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Database: PDB
Entry: 3P34
LinkDB: 3P34
Original site: 3P34 
HEADER    TRANSFERASE                             04-OCT-10   3P34              
TITLE     POLO-LIKE KINASE I POLO-BOX DOMAIN IN COMPLEX WITH MQSPTPL            
TITLE    2 PHOSPHOPEPTIDE                                                       
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,M.HYVONEN,C.ABELL                                             
REVDAT   1   27-APR-11 3P34    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.    1.40 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) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 58.25                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 48107                          
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) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2578                            
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) : 1.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.44                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3551                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.65                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3190                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 172                          
REMARK   3   BIN FREE R VALUE                    : 0.3100                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1881                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 16                                      
REMARK   3   SOLVENT ATOMS            : 270                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.46                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.41000                                             
REMARK   3    B22 (A**2) : -0.43000                                             
REMARK   3    B33 (A**2) : 0.83000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.071         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.070         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.048         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.164         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.954                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1967 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2672 ; 1.048 ; 1.987       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   245 ; 5.376 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    85 ;29.202 ;23.176       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   340 ;13.874 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;14.192 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   298 ; 0.073 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1456 ; 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):  1198 ; 0.422 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1932 ; 0.824 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   769 ; 1.215 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   734 ; 1.971 ; 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   373        A   580                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.8080  -2.6640   9.9410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0082 T22:   0.1280                                     
REMARK   3      T33:   0.0268 T12:  -0.0074                                     
REMARK   3      T13:   0.0006 T23:   0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5107 L22:   1.1239                                     
REMARK   3      L33:   1.3414 L12:  -0.4714                                     
REMARK   3      L13:   0.5489 L23:  -0.9083                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0206 S12:   0.0054 S13:  -0.0212                       
REMARK   3      S21:  -0.0498 S22:  -0.0539 S23:  -0.0046                       
REMARK   3      S31:   0.0850 S32:   0.0413 S33:   0.0334                       
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 3P34 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 RCSB061895.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-OCT-09                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
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   : 49803                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 58.380                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7                               
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   (%): 47.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES, 1.0-2.0M (NH4)2SO4, PH      
REMARK 280  7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       18.59200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       44.48750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.52850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       44.48750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       18.59200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.52850            
REMARK 290   SMTRY3   4  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: 1310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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     SER A   593                                                      
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     GLU A 398    CD   OE1  OE2                                       
REMARK 470     ARG A 456    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 488    CD   OE1  OE2                                       
REMARK 470     GLU A 555    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 556    CG   CD   CE   NZ                                   
REMARK 470     ARG A 560    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 575    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A   8       76.76   -107.46                                   
REMARK 500    ASN A 430       -1.08     84.34                                   
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 595                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 596                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 597                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3P2W   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P2Z   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  3P34 A  371   594  UNP    P53350   PLK1_HUMAN     371    594             
DBREF  3P34 B    0     7  PDB    3P34     3P34             0      7             
SEQADV 3P34 GLY A    1  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P34 PRO A    2  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P34 LEU A    3  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P34 GLY A    4  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P34 SER A    5  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P34 PRO A    6  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P34 GLU A    7  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P34 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 MET GLN SER TPO PRO LEU NH2                              
MODRES 3P34 TPO B    4  THR  PHOSPHOTHREONINE                                   
HET    ACE  B   0       3                                                       
HET    TPO  B   4      11                                                       
HET    NH2  B   7       1                                                       
HET    SO4  A 595       5                                                       
HET    SO4  A 596       5                                                       
HET    GOL  A 597       6                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     NH2 AMINO GROUP                                                      
HETNAM     SO4 SULFATE ION                                                      
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  SO4    2(O4 S 2-)                                                   
FORMUL   5  GOL    C3 H8 O3                                                     
FORMUL   6  HOH   *270(H2 O)                                                    
HELIX    1   1 CYS A  372  SER A  387  1                                  16    
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 PRO A  469  SER A  471  5                                   3    
HELIX    5   5 LEU A  472  LEU A  490  1                                  19    
HELIX    6   6 LEU A  564  GLY A  571  1                                   8    
HELIX    7   7 CYS A  573  SER A  592  1                                  20    
SHEET    1   A 7 GLU A 460  THR A 464  0                                        
SHEET    2   A 7 SER A 450  ILE A 454 -1  N  LEU A 451   O  LEU A 463           
SHEET    3   A 7 ARG A 441  LEU A 444 -1  N  ARG A 441   O  ILE A 454           
SHEET    4   A 7 VAL A 432  PHE A 436 -1  N  VAL A 432   O  LEU A 444           
SHEET    5   A 7 GLY A 422  LEU A 427 -1  N  TYR A 425   O  GLY A 433           
SHEET    6   A 7 VAL A 411  ASP A 416 -1  N  VAL A 415   O  GLY A 424           
SHEET    7   A 7 MET B   1  GLN B   2 -1  O  MET B   1   N  ASP A 416           
SHEET    1   B 6 LEU A 511  ARG A 516  0                                        
SHEET    2   B 6 ALA A 520  LEU A 525 -1  O  ILE A 522   N  PHE A 515           
SHEET    3   B 6 VAL A 530  PHE A 534 -1  O  GLN A 531   N  LEU A 523           
SHEET    4   B 6 LYS A 540  CYS A 544 -1  O  LEU A 543   N  VAL A 530           
SHEET    5   B 6 ALA A 549  ILE A 553 -1  O  ILE A 553   N  LYS A 540           
SHEET    6   B 6 PHE A 559  ARG A 563 -1  O  TYR A 562   N  VAL A 550           
LINK         C   ACE B   0                 N   MET B   1     1555   1555  1.33  
LINK         C   SER B   3                 N   TPO B   4     1555   1555  1.33  
LINK         C   TPO B   4                 N   PRO B   5     1555   1555  1.33  
LINK         C   LEU B   6                 N   NH2 B   7     1555   1555  1.28  
SITE     1 AC1  9 HOH A  41  HOH A  61  HOH A 268  HOH A 288                    
SITE     2 AC1  9 HOH A 290  ARG A 392  GLY A 393  LEU A 394                    
SITE     3 AC1  9 LYS A 474                                                     
SITE     1 AC2  4 HOH A 121  HOH A 307  ARG A 396  TYR A 570                    
SITE     1 AC3  4 PRO A 469  ASN A 470  SER A 471  HOH A 604                    
CRYST1   37.184   77.057   88.975  90.00  90.00  90.00 P 21 21 21    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      0.026893  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012977  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011239        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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