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Database: PDB
Entry: 2OWB
LinkDB: 2OWB
Original site: 2OWB 
HEADER    TRANSFERASE                             15-FEB-07   2OWB              
TITLE     STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN POLO-LIKE KINASE 1         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK1;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: KINASE DOMAIN (RESIDUES 13-345);                           
COMPND   5 SYNONYM: POLO-LIKE KINASE 1, PLK-1, SERINE/THREONINE-PROTEIN KINASE  
COMPND   6 13, STPK13;                                                          
COMPND   7 EC: 2.7.11.21;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PLK1, PLK;                                                     
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: SF21;                                      
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    CATALYTIC DOMAIN, PLK1, POLO-LIKE KINASE1, KINASE, TRANSFERASE        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.-H.DING,M.KOTHE,D.KOHLS,S.LOW                                       
REVDAT   4   13-JUL-11 2OWB    1       VERSN                                    
REVDAT   3   24-FEB-09 2OWB    1       VERSN                                    
REVDAT   2   21-AUG-07 2OWB    1       JRNL                                     
REVDAT   1   24-APR-07 2OWB    0                                                
JRNL        AUTH   M.KOTHE,D.KOHLS,S.LOW,R.COLI,A.C.CHENG,S.L.JACQUES,          
JRNL        AUTH 2 T.L.JOHNSON,C.LEWIS,C.LOH,J.NONOMIYA,A.L.SHEILS,             
JRNL        AUTH 3 K.A.VERDRIES,T.A.WYNN,C.KUHN,Y.H.DING                        
JRNL        TITL   STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN POLO-LIKE KINASE  
JRNL        TITL 2 1.                                                           
JRNL        REF    BIOCHEMISTRY                  V.  46  5960 2007              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   17461553                                                     
JRNL        DOI    10.1021/BI602474J                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.94                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 22445                          
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) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1205                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1436                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2660                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 80                           
REMARK   3   BIN FREE R VALUE                    : 0.3600                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2379                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 41                                      
REMARK   3   SOLVENT ATOMS            : 256                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.29000                                              
REMARK   3    B22 (A**2) : 2.29000                                              
REMARK   3    B33 (A**2) : -3.43000                                             
REMARK   3    B12 (A**2) : 1.14000                                              
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): 0.181         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.140         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.600         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2484 ; 0.006 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2326 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3351 ; 0.926 ; 1.989       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5412 ; 0.745 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   293 ; 5.177 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   363 ; 0.055 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2700 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   524 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   471 ; 0.168 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2672 ; 0.209 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1477 ; 0.078 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   188 ; 0.114 ; 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):    12 ; 0.111 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    48 ; 0.196 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.170 ; 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):  1470 ; 0.311 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2393 ; 0.591 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1014 ; 0.738 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   958 ; 1.336 ; 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 : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 2OWB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-FEB-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB041664.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23735                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.9500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN BUFFER: 50 MM HEPES, PH 7.5, 5   
REMARK 280  MM TCEP. PROTEIN WAS INCUBATED ON ICE WITH 5 MM LIGAND (1:20        
REMARK 280  DILUTION OF 100 MM STOCK IN H2O FOR AMPPNP OR DMSO FOR PHA-         
REMARK 280  680626) FOR 0.5-1 H, FOLLOWED BY A BRIEF CENTRIFUGATION STEP AND    
REMARK 280  DROP SETTING AT RT (0.5 MICROLITER PROTEIN + 0.5 MICROLITER         
REMARK 280  RESERVOIR SOLUTION CONSISTING OF 500 MM MAGNESIUM ACETATE, 10 %     
REMARK 280  PEG 4000 AND 0.3 MM ZINC ACETATE FOR AMPPNP, VAPOR DIFFUSION,       
REMARK 280  HANGING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      102.39333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       51.19667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       51.19667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      102.39333            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 4500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -99.0 KCAL/MOL                        
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   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      102.39333            
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    11                                                      
REMARK 465     PRO A    12                                                      
REMARK 465     ALA A    13                                                      
REMARK 465     PRO A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     ASP A    16                                                      
REMARK 465     PRO A    17                                                      
REMARK 465     GLY A    18                                                      
REMARK 465     LYS A    19                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     GLY A    21                                                      
REMARK 465     VAL A    22                                                      
REMARK 465     PRO A    23                                                      
REMARK 465     GLY A    24                                                      
REMARK 465     VAL A    25                                                      
REMARK 465     ALA A    26                                                      
REMARK 465     ALA A    27                                                      
REMARK 465     PRO A    28                                                      
REMARK 465     GLY A    29                                                      
REMARK 465     ALA A    30                                                      
REMARK 465     PRO A    31                                                      
REMARK 465     ALA A    32                                                      
REMARK 465     ALA A    33                                                      
REMARK 465     ALA A    34                                                      
REMARK 465     PRO A    35                                                      
REMARK 465     PRO A    36                                                      
REMARK 465     SER A   331                                                      
REMARK 465     LEU A   332                                                      
REMARK 465     ASP A   333                                                      
REMARK 465     PRO A   334                                                      
REMARK 465     SER A   335                                                      
REMARK 465     ASN A   336                                                      
REMARK 465     ARG A   337                                                      
REMARK 465     LYS A   338                                                      
REMARK 465     PRO A   339                                                      
REMARK 465     LEU A   340                                                      
REMARK 465     THR A   341                                                      
REMARK 465     VAL A   342                                                      
REMARK 465     LEU A   343                                                      
REMARK 465     ASN A   344                                                      
REMARK 465     LYS A   345                                                      
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  38       88.84     65.42                                   
REMARK 500    ASP A 122     -168.81   -116.74                                   
REMARK 500    ARG A 135       32.71    -99.79                                   
REMARK 500    ARG A 136     -129.88     63.23                                   
REMARK 500    LYS A 146     -127.78     50.10                                   
REMARK 500    ARG A 175       -0.12     72.96                                   
REMARK 500    ASP A 176       42.13   -145.21                                   
REMARK 500    ASP A 194       82.45     55.05                                   
REMARK 500    SER A 229     -143.94   -151.74                                   
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 A 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 212   SG                                                     
REMARK 620 2 ACT A 502   O    95.5                                              
REMARK 620 3 HIS A  93   NE2 115.9 109.9                                        
REMARK 620 4 CYS A 255   SG  124.0 114.7  97.3                                  
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 ZN A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 626 A 500                 
DBREF  2OWB A   13   345  UNP    P53350   PLK1_HUMAN      13    345             
SEQADV 2OWB GLY A   11  UNP  P53350              CLONING ARTIFACT               
SEQADV 2OWB PRO A   12  UNP  P53350              CLONING ARTIFACT               
SEQADV 2OWB VAL A  210  UNP  P53350    THR   210 ENGINEERED                     
SEQRES   1 A  335  GLY PRO ALA PRO ALA ASP PRO GLY LYS ALA GLY VAL PRO          
SEQRES   2 A  335  GLY VAL ALA ALA PRO GLY ALA PRO ALA ALA ALA PRO PRO          
SEQRES   3 A  335  ALA LYS GLU ILE PRO GLU VAL LEU VAL ASP PRO ARG SER          
SEQRES   4 A  335  ARG ARG ARG TYR VAL ARG GLY ARG PHE LEU GLY LYS GLY          
SEQRES   5 A  335  GLY PHE ALA LYS CYS PHE GLU ILE SER ASP ALA ASP THR          
SEQRES   6 A  335  LYS GLU VAL PHE ALA GLY LYS ILE VAL PRO LYS SER LEU          
SEQRES   7 A  335  LEU LEU LYS PRO HIS GLN ARG GLU LYS MET SER MET GLU          
SEQRES   8 A  335  ILE SER ILE HIS ARG SER LEU ALA HIS GLN HIS VAL VAL          
SEQRES   9 A  335  GLY PHE HIS GLY PHE PHE GLU ASP ASN ASP PHE VAL PHE          
SEQRES  10 A  335  VAL VAL LEU GLU LEU CYS ARG ARG ARG SER LEU LEU GLU          
SEQRES  11 A  335  LEU HIS LYS ARG ARG LYS ALA LEU THR GLU PRO GLU ALA          
SEQRES  12 A  335  ARG TYR TYR LEU ARG GLN ILE VAL LEU GLY CYS GLN TYR          
SEQRES  13 A  335  LEU HIS ARG ASN ARG VAL ILE HIS ARG ASP LEU LYS LEU          
SEQRES  14 A  335  GLY ASN LEU PHE LEU ASN GLU ASP LEU GLU VAL LYS ILE          
SEQRES  15 A  335  GLY ASP PHE GLY LEU ALA THR LYS VAL GLU TYR ASP GLY          
SEQRES  16 A  335  GLU ARG LYS LYS VAL LEU CYS GLY THR PRO ASN TYR ILE          
SEQRES  17 A  335  ALA PRO GLU VAL LEU SER LYS LYS GLY HIS SER PHE GLU          
SEQRES  18 A  335  VAL ASP VAL TRP SER ILE GLY CYS ILE MET TYR THR LEU          
SEQRES  19 A  335  LEU VAL GLY LYS PRO PRO PHE GLU THR SER CYS LEU LYS          
SEQRES  20 A  335  GLU THR TYR LEU ARG ILE LYS LYS ASN GLU TYR SER ILE          
SEQRES  21 A  335  PRO LYS HIS ILE ASN PRO VAL ALA ALA SER LEU ILE GLN          
SEQRES  22 A  335  LYS MET LEU GLN THR ASP PRO THR ALA ARG PRO THR ILE          
SEQRES  23 A  335  ASN GLU LEU LEU ASN ASP GLU PHE PHE THR SER GLY TYR          
SEQRES  24 A  335  ILE PRO ALA ARG LEU PRO ILE THR CYS LEU THR ILE PRO          
SEQRES  25 A  335  PRO ARG PHE SER ILE ALA PRO SER SER LEU ASP PRO SER          
SEQRES  26 A  335  ASN ARG LYS PRO LEU THR VAL LEU ASN LYS                      
HET     ZN  A 501       1                                                       
HET    ACT  A 502       4                                                       
HET    ACT  A 503       4                                                       
HET    626  A 500      32                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     ACT ACETATE ION                                                      
HETNAM     626 4-(4-METHYLPIPERAZIN-1-YL)-N-[5-(2-THIENYLACETYL)-1,5-           
HETNAM   2 626  DIHYDROPYRROLO[3,4-C]PYRAZOL-3-YL]BENZAMIDE                     
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  ACT    2(C2 H3 O2 1-)                                               
FORMUL   5  626    C23 H24 N6 O2 S                                              
FORMUL   6  HOH   *256(H2 O)                                                    
HELIX    1   1 SER A   87  LEU A   89  5                                   3    
HELIX    2   2 LYS A   91  SER A  107  1                                  17    
HELIX    3   3 SER A  137  LYS A  146  1                                  10    
HELIX    4   4 THR A  149  ASN A  170  1                                  22    
HELIX    5   5 LYS A  178  GLY A  180  5                                   3    
HELIX    6   6 ALA A  219  SER A  224  1                                   6    
HELIX    7   7 PHE A  230  GLY A  247  1                                  18    
HELIX    8   8 CYS A  255  ASN A  266  1                                  12    
HELIX    9   9 ASN A  275  LEU A  286  1                                  12    
HELIX   10  10 ASP A  289  ARG A  293  5                                   5    
HELIX   11  11 THR A  295  ASN A  301  5                                   7    
HELIX   12  12 ASP A  302  SER A  307  1                                   6    
HELIX   13  13 PRO A  315  THR A  320  5                                   6    
SHEET    1   A 6 VAL A  43  ASP A  46  0                                        
SHEET    2   A 6 ARG A  51  GLY A  62 -1  O  ARG A  51   N  ASP A  46           
SHEET    3   A 6 ALA A  65  ASP A  72 -1  O  CYS A  67   N  LEU A  59           
SHEET    4   A 6 VAL A  78  PRO A  85 -1  O  GLY A  81   N  PHE A  68           
SHEET    5   A 6 PHE A 125  LEU A 130 -1  O  LEU A 130   N  ALA A  80           
SHEET    6   A 6 PHE A 116  GLU A 121 -1  N  PHE A 120   O  PHE A 127           
SHEET    1   B 2 VAL A 172  ILE A 173  0                                        
SHEET    2   B 2 THR A 199  LYS A 200 -1  O  THR A 199   N  ILE A 173           
SHEET    1   C 2 LEU A 182  LEU A 184  0                                        
SHEET    2   C 2 VAL A 190  ILE A 192 -1  O  LYS A 191   N  PHE A 183           
LINK        ZN    ZN A 501                 SG  CYS A 212     1555   1555  2.22  
LINK        ZN    ZN A 501                 O   ACT A 502     1555   1555  2.24  
LINK        ZN    ZN A 501                 NE2 HIS A  93     1555   1555  2.22  
LINK        ZN    ZN A 501                 SG  CYS A 255     1555   6555  2.23  
SITE     1 AC1  4 HIS A  93  CYS A 212  CYS A 255  ACT A 502                    
SITE     1 AC2  6 HIS A  93  GLN A  94  LYS A  97  CYS A 212                    
SITE     2 AC2  6 LEU A 256   ZN A 501                                          
SITE     1 AC3  7 LYS A 178  LEU A 179  GLY A 180  ASN A 216                    
SITE     2 AC3  7 TYR A 217  HOH A 624  HOH A 674                               
SITE     1 AC4 17 ARG A  57  PHE A  58  LEU A  59  GLY A  62                    
SITE     2 AC4 17 ALA A  65  LYS A  66  CYS A  67  ALA A  80                    
SITE     3 AC4 17 LYS A  82  GLU A 131  CYS A 133  ARG A 134                    
SITE     4 AC4 17 ARG A 136  PHE A 183  HOH A 514  HOH A 538                    
SITE     5 AC4 17 HOH A 545                                                     
CRYST1   66.931   66.931  153.590  90.00  90.00 120.00 P 32 2 1      6          
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      0.014941  0.008626  0.000000        0.00000                         
SCALE2      0.000000  0.017252  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006511        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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