4.9719  19.3057 -75.1733              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2955 T22:   0.2288                                     
REMARK   3      T33:   0.2757 T12:  -0.0256                                     
REMARK   3      T13:  -0.0312 T23:   0.0448                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4020 L22:   0.7143                                     
REMARK   3      L33:   0.2146 L12:  -0.3929                                     
REMARK   3      L13:   0.2702 L23:  -0.1499                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1192 S12:   0.0979 S13:  -0.0499                       
REMARK   3      S21:  -0.4165 S22:   0.1280 S23:   0.0872                       
REMARK   3      S31:   0.1737 S32:  -0.2284 S33:  -0.0111                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 208:287)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  13.2586   5.2271 -69.1061              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1192 T22:   0.1682                                     
REMARK   3      T33:   0.2100 T12:  -0.0095                                     
REMARK   3      T13:   0.0080 T23:  -0.0030                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4196 L22:   0.3725                                     
REMARK   3      L33:   0.2205 L12:   0.0017                                     
REMARK   3      L13:  -0.3055 L23:   0.0017                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1524 S12:   0.0014 S13:  -0.0490                       
REMARK   3      S21:  -0.2711 S22:   0.0572 S23:  -0.1780                       
REMARK   3      S31:   0.2186 S32:  -0.1287 S33:  -0.0213                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 288:310)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  13.5788  12.7006 -60.6431              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1170 T22:   0.1909                                     
REMARK   3      T33:   0.2426 T12:  -0.0172                                     
REMARK   3      T13:  -0.0347 T23:  -0.0292                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0434 L22:   0.1736                                     
REMARK   3      L33:   0.1572 L12:  -0.0601                                     
REMARK   3      L13:  -0.0629 L23:   0.0011                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0673 S12:  -0.1012 S13:   0.0571                       
REMARK   3      S21:  -0.0263 S22:   0.0345 S23:  -0.1146                       
REMARK   3      S31:  -0.1250 S32:  -0.0403 S33:   0.0167                       
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 311:399)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -10.2314  -0.2389 -74.4087              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0229 T22:   0.2652                                     
REMARK   3      T33:   0.1700 T12:  -0.1614                                     
REMARK   3      T13:  -0.1073 T23:  -0.0031                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1830 L22:   0.3018                                     
REMARK   3      L33:   0.2232 L12:  -0.2004                                     
REMARK   3      L13:  -0.1280 L23:   0.2639                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1202 S12:   0.2963 S13:  -0.0390                       
REMARK   3      S21:  -0.1918 S22:   0.1072 S23:   0.1383                       
REMARK   3      S31:   0.0103 S32:   0.0504 S33:  -0.0137                       
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 400:431)                         
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0156  -6.4740 -82.9120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3465 T22:   0.2911                                     
REMARK   3      T33:   0.1220 T12:  -0.1217                                     
REMARK   3      T13:   0.0654 T23:  -0.0869                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3303 L22:   0.9552                                     
REMARK   3      L33:   0.3578 L12:   0.5586                                     
REMARK   3      L13:   0.1850 L23:   0.2900                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2142 S12:   0.3704 S13:  -0.4099                       
REMARK   3      S21:   0.0061 S22:   0.1435 S23:  -0.3195                       
REMARK   3      S31:  -0.0461 S32:  -0.0317 S33:  -0.0469                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 2                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 1:296 )                 
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 1:296 )                 
REMARK   3     ATOM PAIRS NUMBER  : 2382                                        
REMARK   3     RMSD               : 0.046                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN B AND (RESSEQ 175:431 )               
REMARK   3     SELECTION          : CHAIN D AND (RESSEQ 175:431 )               
REMARK   3     ATOM PAIRS NUMBER  : 2069                                        
REMARK   3     RMSD               : 0.077                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4I3Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-NOV-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000076274.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-MAR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-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   : 98449                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.120                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.85700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% W/V POLYACRYLIC ACID SODIUM SALT     
REMARK 280  5100, 20MM MGCL2, 100MM HEPES PH 7.5, VAPOR DIFFUSION, SITTING      
REMARK 280  DROP, TEMPERATURE 293.15K                                           
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       82.06500            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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       39.30   -144.03                                   
REMARK 500    ASP A 145       75.44     52.97                                   
REMARK 500    VAL A 163      -96.25   -122.11                                   
REMARK 500    SER A 181     -145.30   -144.68                                   
REMARK 500    ASP A 256     -179.64    -69.81                                   
REMARK 500    ASP C 127       38.95   -144.15                                   
REMARK 500    ASP C 145       79.19     51.64                                   
REMARK 500    VAL C 163      -96.18   -120.52                                   
REMARK 500    SER C 181     -145.17   -147.36                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A 301   O3B                                                    
REMARK 620 2 ADP A 301   O1A  80.1                                              
REMARK 620 3 ASN A 132   OD1 170.7  90.6                                        
REMARK 620 4 ASP A 145   OD2  95.1  90.6  85.3                                  
REMARK 620 5 HOH A 402   O   101.3 166.8  87.9  76.2                            
REMARK 620 6 HOH A 401   O    89.9  88.8  89.5 174.8 104.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP C 301   O3B                                                    
REMARK 620 2 ADP C 301   O1A  81.2                                              
REMARK 620 3 ASN C 132   OD1 169.5  88.8                                        
REMARK 620 4 ASP C 145   OD2  92.3  88.2  84.0                                  
REMARK 620 5 HOH C 402   O    99.0 168.6  90.1  80.4                            
REMARK 620 6 HOH C 401   O    90.8  89.5  92.4 175.8 101.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 303  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A 301   O2B                                                    
REMARK 620 2 ASP A 145   OD1  86.6                                              
REMARK 620 3 ASP A 145   OD2  87.0  51.0                                        
REMARK 620 4 HOH A 404   O    82.9 118.2 165.9                                  
REMARK 620 5 HOH A 403   O    93.6 151.0 100.0  90.6                            
REMARK 620 6 HOH A 413   O   155.1  70.8  70.9 116.5 101.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 303  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP C 301   O2B                                                    
REMARK 620 2 ASP C 145   OD2  80.5                                              
REMARK 620 3 ASP C 145   OD1  80.1  50.5                                        
REMARK 620 4 HOH C 403   O    90.0 104.8 154.4                                  
REMARK 620 5 HOH C 404   O    68.7 148.6 115.3  82.1                            
REMARK 620 6 HOH C 410   O   122.6 138.4  96.3 108.9  61.5                      
REMARK 620 7 HOH C 406   O   141.7  70.7  62.2 121.1 132.3  71.2                
REMARK 620 N                    1     2     3     4     5     6                 
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 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 307                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 503                 
DBREF  4I3Z A    1   296  UNP    P24941   CDK2_HUMAN       1    296             
DBREF  4I3Z B  175   431  UNP    P51943   CCNA2_MOUSE    165    421             
DBREF  4I3Z C    1   296  UNP    P24941   CDK2_HUMAN       1    296             
DBREF  4I3Z D  175   431  UNP    P51943   CCNA2_MOUSE    165    421             
SEQRES   1 A  296  MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY          
SEQRES   2 A  296  THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR          
SEQRES   3 A  296  GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR          
SEQRES   4 A  296  GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 A  296  SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS          
SEQRES   6 A  296  LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU          
SEQRES   7 A  296  VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET          
SEQRES   8 A  296  ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE          
SEQRES   9 A  296  LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE          
SEQRES  10 A  296  CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  11 A  296  GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU          
SEQRES  12 A  296  ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL          
SEQRES  13 A  296  ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP TYR ARG          
SEQRES  14 A  296  ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR          
SEQRES  15 A  296  ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU          
SEQRES  16 A  296  MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU          
SEQRES  17 A  296  ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR          
SEQRES  18 A  296  PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO          
SEQRES  19 A  296  ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP          
SEQRES  20 A  296  PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG          
SEQRES  21 A  296  SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS          
SEQRES  22 A  296  ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE          
SEQRES  23 A  296  GLN ASP VAL THR LYS PRO VAL PRO HIS LEU                      
SEQRES   1 B  257  VAL PRO ASP TYR GLN GLU ASP ILE HIS THR TYR LEU ARG          
SEQRES   2 B  257  GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET          
SEQRES   3 B  257  LYS ARG GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE          
SEQRES   4 B  257  LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS          
SEQRES   5 B  257  LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE          
SEQRES   6 B  257  ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS          
SEQRES   7 B  257  LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER          
SEQRES   8 B  257  LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE          
SEQRES   9 B  257  VAL TYR ILE THR ASP ASP THR TYR SER LYS LYS GLN VAL          
SEQRES  10 B  257  LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU ALA PHE          
SEQRES  11 B  257  ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN          
SEQRES  12 B  257  TYR PHE LEU HIS LEU GLN PRO ALA ASN CYS LYS VAL GLU          
SEQRES  13 B  257  SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP          
SEQRES  14 B  257  ALA ASP PRO TYR LEU LYS TYR LEU PRO SER LEU ILE ALA          
SEQRES  15 B  257  GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY          
SEQRES  16 B  257  GLN SER TRP PRO GLU SER LEU ALA GLN GLN THR GLY TYR          
SEQRES  17 B  257  THR LEU GLU SER LEU LYS PRO CYS LEU VAL ASP LEU HIS          
SEQRES  18 B  257  GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER          
SEQRES  19 B  257  ILE ARG GLU LYS TYR LYS HIS SER LYS TYR HIS SER VAL          
SEQRES  20 B  257  SER LEU LEU ASN PRO PRO GLU THR LEU SER                      
SEQRES   1 C  296  MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY          
SEQRES   2 C  296  THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR          
SEQRES   3 C  296  GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR          
SEQRES   4 C  296  GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 C  296  SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS          
SEQRES   6 C  296  LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU          
SEQRES   7 C  296  VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET          
SEQRES   8 C  296  ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE          
SEQRES   9 C  296  LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE          
SEQRES  10 C  296  CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  11 C  296  GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU          
SEQRES  12 C  296  ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL          
SEQRES  13 C  296  ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP TYR ARG          
SEQRES  14 C  296  ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR          
SEQRES  15 C  296  ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU          
SEQRES  16 C  296  MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU          
SEQRES  17 C  296  ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR          
SEQRES  18 C  296  PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO          
SEQRES  19 C  296  ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP          
SEQRES  20 C  296  PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG          
SEQRES  21 C  296  SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS          
SEQRES  22 C  296  ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE          
SEQRES  23 C  296  GLN ASP VAL THR LYS PRO VAL PRO HIS LEU                      
SEQRES   1 D  257  VAL PRO ASP TYR GLN GLU ASP ILE HIS THR TYR LEU ARG          
SEQRES   2 D  257  GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET          
SEQRES   3 D  257  LYS ARG GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE          
SEQRES   4 D  257  LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS          
SEQRES   5 D  257  LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE          
SEQRES   6 D  257  ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS          
SEQRES   7 D  257  LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER          
SEQRES   8 D  257  LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE          
SEQRES   9 D  257  VAL TYR ILE THR ASP ASP THR TYR SER LYS LYS GLN VAL          
SEQRES  10 D  257  LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU ALA PHE          
SEQRES  11 D  257  ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN          
SEQRES  12 D  257  TYR PHE LEU HIS LEU GLN PRO ALA ASN CYS LYS VAL GLU          
SEQRES  13 D  257  SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP          
SEQRES  14 D  257  ALA ASP PRO TYR LEU LYS TYR LEU PRO SER LEU ILE ALA          
SEQRES  15 D  257  GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY          
SEQRES  16 D  257  GLN SER TRP PRO GLU SER LEU ALA GLN GLN THR GLY TYR          
SEQRES  17 D  257  THR LEU GLU SER LEU LYS PRO CYS LEU VAL ASP LEU HIS          
SEQRES  18 D  257  GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER          
SEQRES  19 D  257  ILE ARG GLU LYS TYR LYS HIS SER LYS TYR HIS SER VAL          
SEQRES  20 D  257  SER LEU LEU ASN PRO PRO GLU THR LEU SER                      
MODRES 4I3Z TPO A  160  THR  PHOSPHOTHREONINE                                   
MODRES 4I3Z TPO C  160  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET    ADP  A 301      27                                                       
HET     MG  A 302       1                                                       
HET     MG  A 303       1                                                       
HET    GOL  A 304       6                                                       
HET    GOL  A 305       6                                                       
HET    GOL  A 306       6                                                       
HET     CL  A 307       1                                                       
HET    GOL  B 501       6                                                       
HET    GOL  B 502       6                                                       
HET    ADP  C 301      27                                                       
HET     MG  C 302       1                                                       
HET     MG  C 303       1                                                       
HET    GOL  C 304       6                                                       
HET     CL  C 305       1                                                       
HET    GOL  D 501       6                                                       
HET    GOL  D 502       6                                                       
HET    GOL  D 503       6                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GOL GLYCEROL                                                         
HETNAM      CL CHLORIDE ION                                                     
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   5  ADP    2(C10 H15 N5 O10 P2)                                         
FORMUL   6   MG    4(MG 2+)                                                     
FORMUL   8  GOL    9(C3 H8 O3)                                                  
FORMUL  11   CL    2(CL 1-)                                                     
FORMUL  22  HOH   *521(H2 O)                                                    
HELIX    1   1 PRO A   45  LEU A   58  1                                  14    
HELIX    2   2 LEU A   87  SER A   94  1                                   8    
HELIX    3   3 PRO A  100  HIS A  121  1                                  22    
HELIX    4   4 LYS A  129  GLN A  131  5                                   3    
HELIX    5   5 THR A  165  ARG A  169  5                                   5    
HELIX    6   6 ALA A  170  LEU A  175  1                                   6    
HELIX    7   7 THR A  182  ARG A  199  1                                  18    
HELIX    8   8 SER A  207  GLY A  220  1                                  14    
HELIX    9   9 GLY A  229  MET A  233  5                                   5    
HELIX   10  10 ASP A  247  VAL A  252  1                                   6    
HELIX   11  11 ASP A  256  LEU A  267  1                                  12    
HELIX   12  12 SER A  276  ALA A  282  1                                   7    
HELIX   13  13 HIS A  283  GLN A  287  5                                   5    
HELIX   14  14 PRO B  176  CYS B  193  1                                  18    
HELIX   15  15 GLY B  198  GLN B  203  5                                   6    
HELIX   16  16 THR B  207  TYR B  225  1                                  19    
HELIX   17  17 GLN B  228  SER B  244  1                                  17    
HELIX   18  18 LYS B  252  GLU B  269  1                                  18    
HELIX   19  19 GLU B  274  THR B  282  1                                   9    
HELIX   20  20 SER B  287  ALA B  303  1                                  17    
HELIX   21  21 THR B  310  LEU B  320  1                                  11    
HELIX   22  22 ASN B  326  ASP B  343  1                                  18    
HELIX   23  23 ASP B  343  LEU B  348  1                                   6    
HELIX   24  24 LEU B  351  GLY B  369  1                                  19    
HELIX   25  25 PRO B  373  GLY B  381  1                                   9    
HELIX   26  26 THR B  383  LYS B  400  1                                  18    
HELIX   27  27 ALA B  401  HIS B  404  5                                   4    
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 PRO C   45  LEU C   58  1                                  14    
HELIX   32  32 LEU C   87  SER C   94  1                                   8    
HELIX   33  33 PRO C  100  HIS C  121  1                                  22    
HELIX   34  34 LYS C  129  GLN C  131  5                                   3    
HELIX   35  35 THR C  165  ARG C  169  5                                   5    
HELIX   36  36 ALA C  170  LEU C  175  1                                   6    
HELIX   37  37 THR C  182  ARG C  199  1                                  18    
HELIX   38  38 SER C  207  GLY C  220  1                                  14    
HELIX   39  39 GLY C  229  MET C  233  5                                   5    
HELIX   40  40 ASP C  247  VAL C  252  1                                   6    
HELIX   41  41 ASP C  256  LEU C  267  1                                  12    
HELIX   42  42 SER C  276  ALA C  282  1                                   7    
HELIX   43  43 HIS C  283  GLN C  287  5                                   5    
HELIX   44  44 PRO D  176  CYS D  193  1                                  18    
HELIX   45  45 GLY D  198  GLN D  203  5                                   6    
HELIX   46  46 THR D  207  TYR D  225  1                                  19    
HELIX   47  47 GLN D  228  SER D  244  1                                  17    
HELIX   48  48 LYS D  252  GLU D  269  1                                  18    
HELIX   49  49 GLU D  274  THR D  282  1                                   9    
HELIX   50  50 SER D  287  ALA D  303  1                                  17    
HELIX   51  51 THR D  310  LEU D  320  1                                  11    
HELIX   52  52 ASN D  326  SER D  340  1                                  15    
HELIX   53  53 ASP D  343  LEU D  348  1                                   6    
HELIX   54  54 LEU D  351  GLY D  369  1                                  19    
HELIX   55  55 PRO D  373  GLY D  381  1                                   9    
HELIX   56  56 THR D  383  LYS D  400  1                                  18    
HELIX   57  57 ALA D  401  HIS D  404  5                                   4    
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 GLY A  16  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  78   N  LYS A  33           
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 GLY C  16  ASN C  23 -1  O  LYS C  20   N  GLU C   8           
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  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  1.33  
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         O3B ADP A 301                MG    MG A 302     1555   1555  1.97  
LINK         O3B ADP C 301                MG    MG C 302     1555   1555  2.00  
LINK         O1A ADP A 301                MG    MG A 302     1555   1555  2.01  
LINK         O1A ADP C 301                MG    MG C 302     1555   1555  2.04  
LINK         O2B ADP A 301                MG    MG A 303     1555   1555  2.10  
LINK         OD1 ASN C 132                MG    MG C 302     1555   1555  2.13  
LINK         OD1 ASN A 132                MG    MG A 302     1555   1555  2.13  
LINK         OD2 ASP A 145                MG    MG A 302     1555   1555  2.14  
LINK         OD2 ASP C 145                MG    MG C 302     1555   1555  2.17  
LINK         O2B ADP C 301                MG    MG C 303     1555   1555  2.21  
LINK         OD1 ASP A 145                MG    MG A 303     1555   1555  2.52  
LINK         OD2 ASP C 145                MG    MG C 303     1555   1555  2.54  
LINK         OD2 ASP A 145                MG    MG A 303     1555   1555  2.60  
LINK         OD1 ASP C 145                MG    MG C 303     1555   1555  2.63  
LINK        MG    MG A 302                 O   HOH A 402     1555   1555  2.07  
LINK        MG    MG C 302                 O   HOH C 402     1555   1555  2.07  
LINK        MG    MG C 302                 O   HOH C 401     1555   1555  2.07  
LINK        MG    MG A 302                 O   HOH A 401     1555   1555  2.13  
LINK        MG    MG A 303                 O   HOH A 404     1555   1555  2.23  
LINK        MG    MG A 303                 O   HOH A 403     1555   1555  2.27  
LINK        MG    MG C 303                 O   HOH C 403     1555   1555  2.29  
LINK        MG    MG C 303                 O   HOH C 404     1555   1555  2.32  
LINK        MG    MG A 303                 O   HOH A 413     1555   1555  2.79  
LINK        MG    MG C 303                 O   HOH C 410     1555   1555  2.84  
LINK        MG    MG C 303                 O   HOH C 406     1555   1555  2.95  
CISPEP   1 VAL A  154    PRO A  155          0        -0.13                     
CISPEP   2 GLN B  323    PRO B  324          0        -0.54                     
CISPEP   3 ASP B  345    PRO B  346          0        10.33                     
CISPEP   4 VAL C  154    PRO C  155          0         0.10                     
CISPEP   5 GLN D  323    PRO D  324          0        -1.20                     
CISPEP   6 ASP D  345    PRO D  346          0         7.70                     
SITE     1 AC1 20 ILE A  10  ALA A  31  LYS A  33  GLU A  81                    
SITE     2 AC1 20 LEU A  83  ASP A  86  LYS A  89  GLN A 131                    
SITE     3 AC1 20 ASN A 132  LEU A 134  ASP A 145   MG A 302                    
SITE     4 AC1 20  MG A 303  GOL A 306  HOH A 401  HOH A 404                    
SITE     5 AC1 20 HOH A 409  HOH A 435  HOH A 440  HOH A 460                    
SITE     1 AC2  5 ASN A 132  ASP A 145  ADP A 301  HOH A 401                    
SITE     2 AC2  5 HOH A 402                                                     
SITE     1 AC3  5 ASP A 145  ADP A 301  HOH A 403  HOH A 404                    
SITE     2 AC3  5 HOH A 413                                                     
SITE     1 AC4  7 ILE A 209  ASP A 210  PHE A 213  ARG A 217                    
SITE     2 AC4  7 GLU D 224  TYR D 225  GLU D 277                               
SITE     1 AC5  7 PHE A   4  ASN A  23  GLU A  28  VAL A  30                    
SITE     2 AC5  7 ASP A  68  HOH A 405  HOH A 513                               
SITE     1 AC6  4 ASP A  86  LYS A  88  LYS A  89  ADP A 301                    
SITE     1 AC7  1 GLN A 131                                                     
SITE     1 AC8  7 GLU B 224  TYR B 225  GLU B 277  ILE C 209                    
SITE     2 AC8  7 ASP C 210  PHE C 213  ARG C 217                               
SITE     1 AC9  7 TYR B 199  ARG B 202  GLN B 203  LEU B 243                    
SITE     2 AC9  7 SER B 244  MET B 246  SER B 247                               
SITE     1 BC1 21 ILE C  10  ALA C  31  LYS C  33  GLU C  81                    
SITE     2 BC1 21 PHE C  82  LEU C  83  ASP C  86  LYS C  89                    
SITE     3 BC1 21 GLN C 131  ASN C 132  LEU C 134  ASP C 145                    
SITE     4 BC1 21  MG C 302   MG C 303  HOH C 401  HOH C 402                    
SITE     5 BC1 21 HOH C 404  HOH C 415  HOH C 433  HOH C 446                    
SITE     6 BC1 21 HOH C 452                                                     
SITE     1 BC2  5 ASN C 132  ASP C 145  ADP C 301  HOH C 401                    
SITE     2 BC2  5 HOH C 402                                                     
SITE     1 BC3  6 ASP C 145  ADP C 301  HOH C 403  HOH C 404                    
SITE     2 BC3  6 HOH C 406  HOH C 410                                          
SITE     1 BC4  5 PHE C   4  ASN C  23  GLU C  28  ASP C  68                    
SITE     2 BC4  5 HOH C 408                                                     
SITE     1 BC5  2 PRO C 130  GLN C 131                                          
SITE     1 BC6  5 PRO A 228  GLN D 370  SER D 371  PRO D 373                    
SITE     2 BC6  5 HOH D 647                                                     
SITE     1 BC7  4 THR D 184  ARG D 187  GLN D 379  HOH D 753                    
SITE     1 BC8  6 TYR D 199  ARG D 202  GLN D 203  LEU D 243                    
SITE     2 BC8  6 SER D 244  SER D 247                                          
CRYST1   70.770  164.130   73.280  90.00 107.07  90.00 P 1 21 1      4          
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      0.014130  0.000000  0.004339        0.00000                         
SCALE2      0.000000  0.006093  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014275        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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