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Database: PDB
Entry: 3HIH
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HEADER    TRANSFERASE                             20-MAY-09   3HIH              
TITLE     STRUCTURE OF HUMAN PLK1-PBD WITH GLYCEROL AND SULFATE IN THE          
TITLE    2 PHOPHOPEPTIDE BINDING SITE                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK1;                      
COMPND   3 CHAIN: A, B;                                                         
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                                                      
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: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PDEST-527                                 
KEYWDS    KINASE, PHOSPHOPEPTIDE-BINDING DOMAIN, TRANSFERASE, SERINE THREONINE  
KEYWDS   2 PROTEIN KINASE, ATP-BINDING, CELL CYCLE, CELL DIVISION, MITOSIS,     
KEYWDS   3 NUCLEOTIDE-BINDING, NUCLEUS, PHOSPHOPROTEIN, SERINE/THREONINE-       
KEYWDS   4 PROTEIN KINASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.WLODAWER,T.MOULAEI                                                  
REVDAT   4   13-JUL-11 3HIH    1       VERSN                                    
REVDAT   3   18-AUG-09 3HIH    1       JRNL                                     
REVDAT   2   11-AUG-09 3HIH    1       JRNL                                     
REVDAT   1   09-JUN-09 3HIH    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.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 48194                          
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) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1271                            
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) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3080                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 84.73                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2440                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 84                           
REMARK   3   BIN FREE R VALUE                    : 0.2900                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3446                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 63                                      
REMARK   3   SOLVENT ATOMS            : 325                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.89                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.65000                                             
REMARK   3    B22 (A**2) : -0.29000                                             
REMARK   3    B33 (A**2) : 0.98000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.30000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.111         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.107         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.074         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.216         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3628 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4907 ; 1.551 ; 1.977       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   435 ; 6.373 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   151 ;27.585 ;23.179       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   626 ;13.769 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;21.193 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   563 ; 0.118 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2626 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1746 ; 0.221 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2530 ; 0.307 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   271 ; 0.155 ; 0.200       
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):    63 ; 0.231 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    29 ; 0.158 ; 0.200       
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):  2255 ; 1.170 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3560 ; 1.946 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1569 ; 2.900 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1347 ; 4.049 ; 4.500       
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 ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3HIH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAY-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB053174.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-AUG-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49465                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : 0.05500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LITHIUM SULFATE MONOHYDRATE, 0.1   
REMARK 280  M BIS-TRIS, 25% W/V PEG 3350, PH 5.5, VAPOR DIFFUSION, HANGING      
REMARK 280  DROP, TEMPERATURE 298K                                              
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       51.15000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     THR B   498                                                      
REMARK 465     PRO B   499                                                      
REMARK 465     GLU B   501                                                      
REMARK 465     GLY B   502                                                      
REMARK 465     ASP B   503                                                      
REMARK 465     GLU B   504                                                      
REMARK 465     LEU B   505                                                      
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     CYS A 372    SG                                                  
REMARK 470     GLN A 379    CD   OE1  NE2                                       
REMARK 470     HIS A 382    ND1  CE1  NE2                                       
REMARK 470     ASP A 419    OD1  OD2                                            
REMARK 470     ARG A 456    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET A 473    SD   CE                                             
REMARK 470     LYS A 474    CD   CE   NZ                                        
REMARK 470     ASP A 503    CG   OD1  OD2                                       
REMARK 470     GLU A 504    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 536    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 555    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 556    NZ                                                  
REMARK 470     ASP A 558    OD1  OD2                                            
REMARK 470     ARG A 560    NH1  NH2                                            
REMARK 470     ARG A 563    NH2                                                 
REMARK 470     LYS A 574    CD   CE   NZ                                        
REMARK 470     GLU A 575    CD   OE1  OE2                                       
REMARK 470     ARG A 584    NH1  NH2                                            
REMARK 470     LYS A 589    CE   NZ                                             
REMARK 470     CYS B 372    SG                                                  
REMARK 470     LYS B 388    CE   NZ                                             
REMARK 470     GLU B 391    OE1  OE2                                            
REMARK 470     ASP B 419    OD1  OD2                                            
REMARK 470     LYS B 420    NZ                                                  
REMARK 470     VAL B 432    N    CA   C    O                                    
REMARK 470     GLU B 455    OE1  OE2                                            
REMARK 470     ARG B 456    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B 474    CD   CE   NZ                                        
REMARK 470     GLU B 488    N    CA   C    O                                    
REMARK 470     LYS B 492    NZ                                                  
REMARK 470     ALA B 495    CB                                                  
REMARK 470     ASN B 496    CB   CG   OD1                                       
REMARK 470     ARG B 507    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 512    NH1                                                 
REMARK 470     GLN B 536    CD   OE1  NE2                                       
REMARK 470     GLU B 555    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 556    CG   CD   CE   NZ                                   
REMARK 470     ARG B 557    NE   CZ   NH1  NH2                                  
REMARK 470     ASP B 558    OD1  OD2                                            
REMARK 470     ARG B 560    NE   CZ   NH1  NH2                                  
REMARK 470     ARG B 563    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU B 575    CD   OE1  OE2                                       
REMARK 470     SER B 578    N    CA   C    O                                    
REMARK 470     LYS B 589    NZ                                                  
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    LEU B 423   CA  -  CB  -  CG  ANGL. DEV. = -14.0 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    LYS A 420      -41.38   -140.34                                   
REMARK 500    ASP A 449      -32.90   -139.54                                   
REMARK 500    HIS A 468       62.46     31.67                                   
REMARK 500    LYS B 420      -41.64   -136.84                                   
REMARK 500    ASN B 430       -0.12     68.29                                   
REMARK 500    ASP B 449      -36.32   -136.82                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASN B 446        24.7      L          L   OUTSIDE RANGE           
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 SO4 A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 7                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 8                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 10                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 12                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 9                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 11                  
DBREF  3HIH A  371   593  UNP    P53350   PLK1_HUMAN     371    593             
DBREF  3HIH B  371   593  UNP    P53350   PLK1_HUMAN     371    593             
SEQRES   1 A  223  ASP CYS HIS LEU SER ASP MET LEU GLN GLN LEU HIS SER          
SEQRES   2 A  223  VAL ASN ALA SER LYS PRO SER GLU ARG GLY LEU VAL ARG          
SEQRES   3 A  223  GLN GLU GLU ALA GLU ASP PRO ALA CYS ILE PRO ILE PHE          
SEQRES   4 A  223  TRP VAL SER LYS TRP VAL ASP TYR SER ASP LYS TYR GLY          
SEQRES   5 A  223  LEU GLY TYR GLN LEU CYS ASP ASN SER VAL GLY VAL LEU          
SEQRES   6 A  223  PHE ASN ASP SER THR ARG LEU ILE LEU TYR ASN ASP GLY          
SEQRES   7 A  223  ASP SER LEU GLN TYR ILE GLU ARG ASP GLY THR GLU SER          
SEQRES   8 A  223  TYR LEU THR VAL SER SER HIS PRO ASN SER LEU MET LYS          
SEQRES   9 A  223  LYS ILE THR LEU LEU LYS TYR PHE ARG ASN TYR MET SER          
SEQRES  10 A  223  GLU HIS LEU LEU LYS ALA GLY ALA ASN ILE THR PRO ARG          
SEQRES  11 A  223  GLU GLY ASP GLU LEU ALA ARG LEU PRO TYR LEU ARG THR          
SEQRES  12 A  223  TRP PHE ARG THR ARG SER ALA ILE ILE LEU HIS LEU SER          
SEQRES  13 A  223  ASN GLY SER VAL GLN ILE ASN PHE PHE GLN ASP HIS THR          
SEQRES  14 A  223  LYS LEU ILE LEU CYS PRO LEU MET ALA ALA VAL THR TYR          
SEQRES  15 A  223  ILE ASP GLU LYS ARG ASP PHE ARG THR TYR ARG LEU SER          
SEQRES  16 A  223  LEU LEU GLU GLU TYR GLY CYS CYS LYS GLU LEU ALA SER          
SEQRES  17 A  223  ARG LEU ARG TYR ALA ARG THR MET VAL ASP LYS LEU LEU          
SEQRES  18 A  223  SER SER                                                      
SEQRES   1 B  223  ASP CYS HIS LEU SER ASP MET LEU GLN GLN LEU HIS SER          
SEQRES   2 B  223  VAL ASN ALA SER LYS PRO SER GLU ARG GLY LEU VAL ARG          
SEQRES   3 B  223  GLN GLU GLU ALA GLU ASP PRO ALA CYS ILE PRO ILE PHE          
SEQRES   4 B  223  TRP VAL SER LYS TRP VAL ASP TYR SER ASP LYS TYR GLY          
SEQRES   5 B  223  LEU GLY TYR GLN LEU CYS ASP ASN SER VAL GLY VAL LEU          
SEQRES   6 B  223  PHE ASN ASP SER THR ARG LEU ILE LEU TYR ASN ASP GLY          
SEQRES   7 B  223  ASP SER LEU GLN TYR ILE GLU ARG ASP GLY THR GLU SER          
SEQRES   8 B  223  TYR LEU THR VAL SER SER HIS PRO ASN SER LEU MET LYS          
SEQRES   9 B  223  LYS ILE THR LEU LEU LYS TYR PHE ARG ASN TYR MET SER          
SEQRES  10 B  223  GLU HIS LEU LEU LYS ALA GLY ALA ASN ILE THR PRO ARG          
SEQRES  11 B  223  GLU GLY ASP GLU LEU ALA ARG LEU PRO TYR LEU ARG THR          
SEQRES  12 B  223  TRP PHE ARG THR ARG SER ALA ILE ILE LEU HIS LEU SER          
SEQRES  13 B  223  ASN GLY SER VAL GLN ILE ASN PHE PHE GLN ASP HIS THR          
SEQRES  14 B  223  LYS LEU ILE LEU CYS PRO LEU MET ALA ALA VAL THR TYR          
SEQRES  15 B  223  ILE ASP GLU LYS ARG ASP PHE ARG THR TYR ARG LEU SER          
SEQRES  16 B  223  LEU LEU GLU GLU TYR GLY CYS CYS LYS GLU LEU ALA SER          
SEQRES  17 B  223  ARG LEU ARG TYR ALA ARG THR MET VAL ASP LYS LEU LEU          
SEQRES  18 B  223  SER SER                                                      
HET    SO4  A   1       5                                                       
HET    SO4  A   2       5                                                       
HET    SO4  A   3       5                                                       
HET    GOL  A   6       7                                                       
HET    GOL  A   7       6                                                       
HET    GOL  A   8       6                                                       
HET    GOL  A  10       6                                                       
HET    EDO  A  12       4                                                       
HET    SO4  B   4       5                                                       
HET    SO4  B   5       5                                                       
HET    GOL  B   9       6                                                       
HET    EDO  B  11       4                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  SO4    5(O4 S 2-)                                                   
FORMUL   6  GOL    5(C3 H8 O3)                                                  
FORMUL  10  EDO    2(C2 H6 O2)                                                  
FORMUL  15  HOH   *325(H2 O)                                                    
HELIX    1   1 ASP A  371  SER A  387  1                                  17    
HELIX    2   2 ARG A  396  GLU A  401  5                                   6    
HELIX    3   3 ASP A  402  ILE A  406  5                                   5    
HELIX    4   4 SER A  466  HIS A  468  5                                   3    
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  SER A  593  1                                  21    
HELIX    9   9 ASP B  371  SER B  387  1                                  17    
HELIX   10  10 LYS B  388  ARG B  392  5                                   5    
HELIX   11  11 ARG B  396  GLU B  401  5                                   6    
HELIX   12  12 ASP B  402  ILE B  406  5                                   5    
HELIX   13  13 SER B  466  HIS B  468  5                                   3    
HELIX   14  14 PRO B  469  SER B  471  5                                   3    
HELIX   15  15 LEU B  472  SER B  487  1                                  16    
HELIX   16  16 LEU B  564  GLY B  571  1                                   8    
HELIX   17  17 ARG B  579  SER B  593  1                                  15    
SHEET    1   A 6 VAL A 411  ASP A 416  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  HIS A 524   N  THR A 513           
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           
SHEET    1   C 6 VAL B 411  ASP B 416  0                                        
SHEET    2   C 6 GLY B 422  LEU B 427 -1  O  GLN B 426   N  SER B 412           
SHEET    3   C 6 VAL B 434  PHE B 436 -1  O  LEU B 435   N  LEU B 423           
SHEET    4   C 6 ARG B 441  LEU B 444 -1  O  LEU B 442   N  VAL B 434           
SHEET    5   C 6 SER B 450  ILE B 454 -1  O  GLN B 452   N  ILE B 443           
SHEET    6   C 6 GLU B 460  THR B 464 -1  O  LEU B 463   N  LEU B 451           
SHEET    1   D 6 LEU B 511  ARG B 516  0                                        
SHEET    2   D 6 ALA B 520  LEU B 525 -1  O  HIS B 524   N  THR B 513           
SHEET    3   D 6 VAL B 530  PHE B 534 -1  O  GLN B 531   N  LEU B 523           
SHEET    4   D 6 LYS B 540  CYS B 544 -1  O  LEU B 543   N  VAL B 530           
SHEET    5   D 6 ALA B 549  ILE B 553 -1  O  ILE B 553   N  LYS B 540           
SHEET    6   D 6 PHE B 559  ARG B 563 -1  O  TYR B 562   N  VAL B 550           
CISPEP   1 ARG B  456    ASP B  457          0        -2.96                     
SITE     1 AC1  7 GOL A   6  HOH A  58  HOH A  80  GLU A 460                    
SITE     2 AC1  7 ARG A 507  HIS A 538  LYS A 540                               
SITE     1 AC2  6 GOL A   8  TYR A 445  TYR A 462  ARG A 507                    
SITE     2 AC2  6 LEU A 508  ARG A 557                                          
SITE     1 AC3  4 THR A 517  ARG A 518  SER A 519  TYR A 582                    
SITE     1 AC4 10 SO4 A   1  HOH A  15  HOH A  58  HOH A  80                    
SITE     2 AC4 10 HOH A 110  LYS A 413  TRP A 414  THR A 459                    
SITE     3 AC4 10 GLU A 460  LEU A 490                                          
SITE     1 AC5  6 HOH A 116  HOH A 186  PHE A 436  ASN A 437                    
SITE     2 AC5  6 ASP A 438  LEU A 478                                          
SITE     1 AC6  3 SO4 A   2  HOH A  31  TYR A 462                               
SITE     1 AC7  5 HOH A   4  ASN A 430  LEU A 444  ARG A 483                    
SITE     2 AC7  5 HOH A 598                                                     
SITE     1 AC8  3 HOH A  82  HOH A 315  TRP A 514                               
SITE     1 AC9  6 GLU A 501  GLY A 502  HOH B 158  HIS B 382                    
SITE     2 AC9  6 ASN B 385  ARG B 584                                          
SITE     1 BC1  3 HOH B  84  HIS B 538  LYS B 540                               
SITE     1 BC2  4 HOH B 123  LEU B 463  THR B 464  SER B 467                    
SITE     1 BC3  3 PHE B 436  ASN B 437  ASP B 438                               
CRYST1   33.300  102.300   68.500  90.00  93.20  90.00 P 1 21 1      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      0.030030  0.000000  0.001679        0.00000                         
SCALE2      0.000000  0.009775  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014621        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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