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Database: PDB
Entry: 3FVH
LinkDB: 3FVH
Original site: 3FVH 
HEADER    CELL CYCLE, PEPTIDE BINDING PROTEIN     15-JAN-09   3FVH              
TITLE     POLO-LIKE KINASE 1 POLO BOX DOMAIN IN COMPLEX WITH AC-LHSPTA-NH2      
TITLE    2 PEPTIDE                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK1;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: POLO-LIKE KINASE 1, PLK-1, SERINE/THREONINE-PROTEIN KINASE  
COMPND   5 13, STPK13;                                                          
COMPND   6 EC: 2.7.11.21;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: ACETYL-LEU-HIS-SER-PHOSPHOTHR-ALA-NH2 PEPTIDE;             
COMPND  10 CHAIN: B;                                                            
COMPND  11 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: PLK, PLK1;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2;                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED                
KEYWDS    POLO LIKE KINASE 1, POLO BOX DOMAIN, PHOSPHOPEPTIDE BINDING DOMAIN,   
KEYWDS   2 ATP-BINDING, CELL CYCLE, CELL DIVISION, KINASE, MITOSIS, NUCLEOTIDE- 
KEYWDS   3 BINDING, NUCLEUS, PHOSPHOPROTEIN, SERINE/THREONINE-PROTEIN KINASE,   
KEYWDS   4 TRANSFERASE, PEPTIDE BINDING PROTEIN                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.C.LIM,M.B.YAFFE                                                     
REVDAT   3   02-FEB-11 3FVH    1       KEYWDS                                   
REVDAT   2   01-SEP-09 3FVH    1       JRNL                                     
REVDAT   1   04-AUG-09 3FVH    0                                                
JRNL        AUTH   S.M.YUN,T.MOULAEI,D.LIM,J.K.BANG,J.E.PARK,S.R.SHENOY,F.LIU,  
JRNL        AUTH 2 Y.H.KANG,C.LIAO,N.K.SOUNG,S.LEE,D.Y.YOON,Y.LIM,D.H.LEE,      
JRNL        AUTH 3 A.OTAKA,E.APPELLA,J.B.MCMAHON,M.C.NICKLAUS,T.R.BURKE,        
JRNL        AUTH 4 M.B.YAFFE,A.WLODAWER,K.S.LEE                                 
JRNL        TITL   STRUCTURAL AND FUNCTIONAL ANALYSES OF MINIMAL                
JRNL        TITL 2 PHOSPHOPEPTIDES TARGETING THE POLO-BOX DOMAIN OF POLO-LIKE   
JRNL        TITL 3 KINASE 1                                                     
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  16   876 2009              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   19597481                                                     
JRNL        DOI    10.1038/NSMB.1628                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.58 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.58                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.17                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.320                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 28941                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1417                            
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 24.1734 -  3.4019    0.91     2624   153  0.1689 0.1596        
REMARK   3     2  3.4019 -  2.7014    1.00     2894   132  0.1792 0.2540        
REMARK   3     3  2.7014 -  2.3602    0.99     2819   158  0.1979 0.2446        
REMARK   3     4  2.3602 -  2.1446    0.98     2750   158  0.1938 0.2401        
REMARK   3     5  2.1446 -  1.9909    0.98     2810   147  0.1925 0.2442        
REMARK   3     6  1.9909 -  1.8736    0.96     2741   137  0.2236 0.2629        
REMARK   3     7  1.8736 -  1.7798    0.96     2767   113  0.1998 0.2689        
REMARK   3     8  1.7798 -  1.7024    0.96     2719   131  0.1990 0.2395        
REMARK   3     9  1.7024 -  1.6368    0.95     2702   154  0.2019 0.2766        
REMARK   3    10  1.6368 -  1.5804    0.94     2698   134  0.2009 0.2730        
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              : 0.40                                          
REMARK   3   B_SOL              : 48.96                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.80                          
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 3FVH COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB051092.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-NOV-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : OSMIC MIRRORS                      
REMARK 200  OPTICS                         : OSMIC                              
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28949                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.580                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.17200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 8.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1UMW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 2000 MME, TRIS PH 8.5, TRIMETHYL-    
REMARK 280  AMINE OXIDE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       31.20600            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 970 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 12200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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     GLY A   367                                                      
REMARK 465     ALA A   368                                                      
REMARK 465     HIS A   369                                                      
REMARK 465     MET A   370                                                      
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   HE1  MET A   586     HZ2  LYS A   589              1.60            
REMARK 500   HG1  THR A   513     O    HOH A   128              1.71            
REMARK 500   HZ3  LYS A   492     O    HOH A   180              1.81            
REMARK 500   HE   ARG A   441     O    LEU A   511              1.82            
REMARK 500   HZ1  LYS A   540     O2P  TPO B     5              1.83            
REMARK 500  HH22  ARG A   500     O    HOH A    61              1.83            
REMARK 500   HZ2  LYS A   413     O    HOH A    19              1.86            
REMARK 500   OD2  ASP A   438     HZ1  LYS A   475              1.87            
REMARK 500   HE   ARG A   594     O    HOH A   226              1.88            
REMARK 500   HG1  THR A   585     O    HOH A   148              1.89            
REMARK 500   H    ASP A   402     O    THR A   561              1.89            
REMARK 500   OE2  GLU A   460    HH12  ARG A   507              1.90            
REMARK 500   OE1  GLN A   397     H    CYS A   573              1.91            
REMARK 500   O    GLU A   455     H    GLY A   458              1.91            
REMARK 500   HD3  ARG A   483     O    HOH A   106              1.92            
REMARK 500   HZ2  LYS A   475     O    HOH A    67              1.92            
REMARK 500   O    VAL A   530     H    LEU A   543              1.92            
REMARK 500   O    VAL A   550     H    TYR A   562              1.93            
REMARK 500   HZ3  LYS A   540     O    HOH A     9              1.95            
REMARK 500   H    LEU A   523     O    GLN A   531              1.95            
REMARK 500   O    LEU A   566     H    TYR A   570              1.95            
REMARK 500   O    VAL A   432     H    LEU A   444              1.96            
REMARK 500   H    ARG A   396     O    TYR A   570              1.96            
REMARK 500   O    LEU A   378     H    HIS A   382              1.96            
REMARK 500  HD22  ASN A   533     O    HOH B     8              1.96            
REMARK 500   H    ASP A   416     O    LEU B     2              1.97            
REMARK 500  HD22  ASN A   385     O    HOH A    82              1.97            
REMARK 500   HG1  THR A   517     OH   TYR A   582              1.97            
REMARK 500   HZ1  LYS A   413     O    HOH A    63              1.97            
REMARK 500   O    CYS A   428     HZ1  LYS A   492              1.97            
REMARK 500   H    GLY A   393     O    HOH A   172              1.97            
REMARK 500   H    VAL A   411     OE1  GLN A   531              1.98            
REMARK 500   OD1  ASP A   447     H    SER A   450              1.98            
REMARK 500   O    LEU A   523     H    GLN A   531              1.98            
REMARK 500   H    PHE A   534     O    THR A   539              1.99            
REMARK 500   H    ILE A   443     O    GLN A   452              1.99            
REMARK 500   O    ILE A   532     H    LEU A   541              1.99            
REMARK 500   O    ASP A   429    HD22  ASN A   446              1.99            
REMARK 500   O    ILE A   542     H    THR A   551              1.99            
REMARK 500   HE   ARG A   516     O    HOH A   249              2.00            
REMARK 500   O    LYS A   540     H    ILE A   553              2.00            
REMARK 500   O    LYS A   480     H    ASN A   484              2.00            
REMARK 500   HG1  THR A   498     O    HOH A    86              2.00            
REMARK 500   O    LEU A   381     H    ASN A   385              2.00            
REMARK 500   O    LEU A   591     H    SER A   595              2.01            
REMARK 500   O    ARG A   441     H    ILE A   454              2.01            
REMARK 500   O    LEU A   567     H    GLY A   571              2.01            
REMARK 500   O    ILE A   406    HH11  ARG A   500              2.01            
REMARK 500   O    SER A   412     H    ALA A   493              2.01            
REMARK 500   O    TYR A   453     H    SER A   461              2.01            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     202 CLOSE CONTACTS                                
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   HG2  ARG A   599     O    HOH A    30     1455     1.85            
REMARK 500   OD1  ASP A   376     HZ1  LYS A   480     2545     1.86            
REMARK 500   OE1  GLU A   488     HE   ARG A   512     2555     1.93            
REMARK 500   OE1  GLU A   398     H    ASN A   470     1656     1.94            
REMARK 500   HH   TYR A   417     OD2  ASP A   503     2555     2.04            
REMARK 500   O    VAL A   395     HG   SER A   471     1656     2.05            
REMARK 500   HB3  ASP A   449     O    HOH A   262     1554     2.12            
REMARK 500   HH   TYR A   485     O    HOH A    56     2555     2.14            
REMARK 500   H    GLU A   460     O    ALA B     6     2545     2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 392   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
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 396       60.85   -119.62                                   
REMARK 500    TYR A 421      -50.28   -123.16                                   
REMARK 500    ASP A 449      -36.19   -135.44                                   
REMARK 500    ASP A 503     -157.57    -93.32                                   
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 ACE B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 B 7                   
DBREF  3FVH A  371   603  UNP    P53350   PLK1_HUMAN     371    603             
DBREF  3FVH B    1     7  PDB    3FVH     3FVH             1      7             
SEQADV 3FVH GLY A  367  UNP  P53350              EXPRESSION TAG                 
SEQADV 3FVH ALA A  368  UNP  P53350              EXPRESSION TAG                 
SEQADV 3FVH HIS A  369  UNP  P53350              EXPRESSION TAG                 
SEQADV 3FVH MET A  370  UNP  P53350              EXPRESSION TAG                 
SEQRES   1 A  237  GLY ALA HIS MET ASP CYS HIS LEU SER ASP MET LEU GLN          
SEQRES   2 A  237  GLN LEU HIS SER VAL ASN ALA SER LYS PRO SER GLU ARG          
SEQRES   3 A  237  GLY LEU VAL ARG GLN GLU GLU ALA GLU ASP PRO ALA CYS          
SEQRES   4 A  237  ILE PRO ILE PHE TRP VAL SER LYS TRP VAL ASP TYR SER          
SEQRES   5 A  237  ASP LYS TYR GLY LEU GLY TYR GLN LEU CYS ASP ASN SER          
SEQRES   6 A  237  VAL GLY VAL LEU PHE ASN ASP SER THR ARG LEU ILE LEU          
SEQRES   7 A  237  TYR ASN ASP GLY ASP SER LEU GLN TYR ILE GLU ARG ASP          
SEQRES   8 A  237  GLY THR GLU SER TYR LEU THR VAL SER SER HIS PRO ASN          
SEQRES   9 A  237  SER LEU MET LYS LYS ILE THR LEU LEU LYS TYR PHE ARG          
SEQRES  10 A  237  ASN TYR MET SER GLU HIS LEU LEU LYS ALA GLY ALA ASN          
SEQRES  11 A  237  ILE THR PRO ARG GLU GLY ASP GLU LEU ALA ARG LEU PRO          
SEQRES  12 A  237  TYR LEU ARG THR TRP PHE ARG THR ARG SER ALA ILE ILE          
SEQRES  13 A  237  LEU HIS LEU SER ASN GLY SER VAL GLN ILE ASN PHE PHE          
SEQRES  14 A  237  GLN ASP HIS THR LYS LEU ILE LEU CYS PRO LEU MET ALA          
SEQRES  15 A  237  ALA VAL THR TYR ILE ASP GLU LYS ARG ASP PHE ARG THR          
SEQRES  16 A  237  TYR ARG LEU SER LEU LEU GLU GLU TYR GLY CYS CYS LYS          
SEQRES  17 A  237  GLU LEU ALA SER ARG LEU ARG TYR ALA ARG THR MET VAL          
SEQRES  18 A  237  ASP LYS LEU LEU SER SER ARG SER ALA SER ASN ARG LEU          
SEQRES  19 A  237  LYS ALA SER                                                  
SEQRES   1 B    7  ACE LEU HIS SER TPO ALA NH2                                  
MODRES 3FVH TPO B    5  THR  PHOSPHOTHREONINE                                   
HET    ACE  B   1       3                                                       
HET    TPO  B   5      17                                                       
HET    NH2  B   7       1                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     NH2 AMINO GROUP                                                      
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   2  ACE    C2 H4 O                                                      
FORMUL   2  TPO    C4 H10 N O6 P                                                
FORMUL   2  NH2    H2 N                                                         
FORMUL   3  HOH   *262(H2 O)                                                    
HELIX    1   1 CYS A  372  SER A  387  1                                  16    
HELIX    2   2 LYS A  388  ARG A  392  5                                   5    
HELIX    3   3 ARG A  396  GLU A  401  5                                   6    
HELIX    4   4 ASP A  402  ILE A  406  5                                   5    
HELIX    5   5 PRO A  469  SER A  471  5                                   3    
HELIX    6   6 LEU A  472  LEU A  490  1                                  19    
HELIX    7   7 LEU A  564  GLY A  571  1                                   8    
HELIX    8   8 CYS A  573  ALA A  602  1                                  30    
SHEET    1   A 6 VAL A 411  TYR A 417  0                                        
SHEET    2   A 6 GLY A 422  LEU A 427 -1  O  GLN A 426   N  LYS A 413           
SHEET    3   A 6 VAL A 432  PHE A 436 -1  O  GLY A 433   N  TYR A 425           
SHEET    4   A 6 ARG A 441  LEU A 444 -1  O  LEU A 444   N  VAL A 432           
SHEET    5   A 6 SER A 450  ILE A 454 -1  O  ILE A 454   N  ARG A 441           
SHEET    6   A 6 GLU A 460  THR A 464 -1  O  LEU A 463   N  LEU A 451           
SHEET    1   B 6 LEU A 511  ARG A 516  0                                        
SHEET    2   B 6 ALA A 520  LEU A 525 -1  O  ILE A 522   N  PHE A 515           
SHEET    3   B 6 VAL A 530  PHE A 534 -1  O  GLN A 531   N  LEU A 523           
SHEET    4   B 6 LYS A 540  CYS A 544 -1  O  LEU A 543   N  VAL A 530           
SHEET    5   B 6 ALA A 549  ILE A 553 -1  O  ILE A 553   N  LYS A 540           
SHEET    6   B 6 PHE A 559  ARG A 563 -1  O  TYR A 562   N  VAL A 550           
LINK         C   ACE B   1                 N   LEU B   2     1555   1555  1.32  
LINK         C   SER B   4                 N   TPO B   5     1555   1555  1.33  
LINK         C   TPO B   5                 N   ALA B   6     1555   1555  1.34  
LINK         C   ALA B   6                 N   NH2 B   7     1555   1555  1.45  
SITE     1 AC1  3 ARG A 516  LEU B   2  HIS B   3                               
SITE     1 AC2  3 HIS A 489  LEU A 491  ALA B   6                               
CRYST1   38.310   62.412   46.607  90.00  94.07  90.00 P 1 21 1      2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.026103  0.000000  0.001857        0.00000                         
SCALE2      0.000000  0.016023  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021510        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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