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Database: PDB
Entry: 3P2Z
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Original site: 3P2Z 
HEADER    TRANSFERASE                             04-OCT-10   3P2Z              
TITLE     POLO-LIKE KINASE I POLO-BOX DOMAIN IN COMPLEX WITH PLHSPTA            
TITLE    2 PHOSPHOPEPTIDE FROM PBIP1                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK1;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: POLO-BOX DOMAIN;                                           
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 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: PHOSPHOPEPTIDE;                                            
COMPND  11 CHAIN: B;                                                            
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PLK1, PLK;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1;                                
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 OTHER_DETAILS: CHEMICALLY SYNTHESIZED                                
KEYWDS    PHOSPHOPROTEIN BINDING DOMAIN, PLK1, KINASE, TRANSFERASE              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.SLEDZ,C.J.STUBBS,M.HYVONEN,C.ABELL                                  
REVDAT   1   27-APR-11 3P2Z    0                                                
JRNL        AUTH   P.SLEDZ,C.J.STUBBS,S.LANG,Y.Q.YANG,G.J.MCKENZIE,             
JRNL        AUTH 2 A.R.VENKITARAMAN,M.HYVONEN,C.ABELL                           
JRNL        TITL   FROM CRYSTAL PACKING TO MOLECULAR RECOGNITION: PREDICTION    
JRNL        TITL 2 AND DISCOVERY OF A BINDING SITE ON THE SURFACE OF POLO-LIKE  
JRNL        TITL 3 KINASE 1                                                     
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.       V.  50  4003 2011              
JRNL        REFN                   ISSN 1433-7851                               
JRNL        PMID   21472932                                                     
JRNL        DOI    10.1002/ANIE.201008019                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.79 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 1.79                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.31                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 17491                          
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) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 945                             
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) : 1.79                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.84                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1254                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.24                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3080                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 52                           
REMARK   3   BIN FREE R VALUE                    : 0.2800                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1735                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 6                                       
REMARK   3   SOLVENT ATOMS            : 146                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.96                          
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.151         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.102         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.096         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.911                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1809 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2459 ; 0.933 ; 1.970       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   222 ; 5.095 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    81 ;26.942 ;22.840       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   301 ;13.180 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;16.528 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   278 ; 0.061 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1345 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1095 ; 0.333 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1765 ; 0.646 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   714 ; 0.854 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   689 ; 1.451 ; 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  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   371        A   580                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.5320   1.9960  10.5080              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0506 T22:   0.0451                                     
REMARK   3      T33:   0.0771 T12:   0.0182                                     
REMARK   3      T13:  -0.0583 T23:  -0.0115                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0944 L22:   1.1642                                     
REMARK   3      L33:   2.3482 L12:   0.4029                                     
REMARK   3      L13:  -0.9226 L23:  -0.7526                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0539 S12:  -0.0455 S13:  -0.0096                       
REMARK   3      S21:  -0.0391 S22:   0.0219 S23:   0.0074                       
REMARK   3      S31:   0.0830 S32:   0.0741 S33:   0.0320                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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: NULL                                      
REMARK   4                                                                      
REMARK   4 3P2Z COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-OCT-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB061890.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9334                             
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   : 18437                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.790                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.310                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.900                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
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: MOLREP                                                
REMARK 200 STARTING MODEL: 1UMW (CHAIN A)                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 32.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M K/NA TARTRATE, 20% PEG 3350,        
REMARK 280  VAPOR DIFFUSION, SITTING 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       33.43150            
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1250 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     ASN A   385                                                      
REMARK 465     ALA A   386                                                      
REMARK 465     SER A   387                                                      
REMARK 465     LYS A   388                                                      
REMARK 465     PRO A   389                                                      
REMARK 465     SER A   390                                                      
REMARK 465     GLU A   391                                                      
REMARK 465     ARG A   392                                                      
REMARK 465     GLY A   393                                                      
REMARK 465     LEU A   394                                                      
REMARK 465     VAL A   395                                                      
REMARK 465     ARG A   396                                                      
REMARK 465     GLN A   397                                                      
REMARK 465     GLU A   398                                                      
REMARK 465     ARG A   500                                                      
REMARK 465     GLU A   501                                                      
REMARK 465     GLY A   502                                                      
REMARK 465     ARG A   594                                                      
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     GLU A   7    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 503    CG   OD1  OD2                                       
REMARK 470     GLU A 504    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 555    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 556    CG   CD   CE   NZ                                   
REMARK 470     GLU A 569    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 574    CG   CD   CE   NZ                                   
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    TYR A 421      -57.37   -120.40                                   
REMARK 500    ASP A 449      -41.91   -134.74                                   
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 GOL A 595                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3P2W   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P34   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P35   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P36   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P37   RELATED DB: PDB                                   
DBREF  3P2Z A  371   594  UNP    P53350   PLK1_HUMAN     371    594             
DBREF  3P2Z B   73    80  PDB    3P2Z     3P2Z            73     80             
SEQADV 3P2Z GLY A    1  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P2Z PRO A    2  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P2Z LEU A    3  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P2Z GLY A    4  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P2Z SER A    5  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P2Z PRO A    6  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P2Z GLU A    7  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P2Z PHE A    8  UNP  P53350              EXPRESSION TAG                 
SEQRES   1 A  232  GLY PRO LEU GLY SER PRO GLU PHE ASP CYS HIS LEU SER          
SEQRES   2 A  232  ASP MET LEU GLN GLN LEU HIS SER VAL ASN ALA SER LYS          
SEQRES   3 A  232  PRO SER GLU ARG GLY LEU VAL ARG GLN GLU GLU ALA GLU          
SEQRES   4 A  232  ASP PRO ALA CYS ILE PRO ILE PHE TRP VAL SER LYS TRP          
SEQRES   5 A  232  VAL ASP TYR SER ASP LYS TYR GLY LEU GLY TYR GLN LEU          
SEQRES   6 A  232  CYS ASP ASN SER VAL GLY VAL LEU PHE ASN ASP SER THR          
SEQRES   7 A  232  ARG LEU ILE LEU TYR ASN ASP GLY ASP SER LEU GLN TYR          
SEQRES   8 A  232  ILE GLU ARG ASP GLY THR GLU SER TYR LEU THR VAL SER          
SEQRES   9 A  232  SER HIS PRO ASN SER LEU MET LYS LYS ILE THR LEU LEU          
SEQRES  10 A  232  LYS TYR PHE ARG ASN TYR MET SER GLU HIS LEU LEU LYS          
SEQRES  11 A  232  ALA GLY ALA ASN ILE THR PRO ARG GLU GLY ASP GLU LEU          
SEQRES  12 A  232  ALA ARG LEU PRO TYR LEU ARG THR TRP PHE ARG THR ARG          
SEQRES  13 A  232  SER ALA ILE ILE LEU HIS LEU SER ASN GLY SER VAL GLN          
SEQRES  14 A  232  ILE ASN PHE PHE GLN ASP HIS THR LYS LEU ILE LEU CYS          
SEQRES  15 A  232  PRO LEU MET ALA ALA VAL THR TYR ILE ASP GLU LYS ARG          
SEQRES  16 A  232  ASP PHE ARG THR TYR ARG LEU SER LEU LEU GLU GLU TYR          
SEQRES  17 A  232  GLY CYS CYS LYS GLU LEU ALA SER ARG LEU ARG TYR ALA          
SEQRES  18 A  232  ARG THR MET VAL ASP LYS LEU LEU SER SER ARG                  
SEQRES   1 B    8  ACE PRO LEU HIS SER TPO ALA NH2                              
MODRES 3P2Z TPO B   78  THR  PHOSPHOTHREONINE                                   
HET    ACE  B  73       3                                                       
HET    TPO  B  78      11                                                       
HET    NH2  B  80       1                                                       
HET    GOL  A 595       6                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     NH2 AMINO GROUP                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  ACE    C2 H4 O                                                      
FORMUL   2  TPO    C4 H10 N O6 P                                                
FORMUL   2  NH2    H2 N                                                         
FORMUL   3  GOL    C3 H8 O3                                                     
FORMUL   4  HOH   *146(H2 O)                                                    
HELIX    1   1 PRO A    6  VAL A  384  1                                  17    
HELIX    2   2 ASP A  402  ILE A  406  5                                   5    
HELIX    3   3 PRO A  469  SER A  471  5                                   3    
HELIX    4   4 LEU A  472  LEU A  490  1                                  19    
HELIX    5   5 LEU A  564  GLY A  571  1                                   8    
HELIX    6   6 CYS A  573  SER A  593  1                                  21    
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  THR A 551   N  ILE A 542           
SHEET    6   B 6 PHE A 559  ARG A 563 -1  O  TYR A 562   N  VAL A 550           
LINK         C   ACE B  73                 N   PRO B  74     1555   1555  1.34  
LINK         C   SER B  77                 N   TPO B  78     1555   1555  1.33  
LINK         C   TPO B  78                 N   ALA B  79     1555   1555  1.33  
LINK         C   ALA B  79                 N   NH2 B  80     1555   1555  1.26  
SITE     1 AC1  6 HOH A 172  LYS A 420  TYR A 421  PHE A 436                    
SITE     2 AC1  6 ASN A 437  ASP A 438                                          
CRYST1   34.412   66.863   43.427  90.00  94.12  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      0.029060  0.000000  0.002091        0.00000                         
SCALE2      0.000000  0.014956  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.023087        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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