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Database: PDB
Entry: 4D1Z
LinkDB: 4D1Z
Original site: 4D1Z 
HEADER    TRANSFERASE                             05-MAY-14   4D1Z              
TITLE     CDK2 IN COMPLEX WITH A LUCIFERIN DERIVATE                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 2;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: KINASE DOMAIN, RESIDUES 1-298;                             
COMPND   5 SYNONYM: CELL DIVISION PROTEIN KINASE 2, P33 PROTEIN KINASE;         
COMPND   6 EC: 2.7.11.22;                                                       
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: 562                                         
KEYWDS    TRANSFERASE, CDK2, KINASE                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    U.ROTHWEILER,R.A.ENGH                                                 
REVDAT   3   02-SEP-15 4D1Z    1       COMPND                                   
REVDAT   2   25-MAR-15 4D1Z    1       JRNL                                     
REVDAT   1   18-MAR-15 4D1Z    0                                                
JRNL        AUTH   U.ROTHWEILER,J.ERIKSSON,W.STENSEN,F.LEESON,R.A.ENGH,         
JRNL        AUTH 2 J.S.SVENDSEN                                                 
JRNL        TITL   LUCIFERIN AND DERIVATIVES AS A DYRK SELECTIVE SCAFFOLD FOR   
JRNL        TITL 2 THE DESIGN OF PROTEIN KINASE INHIBITORS.                     
JRNL        REF    EUR.J.MED.CHEM.               V.  94   140 2015              
JRNL        REFN                   ISSN 0223-5234                               
JRNL        PMID   25768698                                                     
JRNL        DOI    10.1016/J.EJMECH.2015.02.035                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
REMARK   3   AUTHORS     : ADAMS,AFONINE,BURNLEY,CHEN,DAVIS,ECHOLS,GILDEA,      
REMARK   3               : GOPAL,GROS,GROSSE-KUNSTLEVE,HEADD,HUNG,IMMORMINO,    
REMARK   3               : IOERGER,MCCOY,MCKEE,MORIARTY,PAI,READ,RICHARDSON,    
REMARK   3               : RICHARDSON,ROMO,SACCHETTINI,SAUTER,SMITH,STORONI,    
REMARK   3               : TERWILLIGER,ZWART                                    
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.851                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.227                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.99                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.05                          
REMARK   3   NUMBER OF REFLECTIONS             : 24725                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1949                          
REMARK   3   R VALUE            (WORKING SET) : 0.1933                          
REMARK   3   FREE R VALUE                     : 0.2254                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1261                            
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 30.2311 -  3.8485    0.99     2766   148  0.2031 0.2110        
REMARK   3     2  3.8485 -  3.0556    0.99     2665   125  0.1724 0.2062        
REMARK   3     3  3.0556 -  2.6697    1.00     2636   138  0.1864 0.2089        
REMARK   3     4  2.6697 -  2.4257    1.00     2607   139  0.1816 0.2402        
REMARK   3     5  2.4257 -  2.2519    0.99     2576   149  0.1799 0.2257        
REMARK   3     6  2.2519 -  2.1192    0.99     2592   146  0.1909 0.2238        
REMARK   3     7  2.1192 -  2.0130    0.99     2546   149  0.2100 0.2886        
REMARK   3     8  2.0130 -  1.9254    0.99     2581   135  0.2278 0.2733        
REMARK   3     9  1.9254 -  1.8513    0.96     2495   132  0.2457 0.2870        
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)     : 0.19             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.27            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.18                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.008           2109                                  
REMARK   3   ANGLE     :  1.220           2868                                  
REMARK   3   CHIRALITY :  0.069            323                                  
REMARK   3   PLANARITY :  0.007            359                                  
REMARK   3   DIHEDRAL  : 13.165            775                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 3 THROUGH 35 )                      
REMARK   3    ORIGIN FOR THE GROUP (A):  18.1477 -17.3156  13.5868              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2553 T22:   0.4726                                     
REMARK   3      T33:   0.3805 T12:   0.0920                                     
REMARK   3      T13:   0.0018 T23:   0.0651                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2978 L22:   2.0019                                     
REMARK   3      L33:   7.8549 L12:   6.6770                                     
REMARK   3      L13:  -4.5666 L23:  -2.9534                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3698 S12:   0.6016 S13:  -0.0950                       
REMARK   3      S21:  -0.4238 S22:   0.1210 S23:  -0.5968                       
REMARK   3      S31:   0.5670 S32:   0.4000 S33:   0.2449                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 48 THROUGH 72 )                     
REMARK   3    ORIGIN FOR THE GROUP (A):  21.4910  -5.4907  23.3066              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2683 T22:   0.3653                                     
REMARK   3      T33:   0.3921 T12:  -0.0039                                     
REMARK   3      T13:   0.0083 T23:   0.0166                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0013 L22:   5.3963                                     
REMARK   3      L33:   4.4865 L12:  -6.1875                                     
REMARK   3      L13:  -5.0310 L23:   2.7425                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1392 S12:  -0.6776 S13:   0.7935                       
REMARK   3      S21:  -0.0741 S22:   0.2613 S23:  -0.8442                       
REMARK   3      S31:  -0.2868 S32:   0.8299 S33:  -0.4041                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 75 THROUGH 147 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):   7.7874  -1.1287  16.3678              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2006 T22:   0.1345                                     
REMARK   3      T33:   0.2063 T12:  -0.0027                                     
REMARK   3      T13:   0.0446 T23:   0.0737                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5719 L22:   2.9223                                     
REMARK   3      L33:   2.0877 L12:  -1.8173                                     
REMARK   3      L13:   0.6350 L23:   0.1980                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0393 S12:   0.1387 S13:  -0.3190                       
REMARK   3      S21:  -0.1078 S22:  -0.0804 S23:  -0.1232                       
REMARK   3      S31:   0.1960 S32:   0.2738 S33:   0.0386                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 165 THROUGH 295 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   7.5102  16.2031   9.8614              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1398 T22:   0.0614                                     
REMARK   3      T33:   0.1068 T12:   0.0288                                     
REMARK   3      T13:  -0.0072 T23:  -0.0162                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4452 L22:   3.0767                                     
REMARK   3      L33:   2.8244 L12:   2.2945                                     
REMARK   3      L13:  -2.0592 L23:  -1.5644                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0921 S12:   0.0080 S13:   0.1007                       
REMARK   3      S21:  -0.0416 S22:  -0.0020 S23:   0.0839                       
REMARK   3      S31:  -0.1233 S32:   0.0361 S33:  -0.0783                       
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 4D1Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-MAY-14.                  
REMARK 100 THE PDBE ID CODE IS EBI-60562.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-JUN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
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) : 0.91841                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (MX-225)                       
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24735                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.85                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.8                                
REMARK 200  R MERGE                    (I) : 0.05                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.90                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.89                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.40                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2R3R                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.1                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0 MM HEPES, 20 MM NACL, PH 7.4           
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       26.91500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       36.53000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.20000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       36.53000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.91500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.20000            
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: PISA                                                  
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     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     GLU A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     THR A    14                                                      
REMARK 465     TYR A    15                                                      
REMARK 465     ARG A    36                                                      
REMARK 465     LEU A    37                                                      
REMARK 465     ASP A    38                                                      
REMARK 465     THR A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 465     THR A    41                                                      
REMARK 465     GLU A    42                                                      
REMARK 465     GLY A    43                                                      
REMARK 465     VAL A    44                                                      
REMARK 465     PRO A    45                                                      
REMARK 465     SER A    46                                                      
REMARK 465     THR A    47                                                      
REMARK 465     GLU A    73                                                      
REMARK 465     ASN A    74                                                      
REMARK 465     LEU A   148                                                      
REMARK 465     ALA A   149                                                      
REMARK 465     ARG A   150                                                      
REMARK 465     ALA A   151                                                      
REMARK 465     PHE A   152                                                      
REMARK 465     GLY A   153                                                      
REMARK 465     VAL A   154                                                      
REMARK 465     PRO A   155                                                      
REMARK 465     VAL A   156                                                      
REMARK 465     ARG A   157                                                      
REMARK 465     THR A   158                                                      
REMARK 465     TYR A   159                                                      
REMARK 465     THR A   160                                                      
REMARK 465     HIS A   161                                                      
REMARK 465     GLU A   162                                                      
REMARK 465     VAL A   163                                                      
REMARK 465     VAL A   164                                                      
REMARK 465     LEU A   296                                                      
REMARK 465     ARG A   297                                                      
REMARK 465     LEU A   298                                                      
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     LYS A   6    CG   CD   CE   NZ                                   
REMARK 470     LYS A   9    CG   CD   CE   NZ                                   
REMARK 470     LEU A  25    CG   CD1  CD2                                       
REMARK 470     LYS A  34    CG   CD   CE   NZ                                   
REMARK 470     ARG A  50    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  51    CG   CD   OE1  OE2                                  
REMARK 470     LEU A  54    CG   CD1  CD2                                       
REMARK 470     LEU A  55    CG   CD1  CD2                                       
REMARK 470     GLU A  57    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  75    CG   CD   CE   NZ                                   
REMARK 470     LEU A  96    CG   CD1  CD2                                       
REMARK 470     ARG A 122    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 246    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 247    CG   OD1  OD2                                       
REMARK 470     LYS A 278    CD   CE   NZ                                        
REMARK 470     HIS A 295    CG   ND1  CD2  CE1  NE2                             
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   NH1  ARG A   169     O    HOH A  2069              2.18            
REMARK 500   HD1  HIS A   268     OXT  WG8 A  1297              1.59            
REMARK 500   O    HOH A  2004     O    HOH A  2005              2.08            
REMARK 500   O    HOH A  2031     O    HOH A  2078              2.18            
REMARK 500   O    HOH A  2051     O    HOH A  2118              2.15            
REMARK 500   O    HOH A  2117     O    HOH A  2118              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OG   SER A   249     O    HOH A  2085     4455     2.00            
REMARK 500   HG   SER A   249     O    HOH A  2085     4455     1.57            
REMARK 500   O    HOH A  2008     O    HOH A  2113     3545     2.06            
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    ARG A 126      -11.60     68.31                                   
REMARK 500    TYR A 179       67.04   -117.79                                   
REMARK 500    PHE A 248      -21.81     78.63                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2007        DISTANCE =  5.78 ANGSTROMS                       
REMARK 525    HOH A2033        DISTANCE =  5.06 ANGSTROMS                       
REMARK 525    HOH A2045        DISTANCE =  6.31 ANGSTROMS                       
REMARK 525    HOH A2138        DISTANCE =  5.20 ANGSTROMS                       
REMARK 525    HOH A2139        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH A2140        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH A2141        DISTANCE =  6.90 ANGSTROMS                       
REMARK 525    HOH A2142        DISTANCE =  6.32 ANGSTROMS                       
REMARK 525    HOH A2143        DISTANCE =  6.94 ANGSTROMS                       
REMARK 525    HOH A2144        DISTANCE =  5.70 ANGSTROMS                       
REMARK 525    HOH A2145        DISTANCE =  5.35 ANGSTROMS                       
REMARK 525    HOH A2146        DISTANCE =  8.99 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WG8 A1296                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WG8 A1297                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4D1X   RELATED DB: PDB                                   
REMARK 900  CDK2 IN COMPLEX WITH LUCIFERIN                                      
DBREF  4D1Z A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
SEQRES   1 A  298  MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY          
SEQRES   2 A  298  THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR          
SEQRES   3 A  298  GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR          
SEQRES   4 A  298  GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 A  298  SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS          
SEQRES   6 A  298  LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU          
SEQRES   7 A  298  VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET          
SEQRES   8 A  298  ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE          
SEQRES   9 A  298  LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE          
SEQRES  10 A  298  CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  11 A  298  GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU          
SEQRES  12 A  298  ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL          
SEQRES  13 A  298  ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP TYR ARG          
SEQRES  14 A  298  ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR          
SEQRES  15 A  298  ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU          
SEQRES  16 A  298  MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU          
SEQRES  17 A  298  ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR          
SEQRES  18 A  298  PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO          
SEQRES  19 A  298  ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP          
SEQRES  20 A  298  PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG          
SEQRES  21 A  298  SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS          
SEQRES  22 A  298  ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE          
SEQRES  23 A  298  GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU              
HET    WG8  A1296      28                                                       
HET    WG8  A1297      28                                                       
HETNAM     WG8 (4S)-2-(8-HYDROXYQUINOLIN-2-YL)-4,5-DIHYDRO-                     
HETNAM   2 WG8  1,3-THIAZOLE-4-CARBOXYLIC ACID                                  
FORMUL   2  WG8    2(C13 H10 N2 O3 S)                                           
FORMUL   3  HOH   *146(H2 O)                                                    
HELIX    1   1 ALA A   48  LEU A   58  1                                  11    
HELIX    2   2 LEU A   87  SER A   94  1                                   8    
HELIX    3   3 PRO A  100  HIS A  121  1                                  22    
HELIX    4   4 LYS A  129  GLN A  131  5                                   3    
HELIX    5   5 ALA A  170  LEU A  175  1                                   6    
HELIX    6   6 THR A  182  ARG A  199  1                                  18    
HELIX    7   7 SER A  207  GLY A  220  1                                  14    
HELIX    8   8 GLY A  229  MET A  233  5                                   5    
HELIX    9   9 ASP A  256  LEU A  267  1                                  12    
HELIX   10  10 SER A  276  ALA A  282  1                                   7    
HELIX   11  11 HIS A  283  GLN A  287  5                                   5    
SHEET    1  AA 5 PHE A   4  GLY A  11  0                                        
SHEET    2  AA 5 VAL A  17  ASN A  23 -1  O  VAL A  18   N  ILE A  10           
SHEET    3  AA 5 VAL A  29  ILE A  35 -1  O  VAL A  30   N  ALA A  21           
SHEET    4  AA 5 LEU A  76  GLU A  81 -1  O  LEU A  76   N  ILE A  35           
SHEET    5  AA 5 LEU A  66  HIS A  71 -1  N  LEU A  67   O  VAL A  79           
SHEET    1  AB 3 GLN A  85  ASP A  86  0                                        
SHEET    2  AB 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3  AB 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
CISPEP   1 PRO A  253    PRO A  254          0         4.56                     
SITE     1 AC1  7 ILE A  10  LYS A  33  PHE A  80  PHE A  82                    
SITE     2 AC1  7 LEU A  83  LEU A 134  ASP A 145                               
SITE     1 AC2  7 LEU A 219  THR A 221  ARG A 245  HIS A 268                    
SITE     2 AC2  7 TYR A 269  VAL A 293  HOH A2096                               
CRYST1   53.830   72.400   73.060  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      0.018577  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013812  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013687        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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