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Database: PDB
Entry: 4X21
LinkDB: 4X21
Original site: 4X21 
HEADER    TRANSFERASE                             25-NOV-14   4X21              
TITLE     THE MAP KINASE JNK3 AS TARGET FOR HALOGEN BONDING                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 10;                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 39-402;                                       
COMPND   5 SYNONYM: MAPK 10,MAP KINASE P49 3F12,STRESS-ACTIVATED PROTEIN KINASE 
COMPND   6 1B,SAPK1B,STRESS-ACTIVATED PROTEIN KINASE JNK3,C-JUN N-TERMINAL      
COMPND   7 KINASE 3;                                                            
COMPND   8 EC: 2.7.11.24;                                                       
COMPND   9 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: MAPK10, JNK3, JNK3A, PRKM10, SAPK1B;                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET24A                                    
KEYWDS    MAPK, HALOGEN BOND COMPLEX, TRANSFERASE                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.LANGE,F.M.BUETTNER,M.B.GUENTHER,M.O.ZIMMERMANN,S.HENNIG,S.A.LAUFER, 
AUTHOR   2 T.STEHLE,F.BOECKLER                                                  
REVDAT   3   02-DEC-15 4X21    1       JRNL                                     
REVDAT   2   25-NOV-15 4X21    1       JRNL                                     
REVDAT   1   11-NOV-15 4X21    0                                                
JRNL        AUTH   A.LANGE,M.GUNTHER,F.M.BUTTNER,M.O.ZIMMERMANN,J.HEIDRICH,     
JRNL        AUTH 2 S.HENNIG,S.ZAHN,C.SCHALL,A.SIEVERS-ENGLER,F.ANSIDERI,P.KOCH, 
JRNL        AUTH 3 M.LAEMMERHOFER,T.STEHLE,S.A.LAUFER,F.M.BOECKLER              
JRNL        TITL   TARGETING THE GATEKEEPER MET146 OF C-JUN N-TERMINAL KINASE 3 
JRNL        TITL 2 INDUCES A BIVALENT HALOGEN/CHALCOGEN BOND.                   
JRNL        REF    J.AM.CHEM.SOC.                V. 137 14640 2015              
JRNL        REFN                   ESSN 1520-5126                               
JRNL        PMID   26505827                                                     
JRNL        DOI    10.1021/JACS.5B07090                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.4_1496)                   
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) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.98                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.370                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 56049                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.201                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.224                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2803                            
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 46.9981 -  5.2905    1.00     2897   153  0.2105 0.2307        
REMARK   3     2  5.2905 -  4.2001    1.00     2746   145  0.1623 0.1581        
REMARK   3     3  4.2001 -  3.6694    1.00     2686   141  0.1696 0.1941        
REMARK   3     4  3.6694 -  3.3340    1.00     2710   143  0.1845 0.1926        
REMARK   3     5  3.3340 -  3.0951    1.00     2674   140  0.1961 0.2383        
REMARK   3     6  3.0951 -  2.9126    1.00     2658   140  0.2098 0.2369        
REMARK   3     7  2.9126 -  2.7668    1.00     2662   140  0.2062 0.2278        
REMARK   3     8  2.7668 -  2.6464    1.00     2665   141  0.2024 0.2392        
REMARK   3     9  2.6464 -  2.5445    1.00     2650   139  0.2040 0.2339        
REMARK   3    10  2.5445 -  2.4567    1.00     2626   138  0.2055 0.2597        
REMARK   3    11  2.4567 -  2.3799    1.00     2647   140  0.2046 0.2304        
REMARK   3    12  2.3799 -  2.3119    1.00     2613   137  0.2117 0.2558        
REMARK   3    13  2.3119 -  2.2510    1.00     2659   140  0.2166 0.2686        
REMARK   3    14  2.2510 -  2.1961    1.00     2584   136  0.2170 0.2280        
REMARK   3    15  2.1961 -  2.1462    1.00     2678   141  0.2116 0.2577        
REMARK   3    16  2.1462 -  2.1005    1.00     2591   136  0.2264 0.2702        
REMARK   3    17  2.1005 -  2.0585    1.00     2658   140  0.2421 0.2589        
REMARK   3    18  2.0585 -  2.0196    1.00     2609   138  0.2470 0.2733        
REMARK   3    19  2.0196 -  1.9836    1.00     2611   137  0.2573 0.2900        
REMARK   3    20  1.9836 -  1.9499    1.00     2622   138  0.2766 0.3098        
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              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.040           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.014           5379                                  
REMARK   3   ANGLE     :  1.241           7321                                  
REMARK   3   CHIRALITY :  0.078            830                                  
REMARK   3   PLANARITY :  0.006            926                                  
REMARK   3   DIHEDRAL  : 15.615           1937                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 11                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 46 THROUGH 83 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  12.8390  42.7463  80.9679              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3482 T22:   0.2788                                     
REMARK   3      T33:   0.1927 T12:   0.0198                                     
REMARK   3      T13:   0.0367 T23:  -0.0205                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9448 L22:   3.3749                                     
REMARK   3      L33:   3.1692 L12:   1.0814                                     
REMARK   3      L13:   0.6047 L23:  -0.5321                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0697 S12:  -0.0468 S13:   0.1464                       
REMARK   3      S21:   0.2494 S22:  -0.0738 S23:  -0.1080                       
REMARK   3      S31:  -0.0481 S32:  -0.1666 S33:   0.1384                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 84 THROUGH 117 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  17.4427  45.6987  68.7377              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3250 T22:   0.3895                                     
REMARK   3      T33:   0.2945 T12:   0.0146                                     
REMARK   3      T13:  -0.0176 T23:  -0.0237                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5586 L22:   1.0348                                     
REMARK   3      L33:   2.2833 L12:   0.3851                                     
REMARK   3      L13:  -1.1374 L23:  -0.8187                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1640 S12:  -0.0685 S13:   0.1552                       
REMARK   3      S21:  -0.0973 S22:  -0.0242 S23:   0.0079                       
REMARK   3      S31:   0.0915 S32:   0.0123 S33:   0.1309                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 118 THROUGH 205 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  14.4285  34.2079  63.3119              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1767 T22:   0.1811                                     
REMARK   3      T33:   0.1504 T12:  -0.0083                                     
REMARK   3      T13:  -0.0058 T23:  -0.0078                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6863 L22:   1.4618                                     
REMARK   3      L33:   1.7927 L12:   0.1192                                     
REMARK   3      L13:  -0.2700 L23:   1.1166                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0460 S12:  -0.0640 S13:   0.0198                       
REMARK   3      S21:   0.1318 S22:  -0.0665 S23:   0.0053                       
REMARK   3      S31:  -0.0741 S32:  -0.0606 S33:   0.0250                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 206 THROUGH 258 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  27.4436  28.5710  55.4883              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2301 T22:   0.1962                                     
REMARK   3      T33:   0.1989 T12:  -0.0361                                     
REMARK   3      T13:  -0.0032 T23:  -0.0333                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3880 L22:   1.4664                                     
REMARK   3      L33:   0.8602 L12:  -0.5686                                     
REMARK   3      L13:  -0.1066 L23:   0.3439                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0214 S12:  -0.1063 S13:   0.2742                       
REMARK   3      S21:   0.1788 S22:   0.0452 S23:  -0.1642                       
REMARK   3      S31:  -0.1417 S32:   0.1460 S33:  -0.0855                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 259 THROUGH 279 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  35.8218  20.3333  58.1723              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2276 T22:   0.2632                                     
REMARK   3      T33:   0.3141 T12:  -0.0223                                     
REMARK   3      T13:  -0.0523 T23:  -0.0259                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5460 L22:   2.4927                                     
REMARK   3      L33:   1.9006 L12:   0.3826                                     
REMARK   3      L13:  -0.3178 L23:   0.7619                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1952 S12:  -0.2880 S13:  -0.2153                       
REMARK   3      S21:   0.3168 S22:   0.0785 S23:  -0.6253                       
REMARK   3      S31:   0.0862 S32:   0.4372 S33:  -0.2241                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 280 THROUGH 362 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  26.7743  18.1952  48.1095              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1782 T22:   0.1722                                     
REMARK   3      T33:   0.1460 T12:  -0.0030                                     
REMARK   3      T13:   0.0257 T23:  -0.0461                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5632 L22:   2.0050                                     
REMARK   3      L33:   1.5450 L12:   0.4685                                     
REMARK   3      L13:   0.0026 L23:   0.0539                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0042 S12:   0.0357 S13:  -0.1693                       
REMARK   3      S21:  -0.1865 S22:   0.0618 S23:  -0.2953                       
REMARK   3      S31:  -0.0231 S32:   0.1500 S33:  -0.0473                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 363 THROUGH 400 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  16.5555  48.4736  58.0419              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3292 T22:   0.3242                                     
REMARK   3      T33:   0.3250 T12:  -0.0073                                     
REMARK   3      T13:   0.0679 T23:   0.0453                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6152 L22:   2.1636                                     
REMARK   3      L33:   2.2517 L12:   1.5293                                     
REMARK   3      L13:   1.5833 L23:   1.7475                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2872 S12:   0.3966 S13:   0.2636                       
REMARK   3      S21:  -0.3766 S22:   0.2647 S23:   0.1623                       
REMARK   3      S31:  -0.4614 S32:   0.3716 S33:  -0.0179                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 47 THROUGH 130 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  60.2976  26.5931  72.4414              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3738 T22:   0.4174                                     
REMARK   3      T33:   0.6438 T12:  -0.0433                                     
REMARK   3      T13:  -0.0529 T23:   0.1098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2689 L22:   0.3501                                     
REMARK   3      L33:   1.3809 L12:  -0.4453                                     
REMARK   3      L13:   1.3257 L23:  -0.6533                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1026 S12:  -0.1573 S13:  -0.9878                       
REMARK   3      S21:  -0.0955 S22:   0.2778 S23:   0.3397                       
REMARK   3      S31:   0.3784 S32:  -0.2307 S33:  -0.3079                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 131 THROUGH 241 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  56.6816  40.5532  65.3938              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2025 T22:   0.2472                                     
REMARK   3      T33:   0.2886 T12:  -0.0328                                     
REMARK   3      T13:  -0.0088 T23:   0.0043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8922 L22:   1.4841                                     
REMARK   3      L33:   1.1769 L12:  -0.4164                                     
REMARK   3      L13:   0.2971 L23:  -0.7100                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1036 S12:  -0.1333 S13:  -0.4633                       
REMARK   3      S21:   0.0078 S22:  -0.0472 S23:  -0.0731                       
REMARK   3      S31:   0.1424 S32:  -0.0230 S33:  -0.0636                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 242 THROUGH 355 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  57.8893  56.7129  53.3777              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1975 T22:   0.2391                                     
REMARK   3      T33:   0.1623 T12:  -0.0086                                     
REMARK   3      T13:  -0.0150 T23:  -0.0055                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1578 L22:   1.7828                                     
REMARK   3      L33:   1.3319 L12:  -0.0504                                     
REMARK   3      L13:  -1.2213 L23:  -0.1540                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0060 S12:   0.3715 S13:  -0.0484                       
REMARK   3      S21:  -0.1002 S22:  -0.0545 S23:  -0.0224                       
REMARK   3      S31:   0.0118 S32:  -0.1124 S33:   0.0302                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 356 THROUGH 400 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  56.9889  41.4776  77.4378              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3805 T22:   0.6023                                     
REMARK   3      T33:   0.4187 T12:   0.0689                                     
REMARK   3      T13:   0.0139 T23:   0.0326                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9218 L22:   1.9676                                     
REMARK   3      L33:   1.3211 L12:  -3.3308                                     
REMARK   3      L13:   2.5734 L23:  -1.7786                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5052 S12:  -1.2768 S13:   0.0606                       
REMARK   3      S21:   0.2072 S22:   0.5696 S23:   0.0579                       
REMARK   3      S31:   0.0099 S32:  -0.5470 S33:  -0.0919                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4X21 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-NOV-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000204930.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-SEP-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.1                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.918409                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56051                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 13.20                              
REMARK 200  R MERGE                    (I) : 0.15200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.3500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.40                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.22600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.420                              
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: 2P33                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, SODIUM CHLORIDE, MAGNESIUM        
REMARK 280  CHLORIDE, BETA-MERCAPTOETHANOL ETHYLENE GLYCOLE, ZWITTERGENT 3-     
REMARK 280  14, AMP-PCP BIS-TRIS, SODIUM CHLORIDE, PEG 3350, GLYCEROLE, PH      
REMARK 280  7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292.15K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       77.97000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.92000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       77.97000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.92000            
REMARK 290   SMTRY3   4  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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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     GLY A    36                                                      
REMARK 465     GLY A    37                                                      
REMARK 465     SER A    38                                                      
REMARK 465     MET A    39                                                      
REMARK 465     SER A    40                                                      
REMARK 465     LYS A    41                                                      
REMARK 465     SER A    42                                                      
REMARK 465     LYS A    43                                                      
REMARK 465     VAL A    44                                                      
REMARK 465     ASP A    45                                                      
REMARK 465     ALA A   211                                                      
REMARK 465     ARG A   212                                                      
REMARK 465     THR A   213                                                      
REMARK 465     ALA A   214                                                      
REMARK 465     GLY A   215                                                      
REMARK 465     THR A   216                                                      
REMARK 465     SER A   217                                                      
REMARK 465     PHE A   218                                                      
REMARK 465     MET A   219                                                      
REMARK 465     MET A   220                                                      
REMARK 465     THR A   221                                                      
REMARK 465     PRO A   222                                                      
REMARK 465     TYR A   223                                                      
REMARK 465     VAL A   224                                                      
REMARK 465     TYR A   376                                                      
REMARK 465     ASP A   377                                                      
REMARK 465     LYS A   378                                                      
REMARK 465     GLN A   379                                                      
REMARK 465     LEU A   380                                                      
REMARK 465     SER A   401                                                      
REMARK 465     GLU A   402                                                      
REMARK 465     GLY B    36                                                      
REMARK 465     GLY B    37                                                      
REMARK 465     SER B    38                                                      
REMARK 465     MET B    39                                                      
REMARK 465     SER B    40                                                      
REMARK 465     LYS B    41                                                      
REMARK 465     SER B    42                                                      
REMARK 465     LYS B    43                                                      
REMARK 465     VAL B    44                                                      
REMARK 465     ASP B    45                                                      
REMARK 465     ASN B    46                                                      
REMARK 465     ARG B   212                                                      
REMARK 465     THR B   213                                                      
REMARK 465     ALA B   214                                                      
REMARK 465     GLY B   215                                                      
REMARK 465     THR B   216                                                      
REMARK 465     SER B   217                                                      
REMARK 465     PHE B   218                                                      
REMARK 465     MET B   219                                                      
REMARK 465     MET B   220                                                      
REMARK 465     THR B   221                                                      
REMARK 465     PRO B   222                                                      
REMARK 465     TYR B   223                                                      
REMARK 465     VAL B   224                                                      
REMARK 465     TYR B   376                                                      
REMARK 465     ASP B   377                                                      
REMARK 465     LYS B   378                                                      
REMARK 465     GLN B   379                                                      
REMARK 465     LEU B   380                                                      
REMARK 465     SER B   401                                                      
REMARK 465     GLU B   402                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  52    CG   CD   OE1  OE2                                  
REMARK 470     ASN A  66    CG   OD1  ND2                                       
REMARK 470     LYS A  68    CG   CD   CE   NZ                                   
REMARK 470     GLN A  75    CG   CD   OE1  NE2                                  
REMARK 470     ARG A  97    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 100    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 106    CD   CE   NZ                                        
REMARK 470     ARG A 107    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 110    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 137    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 138    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 140    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 155    CD   OE1  NE2                                       
REMARK 470     GLU A 164    CD   OE1  OE2                                       
REMARK 470     LYS A 198    CE   NZ                                             
REMARK 470     LEU A 210    CG   CD1  CD2                                       
REMARK 470     VAL A 225    CG1  CG2                                            
REMARK 470     LYS A 241    CE   NZ                                             
REMARK 470     ARG A 266    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 274    CE   NZ                                             
REMARK 470     GLU A 285    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 288    CG   CD   CE   NZ                                   
REMARK 470     ASN A 296    CG   OD1  ND2                                       
REMARK 470     LYS A 303    CD   CE   NZ                                        
REMARK 470     GLU A 323    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 375    CG1  CG2  CD1                                       
REMARK 470     ASP A 381    CG   OD1  OD2                                       
REMARK 470     GLU A 382    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 383    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 384    CD   OE1  OE2                                       
REMARK 470     ILE A 387    CG1  CG2  CD1                                       
REMARK 470     GLU A 388    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 391    CE   NZ                                             
REMARK 470     GLU A 392    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 396    CD   CE   NZ                                        
REMARK 470     ASN A 400    CG   OD1  ND2                                       
REMARK 470     GLU B  52    CG   CD   OE1  OE2                                  
REMARK 470     ASP B  55    CG   OD1  OD2                                       
REMARK 470     LYS B  62    CG   CD   CE   NZ                                   
REMARK 470     GLN B  65    CG   CD   OE1  NE2                                  
REMARK 470     ASN B  66    CG   OD1  ND2                                       
REMARK 470     LYS B  68    CG   CD   CE   NZ                                   
REMARK 470     GLN B  75    CG   CD   OE1  NE2                                  
REMARK 470     ILE B  77    CG1  CG2  CD1                                       
REMARK 470     LYS B 106    CG   CD   CE   NZ                                   
REMARK 470     ARG B 107    NE   CZ   NH1  NH2                                  
REMARK 470     LYS B 116    CG   CD   CE   NZ                                   
REMARK 470     ASN B 119    CG   OD1  ND2                                       
REMARK 470     LYS B 134    CG   CD   CE   NZ                                   
REMARK 470     GLU B 137    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 155    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 160    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 260    CG   CD   CE   NZ                                   
REMARK 470     ARG B 266    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 285    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 288    CD   CE   NZ                                        
REMARK 470     LYS B 289    CG   CD   CE   NZ                                   
REMARK 470     GLN B 291    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 295    CZ   NH1  NH2                                       
REMARK 470     ASN B 296    CG   OD1  ND2                                       
REMARK 470     ASP B 321    CG   OD1  OD2                                       
REMARK 470     GLU B 323    CD   OE1  OE2                                       
REMARK 470     LYS B 326    CG   CD   CE   NZ                                   
REMARK 470     GLN B 374    CG   CD   OE1  NE2                                  
REMARK 470     ILE B 375    CG1  CG2  CD1                                       
REMARK 470     ASP B 381    CG   OD1  OD2                                       
REMARK 470     GLU B 382    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 383    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 384    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 396    CG   CD   CE   NZ                                   
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    ARG A 188       -6.59     67.34                                   
REMARK 500    GLN B 140      -53.51   -130.35                                   
REMARK 500    ARG B 188       -2.62     69.42                                   
REMARK 500    THR B 308      149.43     87.58                                   
REMARK 500    ALA B 320       54.44   -153.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 3WH A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 3WH B 501 and MET B    
REMARK 800  146                                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2P33   RELATED DB: PDB                                   
REMARK 900 2P33 IS THE SAME KINASE IN COMPLEX WITH ANOTHER LIGAND               
DBREF  4X21 A   39   402  UNP    P53779   MK10_HUMAN      39    402             
DBREF  4X21 B   39   402  UNP    P53779   MK10_HUMAN      39    402             
SEQADV 4X21 GLY A   36  UNP  P53779              EXPRESSION TAG                 
SEQADV 4X21 GLY A   37  UNP  P53779              EXPRESSION TAG                 
SEQADV 4X21 SER A   38  UNP  P53779              EXPRESSION TAG                 
SEQADV 4X21 GLY B   36  UNP  P53779              EXPRESSION TAG                 
SEQADV 4X21 GLY B   37  UNP  P53779              EXPRESSION TAG                 
SEQADV 4X21 SER B   38  UNP  P53779              EXPRESSION TAG                 
SEQRES   1 A  367  GLY GLY SER MET SER LYS SER LYS VAL ASP ASN GLN PHE          
SEQRES   2 A  367  TYR SER VAL GLU VAL GLY ASP SER THR PHE THR VAL LEU          
SEQRES   3 A  367  LYS ARG TYR GLN ASN LEU LYS PRO ILE GLY SER GLY ALA          
SEQRES   4 A  367  GLN GLY ILE VAL CYS ALA ALA TYR ASP ALA VAL LEU ASP          
SEQRES   5 A  367  ARG ASN VAL ALA ILE LYS LYS LEU SER ARG PRO PHE GLN          
SEQRES   6 A  367  ASN GLN THR HIS ALA LYS ARG ALA TYR ARG GLU LEU VAL          
SEQRES   7 A  367  LEU MET LYS CYS VAL ASN HIS LYS ASN ILE ILE SER LEU          
SEQRES   8 A  367  LEU ASN VAL PHE THR PRO GLN LYS THR LEU GLU GLU PHE          
SEQRES   9 A  367  GLN ASP VAL TYR LEU VAL MET GLU LEU MET ASP ALA ASN          
SEQRES  10 A  367  LEU CYS GLN VAL ILE GLN MET GLU LEU ASP HIS GLU ARG          
SEQRES  11 A  367  MET SER TYR LEU LEU TYR GLN MET LEU CYS GLY ILE LYS          
SEQRES  12 A  367  HIS LEU HIS SER ALA GLY ILE ILE HIS ARG ASP LEU LYS          
SEQRES  13 A  367  PRO SER ASN ILE VAL VAL LYS SER ASP CYS THR LEU LYS          
SEQRES  14 A  367  ILE LEU ASP PHE GLY LEU ALA ARG THR ALA GLY THR SER          
SEQRES  15 A  367  PHE MET MET THR PRO TYR VAL VAL THR ARG TYR TYR ARG          
SEQRES  16 A  367  ALA PRO GLU VAL ILE LEU GLY MET GLY TYR LYS GLU ASN          
SEQRES  17 A  367  VAL ASP ILE TRP SER VAL GLY CYS ILE MET GLY GLU MET          
SEQRES  18 A  367  VAL ARG HIS LYS ILE LEU PHE PRO GLY ARG ASP TYR ILE          
SEQRES  19 A  367  ASP GLN TRP ASN LYS VAL ILE GLU GLN LEU GLY THR PRO          
SEQRES  20 A  367  CYS PRO GLU PHE MET LYS LYS LEU GLN PRO THR VAL ARG          
SEQRES  21 A  367  ASN TYR VAL GLU ASN ARG PRO LYS TYR ALA GLY LEU THR          
SEQRES  22 A  367  PHE PRO LYS LEU PHE PRO ASP SER LEU PHE PRO ALA ASP          
SEQRES  23 A  367  SER GLU HIS ASN LYS LEU LYS ALA SER GLN ALA ARG ASP          
SEQRES  24 A  367  LEU LEU SER LYS MET LEU VAL ILE ASP PRO ALA LYS ARG          
SEQRES  25 A  367  ILE SER VAL ASP ASP ALA LEU GLN HIS PRO TYR ILE ASN          
SEQRES  26 A  367  VAL TRP TYR ASP PRO ALA GLU VAL GLU ALA PRO PRO PRO          
SEQRES  27 A  367  GLN ILE TYR ASP LYS GLN LEU ASP GLU ARG GLU HIS THR          
SEQRES  28 A  367  ILE GLU GLU TRP LYS GLU LEU ILE TYR LYS GLU VAL MET          
SEQRES  29 A  367  ASN SER GLU                                                  
SEQRES   1 B  367  GLY GLY SER MET SER LYS SER LYS VAL ASP ASN GLN PHE          
SEQRES   2 B  367  TYR SER VAL GLU VAL GLY ASP SER THR PHE THR VAL LEU          
SEQRES   3 B  367  LYS ARG TYR GLN ASN LEU LYS PRO ILE GLY SER GLY ALA          
SEQRES   4 B  367  GLN GLY ILE VAL CYS ALA ALA TYR ASP ALA VAL LEU ASP          
SEQRES   5 B  367  ARG ASN VAL ALA ILE LYS LYS LEU SER ARG PRO PHE GLN          
SEQRES   6 B  367  ASN GLN THR HIS ALA LYS ARG ALA TYR ARG GLU LEU VAL          
SEQRES   7 B  367  LEU MET LYS CYS VAL ASN HIS LYS ASN ILE ILE SER LEU          
SEQRES   8 B  367  LEU ASN VAL PHE THR PRO GLN LYS THR LEU GLU GLU PHE          
SEQRES   9 B  367  GLN ASP VAL TYR LEU VAL MET GLU LEU MET ASP ALA ASN          
SEQRES  10 B  367  LEU CYS GLN VAL ILE GLN MET GLU LEU ASP HIS GLU ARG          
SEQRES  11 B  367  MET SER TYR LEU LEU TYR GLN MET LEU CYS GLY ILE LYS          
SEQRES  12 B  367  HIS LEU HIS SER ALA GLY ILE ILE HIS ARG ASP LEU LYS          
SEQRES  13 B  367  PRO SER ASN ILE VAL VAL LYS SER ASP CYS THR LEU LYS          
SEQRES  14 B  367  ILE LEU ASP PHE GLY LEU ALA ARG THR ALA GLY THR SER          
SEQRES  15 B  367  PHE MET MET THR PRO TYR VAL VAL THR ARG TYR TYR ARG          
SEQRES  16 B  367  ALA PRO GLU VAL ILE LEU GLY MET GLY TYR LYS GLU ASN          
SEQRES  17 B  367  VAL ASP ILE TRP SER VAL GLY CYS ILE MET GLY GLU MET          
SEQRES  18 B  367  VAL ARG HIS LYS ILE LEU PHE PRO GLY ARG ASP TYR ILE          
SEQRES  19 B  367  ASP GLN TRP ASN LYS VAL ILE GLU GLN LEU GLY THR PRO          
SEQRES  20 B  367  CYS PRO GLU PHE MET LYS LYS LEU GLN PRO THR VAL ARG          
SEQRES  21 B  367  ASN TYR VAL GLU ASN ARG PRO LYS TYR ALA GLY LEU THR          
SEQRES  22 B  367  PHE PRO LYS LEU PHE PRO ASP SER LEU PHE PRO ALA ASP          
SEQRES  23 B  367  SER GLU HIS ASN LYS LEU LYS ALA SER GLN ALA ARG ASP          
SEQRES  24 B  367  LEU LEU SER LYS MET LEU VAL ILE ASP PRO ALA LYS ARG          
SEQRES  25 B  367  ILE SER VAL ASP ASP ALA LEU GLN HIS PRO TYR ILE ASN          
SEQRES  26 B  367  VAL TRP TYR ASP PRO ALA GLU VAL GLU ALA PRO PRO PRO          
SEQRES  27 B  367  GLN ILE TYR ASP LYS GLN LEU ASP GLU ARG GLU HIS THR          
SEQRES  28 B  367  ILE GLU GLU TRP LYS GLU LEU ILE TYR LYS GLU VAL MET          
SEQRES  29 B  367  ASN SER GLU                                                  
HET    3WH  A 501      28                                                       
HET     CL  A 502       1                                                       
HET    3WH  B 501      28                                                       
HET     CL  B 502       1                                                       
HETNAM     3WH N-ETHYL-4-{[4-(1H-INDOL-3-YL)-5-IODOPYRIMIDIN-2-                 
HETNAM   2 3WH  YL]AMINO}PIPERIDINE-1-CARBOXAMIDE                               
HETNAM      CL CHLORIDE ION                                                     
FORMUL   3  3WH    2(C20 H23 I N6 O)                                            
FORMUL   4   CL    2(CL 1-)                                                     
FORMUL   7  HOH   *342(H2 O)                                                    
HELIX    1 AA1 ASN A  101  VAL A  118  1                                  18    
HELIX    2 AA2 LEU A  153  ILE A  157  1                                   5    
HELIX    3 AA3 ASP A  162  ALA A  183  1                                  22    
HELIX    4 AA4 LYS A  191  SER A  193  5                                   3    
HELIX    5 AA5 ALA A  231  LEU A  236  1                                   6    
HELIX    6 AA6 ASN A  243  HIS A  259  1                                  17    
HELIX    7 AA7 ASP A  267  GLY A  280  1                                  14    
HELIX    8 AA8 CYS A  283  LYS A  289  1                                   7    
HELIX    9 AA9 GLN A  291  ARG A  301  1                                  11    
HELIX   10 AB1 THR A  308  PHE A  313  1                                   6    
HELIX   11 AB2 PRO A  314  PHE A  318  5                                   5    
HELIX   12 AB3 SER A  322  LEU A  340  1                                  19    
HELIX   13 AB4 ASP A  343  ARG A  347  5                                   5    
HELIX   14 AB5 SER A  349  HIS A  356  1                                   8    
HELIX   15 AB6 HIS A  356  VAL A  361  1                                   6    
HELIX   16 AB7 ASP A  364  GLU A  369  1                                   6    
HELIX   17 AB8 THR A  386  MET A  399  1                                  14    
HELIX   18 AB9 ASN B  101  VAL B  118  1                                  18    
HELIX   19 AC1 LEU B  153  MET B  159  1                                   7    
HELIX   20 AC2 ASP B  162  ALA B  183  1                                  22    
HELIX   21 AC3 LYS B  191  SER B  193  5                                   3    
HELIX   22 AC4 ALA B  231  LEU B  236  1                                   6    
HELIX   23 AC5 ASN B  243  HIS B  259  1                                  17    
HELIX   24 AC6 ASP B  267  GLY B  280  1                                  14    
HELIX   25 AC7 CYS B  283  LYS B  289  1                                   7    
HELIX   26 AC8 GLN B  291  ARG B  301  1                                  11    
HELIX   27 AC9 THR B  308  PHE B  313  1                                   6    
HELIX   28 AD1 PRO B  314  PHE B  318  5                                   5    
HELIX   29 AD2 SER B  322  LEU B  340  1                                  19    
HELIX   30 AD3 SER B  349  HIS B  356  1                                   8    
HELIX   31 AD4 ILE B  359  TYR B  363  5                                   5    
HELIX   32 AD5 ASP B  364  GLU B  369  1                                   6    
HELIX   33 AD6 THR B  386  ASN B  400  1                                  15    
SHEET    1 AA1 2 PHE A  48  VAL A  53  0                                        
SHEET    2 AA1 2 SER A  56  LEU A  61 -1  O  PHE A  58   N  VAL A  51           
SHEET    1 AA2 5 TYR A  64  SER A  72  0                                        
SHEET    2 AA2 5 GLY A  76  ASP A  83 -1  O  ALA A  80   N  LYS A  68           
SHEET    3 AA2 5 ARG A  88  LEU A  95 -1  O  VAL A  90   N  ALA A  81           
SHEET    4 AA2 5 TYR A 143  GLU A 147 -1  O  LEU A 144   N  LYS A  93           
SHEET    5 AA2 5 LEU A 126  PHE A 130 -1  N  LEU A 127   O  VAL A 145           
SHEET    1 AA3 3 ALA A 151  ASN A 152  0                                        
SHEET    2 AA3 3 ILE A 195  VAL A 197 -1  O  VAL A 197   N  ALA A 151           
SHEET    3 AA3 3 LEU A 203  ILE A 205 -1  O  LYS A 204   N  VAL A 196           
SHEET    1 AA4 2 PHE B  48  VAL B  53  0                                        
SHEET    2 AA4 2 SER B  56  LEU B  61 -1  O  SER B  56   N  VAL B  53           
SHEET    1 AA5 5 TYR B  64  GLY B  73  0                                        
SHEET    2 AA5 5 GLY B  76  ASP B  83 -1  O  ALA B  80   N  LYS B  68           
SHEET    3 AA5 5 ARG B  88  SER B  96 -1  O  VAL B  90   N  ALA B  81           
SHEET    4 AA5 5 ASP B 141  GLU B 147 -1  O  VAL B 142   N  LEU B  95           
SHEET    5 AA5 5 LEU B 126  PHE B 130 -1  N  LEU B 127   O  VAL B 145           
SHEET    1 AA6 3 ALA B 151  ASN B 152  0                                        
SHEET    2 AA6 3 ILE B 195  VAL B 197 -1  O  VAL B 197   N  ALA B 151           
SHEET    3 AA6 3 LEU B 203  ILE B 205 -1  O  LYS B 204   N  VAL B 196           
LINK         SD  MET B 146                 I17 3WH B 501     1555   1555  3.05  
SITE     1 AC1 12 VAL A  78  ALA A  91  MET A 146  GLU A 147                    
SITE     2 AC1 12 MET A 149  ASP A 150  ALA A 151  ASN A 152                    
SITE     3 AC1 12 GLN A 155  LEU A 206  HOH A 715  HOH A 782                    
SITE     1 AC2  5 ARG A 227  ASP A 267  TYR A 268  ASP B 200                    
SITE     2 AC2  5 HOH B 684                                                     
SITE     1 AC3  5 GLU B 242  ASN B 243  SER B 349  VAL B 350                    
SITE     2 AC3  5 HOH B 608                                                     
SITE     1 AC4 13 SER B  72  VAL B  78  VAL B  90  ALA B  91                    
SITE     2 AC4 13 LYS B  93  LEU B 144  VAL B 145  GLU B 147                    
SITE     3 AC4 13 LEU B 148  MET B 149  ALA B 151  ASN B 152                    
SITE     4 AC4 13 GLN B 155                                                     
CRYST1  155.940  109.840   43.910  90.00  90.00  90.00 P 21 21 2     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      0.006413  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009104  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022774        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system