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Database: PDB
Entry: 6FJ0
LinkDB: 6FJ0
Original site: 6FJ0 
HEADER    TRANSFERASE                             19-JAN-18   6FJ0              
TITLE     CRYSTAL STRUCTURE OF ERK2 IN COMPLEX WITH AN ADENOSINE DERIVATIVE     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 1;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MAPK 1,ERT1,EXTRACELLULAR SIGNAL-REGULATED KINASE 2,ERK-2,  
COMPND   5 MAP KINASE ISOFORM P42,P42-MAPK,MITOGEN-ACTIVATED PROTEIN KINASE 2,  
COMPND   6 MAPK 2;                                                              
COMPND   7 EC: 2.7.11.24;                                                       
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: MAPK1, ERK2, MAPK, PRKM1;                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.GELIN,G.LABESSE                                                     
REVDAT   1   30-JAN-19 6FJ0    0                                                
JRNL        AUTH   M.GELIN,S.POCHET,G.LABESSE                                   
JRNL        TITL   CRYSTAL STRUCTURE OF ERK2 IN COMPLEX WITH AN ADENOSINE       
JRNL        TITL 2 DERIVATIVE                                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.66 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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) : 1.66                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.80                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 44235                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.167                           
REMARK   3   R VALUE            (WORKING SET) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.194                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.950                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4011                            
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 43.8152 -  5.0945    0.97     2805   132  0.2023 0.2179        
REMARK   3     2  5.0945 -  4.0446    0.90     2536   161  0.1471 0.1602        
REMARK   3     3  4.0446 -  3.5336    0.91     2610   127  0.1459 0.1623        
REMARK   3     4  3.5336 -  3.2106    0.92     2678   125  0.1500 0.1776        
REMARK   3     5  3.2106 -  2.9805    0.92     2666   128  0.1578 0.1543        
REMARK   3     6  2.9805 -  2.8048    0.92     2642   137  0.1578 0.2048        
REMARK   3     7  2.8048 -  2.6644    0.92     2603   157  0.1581 0.1774        
REMARK   3     8  2.6644 -  2.5484    0.92     2588   156  0.1592 0.2010        
REMARK   3     9  2.5484 -  2.4503    0.92     2663   148  0.1571 0.2100        
REMARK   3    10  2.4503 -  2.3658    0.92     2621   152  0.1577 0.2092        
REMARK   3    11  2.3658 -  2.2918    0.93     2609   159  0.1587 0.2046        
REMARK   3    12  2.2918 -  2.2263    0.92     2652   142  0.1564 0.1854        
REMARK   3    13  2.2263 -  2.1677    0.93     2690   138  0.1512 0.1809        
REMARK   3    14  2.1677 -  2.1148    0.93     2568   172  0.1541 0.1904        
REMARK   3    15  2.1148 -  2.0667    0.94     2723   167  0.1511 0.1657        
REMARK   3    16  2.0667 -  2.0227    0.94     2657   134  0.1607 0.2090        
REMARK   3    17  2.0227 -  1.9823    0.94     2751   102  0.1731 0.2356        
REMARK   3    18  1.9823 -  1.9449    0.93     2672   112  0.1797 0.2291        
REMARK   3    19  1.9449 -  1.9101    0.94     2721   152  0.1676 0.2059        
REMARK   3    20  1.9101 -  1.8778    0.94     2702   114  0.1769 0.1946        
REMARK   3    21  1.8778 -  1.8475    0.94     2680   135  0.1732 0.2362        
REMARK   3    22  1.8475 -  1.8190    0.95     2775   100  0.1777 0.2194        
REMARK   3    23  1.8190 -  1.7923    0.94     2663   139  0.1874 0.2262        
REMARK   3    24  1.7923 -  1.7671    0.94     2762   135  0.2005 0.2420        
REMARK   3    25  1.7671 -  1.7432    0.95     2681   134  0.2130 0.2763        
REMARK   3    26  1.7432 -  1.7205    0.94     2681   151  0.2276 0.2948        
REMARK   3    27  1.7205 -  1.6990    0.93     2654   141  0.2393 0.2438        
REMARK   3    28  1.6990 -  1.6786    0.90     2627   126  0.2622 0.3392        
REMARK   3    29  1.6786 -  1.6590    0.86     2411   135  0.2620 0.3263        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.30                                          
REMARK   3   SHRINKAGE RADIUS   : 1.10                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.690           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.84                          
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 9 THROUGH 59 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -18.3011  17.9893  30.6855              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4217 T22:   0.6493                                     
REMARK   3      T33:   0.2639 T12:   0.0666                                     
REMARK   3      T13:  -0.1325 T23:   0.1671                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5677 L22:   0.5681                                     
REMARK   3      L33:   2.3871 L12:  -0.2996                                     
REMARK   3      L13:  -0.0525 L23:   1.0735                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2831 S12:  -0.0755 S13:   0.8519                       
REMARK   3      S21:  -0.2939 S22:   0.2689 S23:   0.1643                       
REMARK   3      S31:  -0.9256 S32:  -0.6505 S33:   0.2258                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 60 THROUGH 98 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.0706   8.8663  30.9936              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1949 T22:   0.4482                                     
REMARK   3      T33:   0.0702 T12:  -0.0796                                     
REMARK   3      T13:  -0.0910 T23:   0.0568                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4828 L22:   0.4888                                     
REMARK   3      L33:   3.6630 L12:  -0.0969                                     
REMARK   3      L13:   0.0901 L23:  -0.2324                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1651 S12:   0.1742 S13:   0.0952                       
REMARK   3      S21:  -0.2365 S22:   0.1558 S23:  -0.1051                       
REMARK   3      S31:  -0.1761 S32:   0.0550 S33:  -0.0639                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 99 THROUGH 163 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -12.3773   8.8582  49.5505              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0572 T22:   0.3034                                     
REMARK   3      T33:   0.1355 T12:   0.0188                                     
REMARK   3      T13:   0.0051 T23:   0.0210                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1710 L22:   1.1608                                     
REMARK   3      L33:   1.1525 L12:   0.2946                                     
REMARK   3      L13:   0.2995 L23:   0.1793                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0339 S12:  -0.0187 S13:   0.1767                       
REMARK   3      S21:  -0.0245 S22:   0.0367 S23:   0.2295                       
REMARK   3      S31:  -0.0819 S32:  -0.2698 S33:   0.0431                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 164 THROUGH 188 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   8.6512  10.0383  45.1682              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1608 T22:   0.3612                                     
REMARK   3      T33:   0.1919 T12:  -0.0076                                     
REMARK   3      T13:   0.0086 T23:  -0.0217                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3122 L22:   0.5098                                     
REMARK   3      L33:   1.2510 L12:   1.0997                                     
REMARK   3      L13:   1.2445 L23:   0.5196                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2135 S12:   0.3273 S13:   0.0909                       
REMARK   3      S21:  -0.0396 S22:   0.2550 S23:  -0.2273                       
REMARK   3      S31:  -0.2067 S32:   0.2880 S33:   0.0020                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 189 THROUGH 319 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   3.3373  10.1109  60.9377              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0893 T22:   0.2549                                     
REMARK   3      T33:   0.1065 T12:  -0.0005                                     
REMARK   3      T13:  -0.0038 T23:   0.0103                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7480 L22:   1.2347                                     
REMARK   3      L33:   0.9052 L12:   1.1016                                     
REMARK   3      L13:   0.6919 L23:   0.2730                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0375 S12:  -0.0871 S13:   0.0960                       
REMARK   3      S21:   0.1034 S22:  -0.0591 S23:  -0.0011                       
REMARK   3      S31:  -0.0235 S32:   0.0691 S33:   0.0154                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 320 THROUGH 353 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.4572   4.1005  29.0161              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2966 T22:   0.5277                                     
REMARK   3      T33:   0.2153 T12:  -0.0573                                     
REMARK   3      T13:   0.0308 T23:   0.0036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1441 L22:   1.2306                                     
REMARK   3      L33:   1.1598 L12:  -0.0788                                     
REMARK   3      L13:   0.2979 L23:  -0.8364                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0571 S12:   0.2631 S13:   0.0949                       
REMARK   3      S21:  -0.5351 S22:  -0.0703 S23:  -0.1929                       
REMARK   3      S31:   0.2656 S32:   0.5464 S33:   0.0553                       
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 6FJ0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JAN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200008412.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-AUG-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.93930                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.2.19                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44257                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.659                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.811                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 2.800                              
REMARK 200  R MERGE                    (I) : 0.02900                            
REMARK 200  R SYM                      (I) : 0.02900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.16200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.16200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 3QYZ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG MME 2000, 0.1M MES PH 6.5, 0.1M      
REMARK 280  AMMONIUM SULFATE, 0.02M BETA-MERCAPTOETHANOL, 0.002M MAGNESIUM      
REMARK 280  SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K            
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       34.89500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1000 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
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 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     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     ASP A   330                                                      
REMARK 465     MET A   331                                                      
REMARK 465     GLU A   332                                                      
REMARK 465     LEU A   333                                                      
REMARK 465     ASP A   334                                                      
REMARK 465     PRO A   354                                                      
REMARK 465     GLY A   355                                                      
REMARK 465     TYR A   356                                                      
REMARK 465     ARG A   357                                                      
REMARK 465     SER A   358                                                      
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     ARG A  13    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 328    CG   CD   CE   NZ                                   
REMARK 470     PHE A 329    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     ASP A 335    CB   CG   OD1  OD2                                  
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  13       44.69     18.99                                   
REMARK 500    ASP A 147       42.37   -149.70                                   
REMARK 500    ASP A 165       87.40     55.58                                   
REMARK 500    ALA A 187      176.72     65.93                                   
REMARK 500    ASN A 199       18.37   -161.94                                   
REMARK 500    LEU A 292       48.20    -93.51                                   
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 DMS A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue A3N A 406                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3QYZ   RELATED DB: PDB                                   
REMARK 900 CONTAINS THE SAME PROTEIN IN COMPLEX WITH ANOTHER ADENOSINE          
REMARK 900 DERIVATIVE                                                           
REMARK 900 RELATED ID: 6FI3   RELATED DB: PDB                                   
REMARK 900 CONTAINS THE SAME PROTEIN IN COMPLEX WITH ANOTHER ADENOSINE          
REMARK 900 DERIVATIVE                                                           
REMARK 900 RELATED ID: 6FI6   RELATED DB: PDB                                   
REMARK 900 CONTAINS THE SAME PROTEIN IN COMPLEX WITH ANOTHER ADENOSINE          
REMARK 900 DERIVATIVE                                                           
DBREF  6FJ0 A    1   358  UNP    P63086   MK01_RAT         1    358             
SEQADV 6FJ0 HIS A   -5  UNP  P63086              EXPRESSION TAG                 
SEQADV 6FJ0 HIS A   -4  UNP  P63086              EXPRESSION TAG                 
SEQADV 6FJ0 HIS A   -3  UNP  P63086              EXPRESSION TAG                 
SEQADV 6FJ0 HIS A   -2  UNP  P63086              EXPRESSION TAG                 
SEQADV 6FJ0 HIS A   -1  UNP  P63086              EXPRESSION TAG                 
SEQADV 6FJ0 HIS A    0  UNP  P63086              EXPRESSION TAG                 
SEQRES   1 A  364  HIS HIS HIS HIS HIS HIS MET ALA ALA ALA ALA ALA ALA          
SEQRES   2 A  364  GLY PRO GLU MET VAL ARG GLY GLN VAL PHE ASP VAL GLY          
SEQRES   3 A  364  PRO ARG TYR THR ASN LEU SER TYR ILE GLY GLU GLY ALA          
SEQRES   4 A  364  TYR GLY MET VAL CYS SER ALA TYR ASP ASN LEU ASN LYS          
SEQRES   5 A  364  VAL ARG VAL ALA ILE LYS LYS ILE SER PRO PHE GLU HIS          
SEQRES   6 A  364  GLN THR TYR CYS GLN ARG THR LEU ARG GLU ILE LYS ILE          
SEQRES   7 A  364  LEU LEU ARG PHE ARG HIS GLU ASN ILE ILE GLY ILE ASN          
SEQRES   8 A  364  ASP ILE ILE ARG ALA PRO THR ILE GLU GLN MET LYS ASP          
SEQRES   9 A  364  VAL TYR ILE VAL GLN ASP LEU MET GLU THR ASP LEU TYR          
SEQRES  10 A  364  LYS LEU LEU LYS THR GLN HIS LEU SER ASN ASP HIS ILE          
SEQRES  11 A  364  CYS TYR PHE LEU TYR GLN ILE LEU ARG GLY LEU LYS TYR          
SEQRES  12 A  364  ILE HIS SER ALA ASN VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  13 A  364  SER ASN LEU LEU LEU ASN THR THR CME ASP LEU LYS ILE          
SEQRES  14 A  364  CYS ASP PHE GLY LEU ALA ARG VAL ALA ASP PRO ASP HIS          
SEQRES  15 A  364  ASP HIS THR GLY PHE LEU THR GLU TYR VAL ALA THR ARG          
SEQRES  16 A  364  TRP TYR ARG ALA PRO GLU ILE MET LEU ASN SER LYS GLY          
SEQRES  17 A  364  TYR THR LYS SER ILE ASP ILE TRP SER VAL GLY CYS ILE          
SEQRES  18 A  364  LEU ALA GLU MET LEU SER ASN ARG PRO ILE PHE PRO GLY          
SEQRES  19 A  364  LYS HIS TYR LEU ASP GLN LEU ASN HIS ILE LEU GLY ILE          
SEQRES  20 A  364  LEU GLY SER PRO SER GLN GLU ASP LEU ASN CYS ILE ILE          
SEQRES  21 A  364  ASN LEU LYS ALA ARG ASN TYR LEU LEU SER LEU PRO HIS          
SEQRES  22 A  364  LYS ASN LYS VAL PRO TRP ASN ARG LEU PHE PRO ASN ALA          
SEQRES  23 A  364  ASP SER LYS ALA LEU ASP LEU LEU ASP LYS MET LEU THR          
SEQRES  24 A  364  PHE ASN PRO HIS LYS ARG ILE GLU VAL GLU GLN ALA LEU          
SEQRES  25 A  364  ALA HIS PRO TYR LEU GLU GLN TYR TYR ASP PRO SER ASP          
SEQRES  26 A  364  GLU PRO ILE ALA GLU ALA PRO PHE LYS PHE ASP MET GLU          
SEQRES  27 A  364  LEU ASP ASP LEU PRO LYS GLU LYS LEU LYS GLU LEU ILE          
SEQRES  28 A  364  PHE GLU GLU THR ALA ARG PHE GLN PRO GLY TYR ARG SER          
MODRES 6FJ0 CME A  159  CYS  MODIFIED RESIDUE                                   
HET    CME  A 159      10                                                       
HET    DMS  A 401       4                                                       
HET    DMS  A 402       4                                                       
HET    DMS  A 403       4                                                       
HET    DMS  A 404       4                                                       
HET    SO4  A 405       5                                                       
HET    A3N  A 406      22                                                       
HETNAM     CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE                                 
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     SO4 SULFATE ION                                                      
HETNAM     A3N 5'-DEOXY-5'-(PROP-2-YN-1-YLAMINO)ADENOSINE                       
FORMUL   1  CME    C5 H11 N O3 S2                                               
FORMUL   2  DMS    4(C2 H6 O S)                                                 
FORMUL   6  SO4    O4 S 2-                                                      
FORMUL   7  A3N    C13 H16 N6 O3                                                
FORMUL   8  HOH   *330(H2 O)                                                    
HELIX    1 AA1 HIS A   59  PHE A   76  1                                  18    
HELIX    2 AA2 LEU A  110  GLN A  117  1                                   8    
HELIX    3 AA3 SER A  120  ALA A  141  1                                  22    
HELIX    4 AA4 LYS A  149  SER A  151  5                                   3    
HELIX    5 AA5 ASP A  173  ASP A  177  5                                   5    
HELIX    6 AA6 THR A  188  ARG A  192  5                                   5    
HELIX    7 AA7 ALA A  193  ASN A  199  1                                   7    
HELIX    8 AA8 LYS A  205  ASN A  222  1                                  18    
HELIX    9 AA9 LEU A  232  GLY A  243  1                                  12    
HELIX   10 AB1 SER A  246  CYS A  252  1                                   7    
HELIX   11 AB2 ASN A  255  SER A  264  1                                  10    
HELIX   12 AB3 PRO A  272  PHE A  277  1                                   6    
HELIX   13 AB4 ASP A  281  LEU A  292  1                                  12    
HELIX   14 AB5 GLU A  301  ALA A  307  1                                   7    
HELIX   15 AB6 HIS A  308  GLU A  312  5                                   5    
HELIX   16 AB7 ASP A  316  GLU A  320  5                                   5    
HELIX   17 AB8 PRO A  337  THR A  349  1                                  13    
HELIX   18 AB9 ALA A  350  GLN A  353  5                                   4    
SHEET    1 AA1 2 MET A  11  VAL A  12  0                                        
SHEET    2 AA1 2 GLN A  15  VAL A  16 -1  O  GLN A  15   N  VAL A  12           
SHEET    1 AA2 5 TYR A  23  GLU A  31  0                                        
SHEET    2 AA2 5 GLY A  35  ASP A  42 -1  O  TYR A  41   N  THR A  24           
SHEET    3 AA2 5 VAL A  47  ILE A  54 -1  O  VAL A  49   N  ALA A  40           
SHEET    4 AA2 5 VAL A  99  ASP A 104 -1  O  VAL A  99   N  ILE A  54           
SHEET    5 AA2 5 ASP A  86  ILE A  88 -1  N  ASP A  86   O  VAL A 102           
SHEET    1 AA3 3 THR A 108  ASP A 109  0                                        
SHEET    2 AA3 3 LEU A 153  LEU A 155 -1  O  LEU A 155   N  THR A 108           
SHEET    3 AA3 3 LEU A 161  ILE A 163 -1  O  LYS A 162   N  LEU A 154           
SHEET    1 AA4 2 VAL A 143  LEU A 144  0                                        
SHEET    2 AA4 2 ARG A 170  VAL A 171 -1  O  ARG A 170   N  LEU A 144           
LINK         C   THR A 158                 N   CME A 159     1555   1555  1.33  
LINK         C   CME A 159                 N   ASP A 160     1555   1555  1.33  
SITE     1 AC1  2 LYS A 149  SER A 151                                          
SITE     1 AC2  4 ASP A 122  HIS A 123  ARG A 259  TYR A 314                    
SITE     1 AC3  4 HIS A 297  LYS A 298  ARG A 299  GLN A 304                    
SITE     1 AC4  4 GLY A  32  ALA A  33  TYR A  34  GLY A  35                    
SITE     1 AC5  4 ARG A 189  ARG A 192  TYR A 231  HOH A 675                    
SITE     1 AC6  9 GLU A  31  VAL A  37  ALA A  50  GLN A 103                    
SITE     2 AC6  9 ASP A 104  MET A 106  ASP A 109  LYS A 112                    
SITE     3 AC6  9 HOH A 647                                                     
CRYST1   48.550   69.790   59.370  90.00 108.63  90.00 P 1 21 1      2          
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      0.020597  0.000000  0.006944        0.00000                         
SCALE2      0.000000  0.014329  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017775        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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