GenomeNet

Database: PDB
Entry: 2W4O
LinkDB: 2W4O
Original site: 2W4O 
HEADER    TRANSFERASE                             28-NOV-08   2W4O              
TITLE     CRYSTAL STRUCTURE OF HUMAN CAMK4 IN COMPLEX WITH 4-AMINO(SULFAMOYL-   
TITLE    2 PHENYLAMINO)-TRIAZOLE-CARBOTHIOIC ACID (2,6-DIFLUORO-PHENYL)-AMIDE)  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE IV;       
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 15-340;                                           
COMPND   5 SYNONYM: CAM KINASE-GR, CAMK4A;                                      
COMPND   6 EC: 2.7.11.17;                                                       
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: CALM;                                     
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    CALMODULIN-BINDING, NUCLEOTIDE-BINDING, SERINE/THREONINE-PROTEIN      
KEYWDS   2 KINASE, ATP-BINDING, PHOSPHOPROTEIN, KINASE, NUCLEUS, TRANSFERASE    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.R.C.MUNIZ,P.RELLOS,O.GILEADI,O.FEDOROV,P.FILIPPAKOPOULOS,E.SALAH,   
AUTHOR   2 A.PIKE,C.PHILLIPS,F.NIESEN,L.SHRESTHA,N.BURGESS-BROWN,A.BULLOCK,     
AUTHOR   3 G.BERRIDGE,F.VON DELFT,A.M.EDWARDS,C.BOUNTRA,C.H.ARROWSMITH,         
AUTHOR   4 J.WEIGELT,S.KNAPP                                                    
REVDAT   3   24-JAN-18 2W4O    1       JRNL                                     
REVDAT   2   05-DEC-12 2W4O    1       COMPND SOURCE KEYWDS AUTHOR              
REVDAT   2 2                   1       JRNL   REMARK VERSN  DBREF               
REVDAT   2 3                   1       SEQADV HETSYN FORMUL MASTER              
REVDAT   1   20-JAN-09 2W4O    0                                                
JRNL        AUTH   J.R.C.MUNIZ,P.RELLOS,O.GILEADI,O.FEDOROV,P.FILIPPAKOPOULOS,  
JRNL        AUTH 2 E.SALAH,A.PIKE,C.PHILLIPS,F.NIESEN,L.SHRESTHA,               
JRNL        AUTH 3 N.BURGESS-BROWN,A.BULLOCK,G.BERRIDGE,F.VON DELFT,            
JRNL        AUTH 4 A.M.EDWARDS,C.BOUNTRA,C.H.ARROWSMITH,J.WEIGELT,S.KNAPP       
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN CAMK4 IN COMPLEX WITH             
JRNL        TITL 2 4-AMINO(SULFAMOYL-PHENYLAMINO)-TRIAZOLE- CARBOTHIOIC ACID    
JRNL        TITL 3 (2,6-DIFLUORO-PHENYL)-AMIDE)                                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.17 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.17                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.38                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.020                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 15656                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.216                           
REMARK   3   R VALUE            (WORKING SET) : 0.214                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.030                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1570                            
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 36.3822 -  4.8226    0.99     1442   160  0.2205 0.2551        
REMARK   3     2  4.8226 -  3.8292    1.00     1362   151  0.1802 0.1925        
REMARK   3     3  3.8292 -  3.3456    0.99     1350   151  0.1944 0.1929        
REMARK   3     4  3.3456 -  3.0398    0.99     1314   146  0.2164 0.2449        
REMARK   3     5  3.0398 -  2.8221    0.97     1300   147  0.2169 0.2358        
REMARK   3     6  2.8221 -  2.6557    0.97     1281   145  0.2306 0.2583        
REMARK   3     7  2.6557 -  2.5228    0.94     1251   142  0.2272 0.2569        
REMARK   3     8  2.5228 -  2.4130    0.94     1255   137  0.2131 0.2753        
REMARK   3     9  2.4130 -  2.3201    0.93     1237   130  0.2494 0.2974        
REMARK   3    10  2.3201 -  2.2400    0.91     1179   133  0.2360 0.2751        
REMARK   3    11  2.2400 -  2.1700    0.85     1115   128  0.2538 0.2638        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.34                                          
REMARK   3   B_SOL              : 52.28                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.260            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.180           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.43010                                             
REMARK   3    B22 (A**2) : 4.85480                                              
REMARK   3    B33 (A**2) : -4.42470                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           2214                                  
REMARK   3   ANGLE     :  1.390           3012                                  
REMARK   3   CHIRALITY :  0.077            335                                  
REMARK   3   PLANARITY :  0.009            386                                  
REMARK   3   DIHEDRAL  : 18.201            774                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 23:231)                              
REMARK   3    ORIGIN FOR THE GROUP (A):   1.2431   4.8627  15.1404              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2604 T22:   0.2324                                     
REMARK   3      T33:   0.1819 T12:   0.0533                                     
REMARK   3      T13:   0.0017 T23:  -0.0041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6623 L22:   0.6324                                     
REMARK   3      L33:   1.0418 L12:   0.1894                                     
REMARK   3      L13:   0.9229 L23:   0.2172                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0834 S12:  -0.1966 S13:   0.0464                       
REMARK   3      S21:   0.2173 S22:   0.0811 S23:  -0.0027                       
REMARK   3      S31:   0.0201 S32:  -0.1363 S33:  -0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 232:324)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.2191   0.4745  -6.2216              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1799 T22:   0.2035                                     
REMARK   3      T33:   0.1969 T12:   0.0081                                     
REMARK   3      T13:   0.0344 T23:   0.0379                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4271 L22:   0.6132                                     
REMARK   3      L33:   0.8420 L12:  -0.4475                                     
REMARK   3      L13:   0.2084 L23:   0.1857                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1032 S12:   0.2306 S13:   0.1040                       
REMARK   3      S21:  -0.1457 S22:  -0.0686 S23:  -0.0547                       
REMARK   3      S31:   0.0336 S32:   0.0901 S33:  -0.0000                       
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 2W4O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-NOV-08.                  
REMARK 100 THE DEPOSITION ID IS D_1290038227.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-OCT-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99987                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18562                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.980                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.900                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
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: PDB ENTRY 2JAM                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 17% PEG 10K; 0.10M (NH4)(AC); 0.1M BIS   
REMARK 280  -TRIS PH 5.5                                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       21.20000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.57550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.40500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.57550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.20000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.40500            
REMARK 290   SMTRY3   4  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: PQS                                                   
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     MET A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     GLY A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     ASN A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     TYR A    10                                                      
REMARK 465     PHE A    11                                                      
REMARK 465     GLN A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     MET A    14                                                      
REMARK 465     SER A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     VAL A    17                                                      
REMARK 465     THR A    18                                                      
REMARK 465     ALA A    19                                                      
REMARK 465     SER A    20                                                      
REMARK 465     ALA A    21                                                      
REMARK 465     ALA A    22                                                      
REMARK 465     PRO A    23                                                      
REMARK 465     GLY A    24                                                      
REMARK 465     THR A    25                                                      
REMARK 465     ALA A    26                                                      
REMARK 465     SER A    27                                                      
REMARK 465     LEU A    28                                                      
REMARK 465     VAL A    29                                                      
REMARK 465     PRO A    30                                                      
REMARK 465     ASP A    31                                                      
REMARK 465     TYR A    32                                                      
REMARK 465     TRP A    33                                                      
REMARK 465     THR A    80                                                      
REMARK 465     VAL A    81                                                      
REMARK 465     ASP A    82                                                      
REMARK 465     LYS A    83                                                      
REMARK 465     LYS A    84                                                      
REMARK 465     ILE A    85                                                      
REMARK 465     VAL A    86                                                      
REMARK 465     ARG A    87                                                      
REMARK 465     THR A    88                                                      
REMARK 465     GLU A    89                                                      
REMARK 465     GLY A   187                                                      
REMARK 465     LEU A   188                                                      
REMARK 465     SER A   189                                                      
REMARK 465     LYS A   190                                                      
REMARK 465     ILE A   191                                                      
REMARK 465     VAL A   192                                                      
REMARK 465     GLU A   193                                                      
REMARK 465     HIS A   194                                                      
REMARK 465     GLN A   195                                                      
REMARK 465     VAL A   196                                                      
REMARK 465     LEU A   197                                                      
REMARK 465     MET A   198                                                      
REMARK 465     LYS A   199                                                      
REMARK 465     THR A   200                                                      
REMARK 465     VAL A   201                                                      
REMARK 465     CYS A   202                                                      
REMARK 465     ARG A   338                                                      
REMARK 465     LEU A   339                                                      
REMARK 465     GLY A   340                                                      
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     ILE A  34    CG1  CG2  CD1                                       
REMARK 470     ASP A  35    CG   OD1  OD2                                       
REMARK 470     SER A  37    OG                                                  
REMARK 470     ARG A  39    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A  64    CE   NZ                                             
REMARK 470     LEU A  77    CG   CD1  CD2                                       
REMARK 470     LYS A  78    CD   CE   NZ                                        
REMARK 470     LYS A  79    CG   CD   CE   NZ                                   
REMARK 470     ILE A  90    CG1  CG2  CD1                                       
REMARK 470     VAL A  92    CG1  CG2                                            
REMARK 470     LEU A  93    CG   CD1  CD2                                       
REMARK 470     LEU A  94    CG   CD1  CD2                                       
REMARK 470     ARG A  95    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 103    CG   CD   CE   NZ                                   
REMARK 470     ARG A 139    NE   CZ   NH1  NH2                                  
REMARK 470     ARG A 163    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE A 186    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A 244    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 287    CE   NZ                                             
REMARK 470     THR A 301    OG1  CG2                                            
REMARK 470     LYS A 303    CG   CD   CE   NZ                                   
REMARK 470     ASN A 306    CG   OD1  ND2                                       
REMARK 470     LYS A 327    CG   CD   CE   NZ                                   
REMARK 470     LYS A 331    CD   CE   NZ                                        
REMARK 470     SER A 337    OG                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ARG A   163     O    HOH A  2047              2.10            
REMARK 500   O    HOH A  2064     O    HOH A  2065              2.14            
REMARK 500   O    HOH A  2047     O    HOH A  2048              2.16            
REMARK 500   OD1  ASP A   143     O    HOH A  2041              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    GLU A  49     -135.12   -119.97                                   
REMARK 500    THR A 112      -68.15    -93.53                                   
REMARK 500    ARG A 163       -6.92     71.40                                   
REMARK 500    ASP A 164       41.38   -143.37                                   
REMARK 500    THR A 301       38.62    -73.87                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR A   57     SER A   58                 -147.88                    
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 DKI A 1338                
DBREF  2W4O A   15   340  UNP    Q16566   KCC4_HUMAN      15    340             
SEQADV 2W4O MET A   -8  UNP  Q16566              EXPRESSION TAG                 
SEQADV 2W4O HIS A   -7  UNP  Q16566              EXPRESSION TAG                 
SEQADV 2W4O HIS A   -6  UNP  Q16566              EXPRESSION TAG                 
SEQADV 2W4O HIS A   -5  UNP  Q16566              EXPRESSION TAG                 
SEQADV 2W4O HIS A   -4  UNP  Q16566              EXPRESSION TAG                 
SEQADV 2W4O HIS A   -3  UNP  Q16566              EXPRESSION TAG                 
SEQADV 2W4O HIS A   -2  UNP  Q16566              EXPRESSION TAG                 
SEQADV 2W4O SER A   -1  UNP  Q16566              EXPRESSION TAG                 
SEQADV 2W4O SER A    0  UNP  Q16566              EXPRESSION TAG                 
SEQADV 2W4O GLY A    1  UNP  Q16566              EXPRESSION TAG                 
SEQADV 2W4O VAL A    2  UNP  Q16566              EXPRESSION TAG                 
SEQADV 2W4O ASP A    3  UNP  Q16566              EXPRESSION TAG                 
SEQADV 2W4O LEU A    4  UNP  Q16566              EXPRESSION TAG                 
SEQADV 2W4O GLY A    5  UNP  Q16566              EXPRESSION TAG                 
SEQADV 2W4O THR A    6  UNP  Q16566              EXPRESSION TAG                 
SEQADV 2W4O GLU A    7  UNP  Q16566              EXPRESSION TAG                 
SEQADV 2W4O ASN A    8  UNP  Q16566              EXPRESSION TAG                 
SEQADV 2W4O LEU A    9  UNP  Q16566              EXPRESSION TAG                 
SEQADV 2W4O TYR A   10  UNP  Q16566              EXPRESSION TAG                 
SEQADV 2W4O PHE A   11  UNP  Q16566              EXPRESSION TAG                 
SEQADV 2W4O GLN A   12  UNP  Q16566              EXPRESSION TAG                 
SEQADV 2W4O SER A   13  UNP  Q16566              EXPRESSION TAG                 
SEQADV 2W4O MET A   14  UNP  Q16566              EXPRESSION TAG                 
SEQRES   1 A  349  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  349  GLY THR GLU ASN LEU TYR PHE GLN SER MET SER SER VAL          
SEQRES   3 A  349  THR ALA SER ALA ALA PRO GLY THR ALA SER LEU VAL PRO          
SEQRES   4 A  349  ASP TYR TRP ILE ASP GLY SER ASN ARG ASP ALA LEU SER          
SEQRES   5 A  349  ASP PHE PHE GLU VAL GLU SER GLU LEU GLY ARG GLY ALA          
SEQRES   6 A  349  THR SER ILE VAL TYR ARG CYS LYS GLN LYS GLY THR GLN          
SEQRES   7 A  349  LYS PRO TYR ALA LEU LYS VAL LEU LYS LYS THR VAL ASP          
SEQRES   8 A  349  LYS LYS ILE VAL ARG THR GLU ILE GLY VAL LEU LEU ARG          
SEQRES   9 A  349  LEU SER HIS PRO ASN ILE ILE LYS LEU LYS GLU ILE PHE          
SEQRES  10 A  349  GLU THR PRO THR GLU ILE SER LEU VAL LEU GLU LEU VAL          
SEQRES  11 A  349  THR GLY GLY GLU LEU PHE ASP ARG ILE VAL GLU LYS GLY          
SEQRES  12 A  349  TYR TYR SER GLU ARG ASP ALA ALA ASP ALA VAL LYS GLN          
SEQRES  13 A  349  ILE LEU GLU ALA VAL ALA TYR LEU HIS GLU ASN GLY ILE          
SEQRES  14 A  349  VAL HIS ARG ASP LEU LYS PRO GLU ASN LEU LEU TYR ALA          
SEQRES  15 A  349  THR PRO ALA PRO ASP ALA PRO LEU LYS ILE ALA ASP PHE          
SEQRES  16 A  349  GLY LEU SER LYS ILE VAL GLU HIS GLN VAL LEU MET LYS          
SEQRES  17 A  349  THR VAL CYS GLY THR PRO GLY TYR CYS ALA PRO GLU ILE          
SEQRES  18 A  349  LEU ARG GLY CYS ALA TYR GLY PRO GLU VAL ASP MET TRP          
SEQRES  19 A  349  SER VAL GLY ILE ILE THR TYR ILE LEU LEU CYS GLY PHE          
SEQRES  20 A  349  GLU PRO PHE TYR ASP GLU ARG GLY ASP GLN PHE MET PHE          
SEQRES  21 A  349  ARG ARG ILE LEU ASN CYS GLU TYR TYR PHE ILE SER PRO          
SEQRES  22 A  349  TRP TRP ASP GLU VAL SER LEU ASN ALA LYS ASP LEU VAL          
SEQRES  23 A  349  ARG LYS LEU ILE VAL LEU ASP PRO LYS LYS ARG LEU THR          
SEQRES  24 A  349  THR PHE GLN ALA LEU GLN HIS PRO TRP VAL THR GLY LYS          
SEQRES  25 A  349  ALA ALA ASN PHE VAL HIS MET ASP THR ALA GLN LYS LYS          
SEQRES  26 A  349  LEU GLN GLU PHE ASN ALA ARG ARG LYS LEU LYS ALA ALA          
SEQRES  27 A  349  VAL LYS ALA VAL VAL ALA SER SER ARG LEU GLY                  
HET    DKI  A1338      28                                                       
HETNAM     DKI 5-AMINO-3-{[4-(AMINOSULFONYL)PHENYL]AMINO}-N-(2,6-               
HETNAM   2 DKI  DIFLUOROPHENYL)-1H-1,2,4-TRIAZOLE-1-CARBOTHIOAMIDE              
HETSYN     DKI CDK 1/2 INHIBITOR                                                
FORMUL   2  DKI    C15 H13 F2 N7 O2 S2                                          
FORMUL   3  HOH   *115(H2 O)                                                    
HELIX    1   1 ALA A   41  ASP A   44  5                                   4    
HELIX    2   2 ILE A   90  LEU A   96  1                                   7    
HELIX    3   3 GLU A  125  VAL A  131  1                                   7    
HELIX    4   4 SER A  137  ASN A  158  1                                  22    
HELIX    5   5 LYS A  166  GLU A  168  5                                   3    
HELIX    6   6 THR A  204  CYS A  208  5                                   5    
HELIX    7   7 ALA A  209  ARG A  214  1                                   6    
HELIX    8   8 PRO A  220  GLY A  237  1                                  18    
HELIX    9   9 GLY A  246  ASN A  256  1                                  11    
HELIX   10  10 SER A  270  LYS A  279  1                                  10    
HELIX   11  11 ASP A  284  ARG A  288  5                                   5    
HELIX   12  12 THR A  290  HIS A  297  1                                   8    
HELIX   13  13 MET A  310  SER A  336  1                                  27    
SHEET    1  AA 5 PHE A  46  ARG A  54  0                                        
SHEET    2  AA 5 SER A  58  GLN A  65 -1  O  VAL A  60   N  LEU A  52           
SHEET    3  AA 5 PRO A  71  LYS A  78 -1  O  TYR A  72   N  CYS A  63           
SHEET    4  AA 5 GLU A 113  LEU A 118 -1  O  ILE A 114   N  LEU A  77           
SHEET    5  AA 5 LEU A 104  GLU A 109 -1  N  LYS A 105   O  VAL A 117           
SHEET    1  AB 2 LEU A 170  TYR A 172  0                                        
SHEET    2  AB 2 LEU A 181  ILE A 183 -1  O  LYS A 182   N  LEU A 171           
CISPEP   1 SER A  263    PRO A  264          0         9.10                     
SITE     1 AC1 11 LEU A  52  GLY A  53  VAL A  60  GLU A 119                    
SITE     2 AC1 11 LEU A 120  VAL A 121  GLU A 168  LEU A 171                    
SITE     3 AC1 11 ALA A 184  ASP A 185  ARG A 245                               
CRYST1   42.400   70.810   99.151  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.023585  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014122  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010086        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system