GenomeNet

Database: PDB
Entry: 1Q4O
LinkDB: 1Q4O
Original site: 1Q4O 
HEADER    TRANSFERASE                             04-AUG-03   1Q4O              
TITLE     THE STRUCTURE OF THE POLO BOX DOMAIN OF HUMAN PLK1                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK;                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: POLO BOX DOMAIN OF PLK1;                                   
COMPND   5 SYNONYM: PLK-1, SERINE-THREONINE PROTEIN KINASE 13, STPK13;          
COMPND   6 EC: 2.7.1.-;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PLK OR PLK1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: B834 (DE3) PLYSS;                          
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P1                                  
KEYWDS    TRANSFERASE, SERINE/THREONINE-PROTEIN KINASE, ATP-BINDING,            
KEYWDS   2 NUCLEAR PROTEIN                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.Y.CHENG,E.D.LOWE,J.SINCLAIR,E.A.NIGG,L.N.JOHNSON                    
REVDAT   2   24-FEB-09 1Q4O    1       VERSN                                    
REVDAT   1   11-NOV-03 1Q4O    0                                                
JRNL        AUTH   K.Y.CHENG,E.D.LOWE,J.SINCLAIR,E.A.NIGG,L.N.JOHNSON           
JRNL        TITL   THE CRYSTAL STRUCTURE OF THE HUMAN POLO-LIKE                 
JRNL        TITL 2 KINASE-1 POLO BOX DOMAIN AND ITS PHOSPHO-PEPTIDE             
JRNL        TITL 3 COMPLEX.                                                     
JRNL        REF    EMBO J.                       V.  22  5757 2003              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   14592974                                                     
JRNL        DOI    10.1093/EMBOJ/CDG558                                         
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1                                           
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 19093                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGH OUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.288                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1041                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.00                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2270                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 78                           
REMARK   3   BIN FREE R VALUE                    : 0.3520                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3395                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 227                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.40000                                             
REMARK   3    B22 (A**2) : -0.88000                                             
REMARK   3    B33 (A**2) : 1.22000                                              
REMARK   3    B12 (A**2) : 0.22000                                              
REMARK   3    B13 (A**2) : 0.45000                                              
REMARK   3    B23 (A**2) : -1.86000                                             
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): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL                          
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ; 0.017 ;  NULL       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ; 0.002 ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ; 1.720 ;  NULL       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ; 0.900 ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ; 7.620 ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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 : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : NULL                                          
REMARK   3   ION PROBE RADIUS   : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1Q4O COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-AUG-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB019911.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-JUN-03; 06-JUL-03               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : ELETTRA; ESRF                      
REMARK 200  BEAMLINE                       : 5.2R; ID29                         
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.998; 0.9792                      
REMARK 200  MONOCHROMATOR                  : SI MONCHROMATOR AND TOROIDAL       
REMARK 200                                   FOCUSING MIRROR; SI                
REMARK 200                                   MONCHROMATOR AND CYLINDRICAL       
REMARK 200                                   GRAZING INCIDENCE MIRROR           
REMARK 200  OPTICS                         : MIRRORS; MIRRORS                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH; ADSC QUANTUM 4        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20156                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY                : 2.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.14600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: MODEL DERIVED FROM A SOLVE PHASED MAP FROM DATA      
REMARK 200  OF A SE-MET DERIVATIVE                                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, SODIUM CITRATE AND             
REMARK 280  AMMONIUM ACETATE, PH 6.0, VAPOR DIFFUSION, SITTING DROP,            
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   367                                                      
REMARK 465     GLU A   368                                                      
REMARK 465     VAL A   369                                                      
REMARK 465     VAL A   370                                                      
REMARK 465     ASP A   371                                                      
REMARK 465     ALA A   493                                                      
REMARK 465     GLY A   494                                                      
REMARK 465     ALA A   495                                                      
REMARK 465     ASN A   496                                                      
REMARK 465     ILE A   497                                                      
REMARK 465     THR A   498                                                      
REMARK 465     PRO A   499                                                      
REMARK 465     ARG A   500                                                      
REMARK 465     GLU A   501                                                      
REMARK 465     GLY A   502                                                      
REMARK 465     ASP A   503                                                      
REMARK 465     GLU A   504                                                      
REMARK 465     LEU A   505                                                      
REMARK 465     ALA A   506                                                      
REMARK 465     ARG A   507                                                      
REMARK 465     ARG A   594                                                      
REMARK 465     SER A   595                                                      
REMARK 465     ALA A   596                                                      
REMARK 465     SER A   597                                                      
REMARK 465     ASN A   598                                                      
REMARK 465     ARG A   599                                                      
REMARK 465     LEU A   600                                                      
REMARK 465     LYS A   601                                                      
REMARK 465     ALA A   602                                                      
REMARK 465     SER A   603                                                      
REMARK 465     GLY B   367                                                      
REMARK 465     GLU B   368                                                      
REMARK 465     VAL B   369                                                      
REMARK 465     VAL B   370                                                      
REMARK 465     GLY B   494                                                      
REMARK 465     ALA B   495                                                      
REMARK 465     ASN B   496                                                      
REMARK 465     ILE B   497                                                      
REMARK 465     THR B   498                                                      
REMARK 465     PRO B   499                                                      
REMARK 465     ARG B   500                                                      
REMARK 465     GLU B   501                                                      
REMARK 465     GLY B   502                                                      
REMARK 465     ASP B   503                                                      
REMARK 465     GLU B   504                                                      
REMARK 465     LEU B   505                                                      
REMARK 465     ALA B   506                                                      
REMARK 465     ARG B   507                                                      
REMARK 465     SER B   593                                                      
REMARK 465     ARG B   594                                                      
REMARK 465     SER B   595                                                      
REMARK 465     ALA B   596                                                      
REMARK 465     SER B   597                                                      
REMARK 465     ASN B   598                                                      
REMARK 465     ARG B   599                                                      
REMARK 465     LEU B   600                                                      
REMARK 465     LYS B   601                                                      
REMARK 465     ALA B   602                                                      
REMARK 465     SER B   603                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   N    LEU A   508     O    HOH A    80              2.01            
REMARK 500   O    HOH B    24     O    HOH B    59              2.06            
REMARK 500   O    HOH A    14     O    HOH A   152              2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 429   CB  -  CG  -  OD2 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ASP A 449   CB  -  CG  -  OD2 ANGL. DEV. =   7.4 DEGREES          
REMARK 500    THR A 517   CB  -  CA  -  C   ANGL. DEV. = -19.9 DEGREES          
REMARK 500    THR A 517   N   -  CA  -  C   ANGL. DEV. = -21.2 DEGREES          
REMARK 500    ARG A 518   N   -  CA  -  CB  ANGL. DEV. = -26.5 DEGREES          
REMARK 500    ASP A 554   CB  -  CG  -  OD2 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    ARG A 581   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 581   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ASP B 402   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP B 419   CA  -  CB  -  CG  ANGL. DEV. = -14.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A 373      140.64    174.10                                   
REMARK 500    GLU A 391       74.52   -105.49                                   
REMARK 500    ASP A 419       94.98    -60.70                                   
REMARK 500    LYS A 420       50.90     24.91                                   
REMARK 500    TYR A 421      -70.59   -137.26                                   
REMARK 500    ASP A 449      -44.49   -132.73                                   
REMARK 500    LEU A 491     -155.07   -130.61                                   
REMARK 500    ARG A 518       -8.16    -58.46                                   
REMARK 500    CYS B 372      -11.62    108.87                                   
REMARK 500    LYS B 388       72.34     38.67                                   
REMARK 500    GLU B 391       79.03   -101.16                                   
REMARK 500    TYR B 417       51.37   -118.77                                   
REMARK 500    LYS B 420      -42.48   -136.64                                   
REMARK 500    TYR B 421      -76.95    -91.20                                   
REMARK 500    ASN B 430        8.33     82.68                                   
REMARK 500    ASP B 449      -34.04   -138.59                                   
REMARK 500    HIS B 468       72.75     42.84                                   
REMARK 500    THR B 517      -70.90    -99.99                                   
REMARK 500    ARG B 518      -46.01    169.39                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS A  420     TYR A  421                  146.67                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 162        DISTANCE =  5.64 ANGSTROMS                       
REMARK 525    HOH A 202        DISTANCE =  5.30 ANGSTROMS                       
REMARK 525    HOH A 216        DISTANCE =  6.01 ANGSTROMS                       
REMARK 525    HOH A 217        DISTANCE =  7.18 ANGSTROMS                       
REMARK 525    HOH B 240        DISTANCE =  8.32 ANGSTROMS                       
REMARK 525    HOH B 241        DISTANCE =  6.24 ANGSTROMS                       
REMARK 525    HOH B 243        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH A 225        DISTANCE =  7.49 ANGSTROMS                       
REMARK 525    HOH B 245        DISTANCE =  5.35 ANGSTROMS                       
REMARK 525    HOH B 246        DISTANCE =  7.86 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1Q4K   RELATED DB: PDB                                   
REMARK 900 POLO BOX DOMAIN IN COMPLEX WITH A PHOSPHO-PEPTIDE                    
DBREF  1Q4O A  367   603  UNP    P53350   PLK1_HUMAN     367    603             
DBREF  1Q4O B  367   603  UNP    P53350   PLK1_HUMAN     367    603             
SEQRES   1 A  237  GLY GLU VAL VAL ASP CYS HIS LEU SER ASP MET LEU GLN          
SEQRES   2 A  237  GLN LEU HIS SER VAL ASN ALA SER LYS PRO SER GLU ARG          
SEQRES   3 A  237  GLY LEU VAL ARG GLN GLU GLU ALA GLU ASP PRO ALA CYS          
SEQRES   4 A  237  ILE PRO ILE PHE TRP VAL SER LYS TRP VAL ASP TYR SER          
SEQRES   5 A  237  ASP LYS TYR GLY LEU GLY TYR GLN LEU CYS ASP ASN SER          
SEQRES   6 A  237  VAL GLY VAL LEU PHE ASN ASP SER THR ARG LEU ILE LEU          
SEQRES   7 A  237  TYR ASN ASP GLY ASP SER LEU GLN TYR ILE GLU ARG ASP          
SEQRES   8 A  237  GLY THR GLU SER TYR LEU THR VAL SER SER HIS PRO ASN          
SEQRES   9 A  237  SER LEU MET LYS LYS ILE THR LEU LEU LYS TYR PHE ARG          
SEQRES  10 A  237  ASN TYR MET SER GLU HIS LEU LEU LYS ALA GLY ALA ASN          
SEQRES  11 A  237  ILE THR PRO ARG GLU GLY ASP GLU LEU ALA ARG LEU PRO          
SEQRES  12 A  237  TYR LEU ARG THR TRP PHE ARG THR ARG SER ALA ILE ILE          
SEQRES  13 A  237  LEU HIS LEU SER ASN GLY SER VAL GLN ILE ASN PHE PHE          
SEQRES  14 A  237  GLN ASP HIS THR LYS LEU ILE LEU CYS PRO LEU MET ALA          
SEQRES  15 A  237  ALA VAL THR TYR ILE ASP GLU LYS ARG ASP PHE ARG THR          
SEQRES  16 A  237  TYR ARG LEU SER LEU LEU GLU GLU TYR GLY CYS CYS LYS          
SEQRES  17 A  237  GLU LEU ALA SER ARG LEU ARG TYR ALA ARG THR MET VAL          
SEQRES  18 A  237  ASP LYS LEU LEU SER SER ARG SER ALA SER ASN ARG LEU          
SEQRES  19 A  237  LYS ALA SER                                                  
SEQRES   1 B  237  GLY GLU VAL VAL ASP CYS HIS LEU SER ASP MET LEU GLN          
SEQRES   2 B  237  GLN LEU HIS SER VAL ASN ALA SER LYS PRO SER GLU ARG          
SEQRES   3 B  237  GLY LEU VAL ARG GLN GLU GLU ALA GLU ASP PRO ALA CYS          
SEQRES   4 B  237  ILE PRO ILE PHE TRP VAL SER LYS TRP VAL ASP TYR SER          
SEQRES   5 B  237  ASP LYS TYR GLY LEU GLY TYR GLN LEU CYS ASP ASN SER          
SEQRES   6 B  237  VAL GLY VAL LEU PHE ASN ASP SER THR ARG LEU ILE LEU          
SEQRES   7 B  237  TYR ASN ASP GLY ASP SER LEU GLN TYR ILE GLU ARG ASP          
SEQRES   8 B  237  GLY THR GLU SER TYR LEU THR VAL SER SER HIS PRO ASN          
SEQRES   9 B  237  SER LEU MET LYS LYS ILE THR LEU LEU LYS TYR PHE ARG          
SEQRES  10 B  237  ASN TYR MET SER GLU HIS LEU LEU LYS ALA GLY ALA ASN          
SEQRES  11 B  237  ILE THR PRO ARG GLU GLY ASP GLU LEU ALA ARG LEU PRO          
SEQRES  12 B  237  TYR LEU ARG THR TRP PHE ARG THR ARG SER ALA ILE ILE          
SEQRES  13 B  237  LEU HIS LEU SER ASN GLY SER VAL GLN ILE ASN PHE PHE          
SEQRES  14 B  237  GLN ASP HIS THR LYS LEU ILE LEU CYS PRO LEU MET ALA          
SEQRES  15 B  237  ALA VAL THR TYR ILE ASP GLU LYS ARG ASP PHE ARG THR          
SEQRES  16 B  237  TYR ARG LEU SER LEU LEU GLU GLU TYR GLY CYS CYS LYS          
SEQRES  17 B  237  GLU LEU ALA SER ARG LEU ARG TYR ALA ARG THR MET VAL          
SEQRES  18 B  237  ASP LYS LEU LEU SER SER ARG SER ALA SER ASN ARG LEU          
SEQRES  19 B  237  LYS ALA SER                                                  
FORMUL   3  HOH   *227(H2 O)                                                    
HELIX    1   1 HIS A  373  LYS A  388  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 PRO A  545  MET A  547  5                                   3    
HELIX    7   7 LEU A  564  GLY A  571  1                                   8    
HELIX    8   8 CYS A  573  SER A  593  1                                  21    
HELIX    9   9 CYS B  372  SER B  387  1                                  16    
HELIX   10  10 ARG B  396  ALA B  400  5                                   5    
HELIX   11  11 ASP B  402  ILE B  406  5                                   5    
HELIX   12  12 LEU B  472  LEU B  490  1                                  19    
HELIX   13  13 LEU B  564  GLY B  571  1                                   8    
HELIX   14  14 CYS B  573  SER B  592  1                                  20    
SHEET    1   A 6 VAL A 411  TYR A 417  0                                        
SHEET    2   A 6 GLY A 422  LEU A 427 -1  O  GLY A 424   N  VAL A 415           
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  GLN A 452   N  ILE A 443           
SHEET    6   A 6 GLU A 460  THR A 464 -1  O  SER A 461   N  TYR A 453           
SHEET    1   B 6 LEU A 511  THR A 517  0                                        
SHEET    2   B 6 ALA A 520  LEU A 525 -1  O  HIS A 524   N  THR A 513           
SHEET    3   B 6 VAL A 530  PHE A 534 -1  O  ASN A 533   N  ILE A 521           
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  ALA A 549   N  CYS A 544           
SHEET    6   B 6 PHE A 559  ARG A 563 -1  O  TYR A 562   N  VAL A 550           
SHEET    1   C 6 VAL B 411  TYR B 417  0                                        
SHEET    2   C 6 GLY B 422  LEU B 427 -1  O  GLN B 426   N  LYS B 413           
SHEET    3   C 6 VAL B 432  PHE B 436 -1  O  LEU B 435   N  LEU B 423           
SHEET    4   C 6 ARG B 441  LEU B 444 -1  O  LEU B 444   N  VAL B 432           
SHEET    5   C 6 SER B 450  ILE B 454 -1  O  ILE B 454   N  ARG B 441           
SHEET    6   C 6 GLU B 460  THR B 464 -1  O  LEU B 463   N  LEU B 451           
SHEET    1   D 6 LEU B 511  ARG B 516  0                                        
SHEET    2   D 6 ALA B 520  LEU B 525 -1  O  ILE B 522   N  PHE B 515           
SHEET    3   D 6 VAL B 530  PHE B 534 -1  O  GLN B 531   N  LEU B 523           
SHEET    4   D 6 LYS B 540  CYS B 544 -1  O  LEU B 543   N  VAL B 530           
SHEET    5   D 6 ALA B 549  ILE B 553 -1  O  ILE B 553   N  LYS B 540           
SHEET    6   D 6 PHE B 559  ARG B 563 -1  O  TYR B 562   N  VAL B 550           
CRYST1   32.741   42.021   80.727 103.16  93.88  91.32 P 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      0.030543  0.000703  0.002294        0.00000                         
SCALE2      0.000000  0.023804  0.005620        0.00000                         
SCALE3      0.000000  0.000000  0.012757        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system