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Database: PDB
Entry: 4F9C
LinkDB: 4F9C
Original site: 4F9C 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       18-MAY-12   4F9C              
TITLE     HUMAN CDC7 KINASE IN COMPLEX WITH DBF4 AND XL413                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION CYCLE 7-RELATED PROTEIN KINASE;              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CDC7-RELATED KINASE, HSCDC7, HUCDC7;                        
COMPND   5 EC: 2.7.11.1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PROTEIN DBF4 HOMOLOG A;                                    
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: ACTIVATOR OF S PHASE KINASE, CHIFFON HOMOLOG A, DBF4-TYPE   
COMPND  11 ZINC FINGER-CONTAINING PROTEIN 1;                                    
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CDC7, CDC7L1;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA-2(DE3);                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PRSF-DUET;                                
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: ASK, DBF4, DBF4A, ZDBF1;                                       
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: ROSETTA-2(DE3);                            
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PCDF-DUET                                 
KEYWDS    SER/THR PROTEIN KINASE, TRANSFERASE, PHOSPHORYLATION, CELL CYCLE,     
KEYWDS   2 CELL DIVISION, MITOSIS, S PHASE, SERINE/THREONINE-PROTEIN KINASE,    
KEYWDS   3 DBF4-DEPENDENT KINASE, DDK, ATP-BINDING, NUCLEOTIDE-BINDING, ZINC-   
KEYWDS   4 BINDING, NUCLEUS, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.HUGHES,P.CHEREPANOV                                                 
REVDAT   4   15-NOV-17 4F9C    1       REMARK                                   
REVDAT   3   16-AUG-17 4F9C    1       SOURCE REMARK                            
REVDAT   2   12-DEC-12 4F9C    1       JRNL                                     
REVDAT   1   31-OCT-12 4F9C    0                                                
JRNL        AUTH   S.HUGHES,F.ELUSTONDO,A.DI FONZO,F.G.LEROUX,A.C.WONG,         
JRNL        AUTH 2 A.P.SNIJDERS,S.J.MATTHEWS,P.CHEREPANOV                       
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN CDC7 KINASE IN COMPLEX WITH ITS   
JRNL        TITL 2 ACTIVATOR DBF4.                                              
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  19  1101 2012              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   23064647                                                     
JRNL        DOI    10.1038/NSMB.2404                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.08 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.08                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 59.74                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 28458                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1455                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.08                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.13                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1711                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.94                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 104                          
REMARK   3   BIN FREE R VALUE                    : 0.3030                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3177                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 21                                      
REMARK   3   SOLVENT ATOMS            : 81                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.91                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.24000                                              
REMARK   3    B22 (A**2) : 0.24000                                              
REMARK   3    B33 (A**2) : -0.47000                                             
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.209         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.184         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.123         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.524         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.927                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3270 ; 0.009 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4412 ; 1.180 ; 1.981       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   388 ; 5.763 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   152 ;34.340 ;24.276       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   588 ;15.925 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;18.119 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   489 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2435 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4F9C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAY-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000072618.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-OCT-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28512                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.080                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 61.270                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.08                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.13                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.60100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: DIRECT REFINEMENT                                     
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG-1500, 15% GLYCEROL, PH 7.5,      
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      119.47000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       30.63500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       30.63500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       59.73500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       30.63500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       30.63500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      179.20500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       30.63500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       30.63500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       59.73500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       30.63500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       30.63500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      179.20500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      119.47000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5480 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    36                                                      
REMARK 465     LEU A    37                                                      
REMARK 465     ALA A    38                                                      
REMARK 465     GLY A    39                                                      
REMARK 465     VAL A    40                                                      
REMARK 465     GLN A   347                                                      
REMARK 465     SER A   348                                                      
REMARK 465     GLU A   349                                                      
REMARK 465     ALA A   350                                                      
REMARK 465     GLN A   351                                                      
REMARK 465     GLN A   352                                                      
REMARK 465     GLU A   353                                                      
REMARK 465     ARG A   354                                                      
REMARK 465     CYS A   355                                                      
REMARK 465     SER A   356                                                      
REMARK 465     GLN A   357                                                      
REMARK 465     ASN A   358                                                      
REMARK 465     LYS A   359                                                      
REMARK 465     CYS A   360                                                      
REMARK 465     SER A   361                                                      
REMARK 465     ILE A   362                                                      
REMARK 465     CYS A   363                                                      
REMARK 465     LEU A   364                                                      
REMARK 465     SER A   365                                                      
REMARK 465     ARG A   366                                                      
REMARK 465     ARG A   367                                                      
REMARK 465     GLN A   368                                                      
REMARK 465     GLN A   369                                                      
REMARK 465     VAL A   370                                                      
REMARK 465     ALA A   371                                                      
REMARK 465     PRO A   372                                                      
REMARK 465     GLY A   513                                                      
REMARK 465     MET A   514                                                      
REMARK 465     ASP A   515                                                      
REMARK 465     SER A   516                                                      
REMARK 465     SER A   517                                                      
REMARK 465     THR A   518                                                      
REMARK 465     PRO A   519                                                      
REMARK 465     LYS A   520                                                      
REMARK 465     LEU A   521                                                      
REMARK 465     THR A   522                                                      
REMARK 465     SER A   523                                                      
REMARK 465     ASP A   524                                                      
REMARK 465     ILE A   525                                                      
REMARK 465     GLN A   526                                                      
REMARK 465     GLY A   527                                                      
REMARK 465     HIS A   528                                                      
REMARK 465     ALA A   529                                                      
REMARK 465     THR A   530                                                      
REMARK 465     ASN A   531                                                      
REMARK 465     LEU A   532                                                      
REMARK 465     GLU A   533                                                      
REMARK 465     GLY A   534                                                      
REMARK 465     SER A   573                                                      
REMARK 465     LEU A   574                                                      
REMARK 465     GLY B   207                                                      
REMARK 465     PRO B   208                                                      
REMARK 465     GLY B   209                                                      
REMARK 465     THR B   210                                                      
REMARK 465     ARG B   211                                                      
REMARK 465     THR B   212                                                      
REMARK 465     GLY B   213                                                      
REMARK 465     LEU B   228                                                      
REMARK 465     TYR B   229                                                      
REMARK 465     VAL B   255                                                      
REMARK 465     ASP B   256                                                      
REMARK 465     LYS B   257                                                      
REMARK 465     PRO B   258                                                      
REMARK 465     SER B   259                                                      
REMARK 465     SER B   260                                                      
REMARK 465     MET B   261                                                      
REMARK 465     GLN B   262                                                      
REMARK 465     LYS B   263                                                      
REMARK 465     GLN B   264                                                      
REMARK 465     THR B   265                                                      
REMARK 465     GLN B   266                                                      
REMARK 465     VAL B   267                                                      
REMARK 465     LYS B   268                                                      
REMARK 465     LEU B   269                                                      
REMARK 465     ARG B   270                                                      
REMARK 465     ILE B   271                                                      
REMARK 465     GLN B   272                                                      
REMARK 465     THR B   273                                                      
REMARK 465     ASP B   274                                                      
REMARK 465     GLY B   275                                                      
REMARK 465     ASP B   276                                                      
REMARK 465     LYS B   277                                                      
REMARK 465     TYR B   278                                                      
REMARK 465     GLY B   279                                                      
REMARK 465     GLY B   280                                                      
REMARK 465     THR B   281                                                      
REMARK 465     SER B   282                                                      
REMARK 465     ILE B   283                                                      
REMARK 465     GLN B   284                                                      
REMARK 465     LEU B   285                                                      
REMARK 465     GLN B   286                                                      
REMARK 465     LEU B   287                                                      
REMARK 465     LYS B   288                                                      
REMARK 465     GLU B   289                                                      
REMARK 465     LYS B   290                                                      
REMARK 465     LYS B   291                                                      
REMARK 465     LYS B   292                                                      
REMARK 465     LYS B   293                                                      
REMARK 465     LYS B   343                                                      
REMARK 465     ASP B   344                                                      
REMARK 465     THR B   345                                                      
REMARK 465     PRO B   346                                                      
REMARK 465     LYS B   347                                                      
REMARK 465     LYS B   348                                                      
REMARK 465     LYS B   349                                                      
REMARK 465     ARG B   350                                                      
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 B 316    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU B 342    CG   CD   OE1  OE2                                  
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    PRO A  94        6.07    -64.98                                   
REMARK 500    ASN A 127     -116.23     52.22                                   
REMARK 500    ARG A 176       -1.33     73.79                                   
REMARK 500    ASP A 177       41.97   -145.34                                   
REMARK 500    ASP A 196       87.08     79.42                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 309   NE2                                                    
REMARK 620 2 HIS B 315   ND1 103.6                                              
REMARK 620 3 CYS B 299   SG  121.1 113.1                                        
REMARK 620 4 CYS B 296   SG   90.6 112.9 113.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0SX A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 401                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4F99   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4F9A   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4F9B   RELATED DB: PDB                                   
DBREF  4F9C A   37   359  UNP    O00311   CDC7_HUMAN      37    227             
DBREF  4F9C A  360   529  UNP    O00311   CDC7_HUMAN     360    483             
DBREF  4F9C A  530   574  UNP    O00311   CDC7_HUMAN     530    574             
DBREF  4F9C B  210   350  UNP    Q9UBU7   DBF4A_HUMAN    210    350             
SEQADV 4F9C MET A   36  UNP  O00311              EXPRESSION TAG                 
SEQADV 4F9C GLY B  207  UNP  Q9UBU7              EXPRESSION TAG                 
SEQADV 4F9C PRO B  208  UNP  Q9UBU7              EXPRESSION TAG                 
SEQADV 4F9C GLY B  209  UNP  Q9UBU7              EXPRESSION TAG                 
SEQRES   1 A  361  MET LEU ALA GLY VAL LYS LYS ASP ILE GLU LYS LEU TYR          
SEQRES   2 A  361  GLU ALA VAL PRO GLN LEU SER ASN VAL PHE LYS ILE GLU          
SEQRES   3 A  361  ASP LYS ILE GLY GLU GLY THR PHE SER SER VAL TYR LEU          
SEQRES   4 A  361  ALA THR ALA GLN LEU GLN VAL GLY PRO GLU GLU LYS ILE          
SEQRES   5 A  361  ALA LEU LYS HIS LEU ILE PRO THR SER HIS PRO ILE ARG          
SEQRES   6 A  361  ILE ALA ALA GLU LEU GLN CYS LEU THR VAL ALA GLY GLY          
SEQRES   7 A  361  GLN ASP ASN VAL MET GLY VAL LYS TYR CYS PHE ARG LYS          
SEQRES   8 A  361  ASN ASP HIS VAL VAL ILE ALA MET PRO TYR LEU GLU HIS          
SEQRES   9 A  361  GLU SER PHE LEU ASP ILE LEU ASN SER LEU SER PHE GLN          
SEQRES  10 A  361  GLU VAL ARG GLU TYR MET LEU ASN LEU PHE LYS ALA LEU          
SEQRES  11 A  361  LYS ARG ILE HIS GLN PHE GLY ILE VAL HIS ARG ASP VAL          
SEQRES  12 A  361  LYS PRO SER ASN PHE LEU TYR ASN ARG ARG LEU LYS LYS          
SEQRES  13 A  361  TYR ALA LEU VAL ASP PHE GLY LEU ALA GLN GLY THR HIS          
SEQRES  14 A  361  ASP THR LYS ILE GLU LEU LEU LYS PHE VAL GLN SER GLU          
SEQRES  15 A  361  ALA GLN GLN GLU ARG CYS SER GLN ASN LYS CYS SER ILE          
SEQRES  16 A  361  CYS LEU SER ARG ARG GLN GLN VAL ALA PRO ARG ALA GLY          
SEQRES  17 A  361  THR PRO GLY PHE ARG ALA PRO GLU VAL LEU THR LYS CYS          
SEQRES  18 A  361  PRO ASN GLN THR THR ALA ILE ASP MET TRP SER ALA GLY          
SEQRES  19 A  361  VAL ILE PHE LEU SER LEU LEU SER GLY ARG TYR PRO PHE          
SEQRES  20 A  361  TYR LYS ALA SER ASP ASP LEU THR ALA LEU ALA GLN ILE          
SEQRES  21 A  361  MET THR ILE ARG GLY SER ARG GLU THR ILE GLN ALA ALA          
SEQRES  22 A  361  LYS THR PHE GLY LYS SER ILE LEU CYS SER LYS GLU VAL          
SEQRES  23 A  361  PRO ALA GLN ASP LEU ARG LYS LEU CYS GLU ARG LEU ARG          
SEQRES  24 A  361  GLY MET ASP SER SER THR PRO LYS LEU THR SER ASP ILE          
SEQRES  25 A  361  GLN GLY HIS ALA THR ASN LEU GLU GLY TRP ASN GLU VAL          
SEQRES  26 A  361  PRO ASP GLU ALA TYR ASP LEU LEU ASP LYS LEU LEU ASP          
SEQRES  27 A  361  LEU ASN PRO ALA SER ARG ILE THR ALA GLU GLU ALA LEU          
SEQRES  28 A  361  LEU HIS PRO PHE PHE LYS ASP MET SER LEU                      
SEQRES   1 B  144  GLY PRO GLY THR ARG THR GLY ARG LEU LYS LYS PRO PHE          
SEQRES   2 B  144  VAL LYS VAL GLU ASP MET SER GLN LEU TYR ARG PRO PHE          
SEQRES   3 B  144  TYR LEU GLN LEU THR ASN MET PRO PHE ILE ASN TYR SER          
SEQRES   4 B  144  ILE GLN LYS PRO CYS SER PRO PHE ASP VAL ASP LYS PRO          
SEQRES   5 B  144  SER SER MET GLN LYS GLN THR GLN VAL LYS LEU ARG ILE          
SEQRES   6 B  144  GLN THR ASP GLY ASP LYS TYR GLY GLY THR SER ILE GLN          
SEQRES   7 B  144  LEU GLN LEU LYS GLU LYS LYS LYS LYS GLY TYR CYS GLU          
SEQRES   8 B  144  CYS CYS LEU GLN LYS TYR GLU ASP LEU GLU THR HIS LEU          
SEQRES   9 B  144  LEU SER GLU GLN HIS ARG ASN PHE ALA GLN SER ASN GLN          
SEQRES  10 B  144  TYR GLN VAL VAL ASP ASP ILE VAL SER LYS LEU VAL PHE          
SEQRES  11 B  144  ASP PHE VAL GLU TYR GLU LYS ASP THR PRO LYS LYS LYS          
SEQRES  12 B  144  ARG                                                          
HET    0SX  A 601      20                                                       
HET     ZN  B 401       1                                                       
HETNAM     0SX 8-CHLORO-2-[(2S)-PYRROLIDIN-2-YL][1]BENZOFURO[3,2-               
HETNAM   2 0SX  D]PYRIMIDIN-4(3H)-ONE                                           
HETNAM      ZN ZINC ION                                                         
FORMUL   3  0SX    C14 H12 CL N3 O2                                             
FORMUL   4   ZN    ZN 2+                                                        
FORMUL   5  HOH   *81(H2 O)                                                     
HELIX    1   1 LYS A   41  VAL A   51  1                                  11    
HELIX    2   2 PRO A   52  VAL A   57  5                                   6    
HELIX    3   3 HIS A   97  ALA A  111  1                                  15    
HELIX    4   4 SER A  141  ASN A  147  1                                   7    
HELIX    5   5 SER A  150  PHE A  171  1                                  22    
HELIX    6   6 LYS A  179  SER A  181  5                                   3    
HELIX    7   7 ILE A  208  VAL A  214  5                                   7    
HELIX    8   8 THR A  376  ARG A  380  5                                   5    
HELIX    9   9 ALA A  381  THR A  386  1                                   6    
HELIX   10  10 THR A  393  GLY A  410  1                                  18    
HELIX   11  11 ASP A  419  GLY A  432  1                                  14    
HELIX   12  12 GLY A  432  PHE A  443  1                                  12    
HELIX   13  13 ASP A  457  ARG A  466  1                                  10    
HELIX   14  14 PRO A  539  LEU A  550  1                                  12    
HELIX   15  15 THR A  559  LEU A  565  1                                   7    
HELIX   16  16 HIS A  566  LYS A  570  5                                   5    
HELIX   17  17 ASP B  305  SER B  312  1                                   8    
HELIX   18  18 SER B  312  GLN B  320  1                                   9    
HELIX   19  19 TYR B  324  SER B  332  1                                   9    
SHEET    1   A 5 LYS A  59  GLU A  66  0                                        
SHEET    2   A 5 SER A  70  GLN A  78 -1  O  LEU A  74   N  ASP A  62           
SHEET    3   A 5 GLU A  84  LEU A  92 -1  O  ILE A  87   N  ALA A  75           
SHEET    4   A 5 HIS A 129  PRO A 135 -1  O  ILE A 132   N  LYS A  90           
SHEET    5   A 5 TYR A 122  LYS A 126 -1  N  PHE A 124   O  VAL A 131           
SHEET    1   B 2 ILE A 173  VAL A 174  0                                        
SHEET    2   B 2 GLN A 201  GLY A 202 -1  O  GLN A 201   N  VAL A 174           
SHEET    1   C 2 PHE A 183  ASN A 186  0                                        
SHEET    2   C 2 LYS A 191  LEU A 194 -1  O  LYS A 191   N  ASN A 186           
SHEET    1   D 3 LYS A 445  CYS A 449  0                                        
SHEET    2   D 3 PHE B 219  ASP B 224 -1  O  GLU B 223   N  SER A 446           
SHEET    3   D 3 PHE B 232  GLN B 235 -1  O  PHE B 232   N  VAL B 222           
SHEET    1   E 2 TYR B 295  CYS B 296  0                                        
SHEET    2   E 2 GLN B 301  LYS B 302 -1  O  GLN B 301   N  CYS B 296           
LINK         NE2 HIS B 309                ZN    ZN B 401     1555   1555  2.15  
LINK         ND1 HIS B 315                ZN    ZN B 401     1555   1555  2.16  
LINK         SG  CYS B 299                ZN    ZN B 401     1555   1555  2.34  
LINK         SG  CYS B 296                ZN    ZN B 401     1555   1555  2.35  
CISPEP   1 TYR A  412    PRO A  413          0        -6.60                     
CISPEP   2 LYS A  570    ASP A  571          0       -13.24                     
CISPEP   3 LYS B  217    PRO B  218          0        -0.85                     
CISPEP   4 LYS B  248    PRO B  249          0         3.14                     
SITE     1 AC1 15 SER A  70  VAL A  72  ALA A  88  LYS A  90                    
SITE     2 AC1 15 MET A 118  MET A 134  PRO A 135  TYR A 136                    
SITE     3 AC1 15 LEU A 137  ASN A 182  LEU A 184  VAL A 195                    
SITE     4 AC1 15 ASP A 196  HOH A 731  HOH A 766                               
SITE     1 AC2  4 CYS B 296  CYS B 299  HIS B 309  HIS B 315                    
CRYST1   61.270   61.270  238.940  90.00  90.00  90.00 P 41 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016321  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016321  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004185        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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