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Database: PDB
Entry: 1UMW
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HEADER    KINASE                                  29-AUG-03   1UMW              
TITLE     STRUCTURE OF A HUMAN PLK1 POLO-BOX DOMAIN/PHOSPHOPEPTIDE              
TITLE    2 COMPLEX                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK;                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: POLO-BOX DOMAIN, RESIDUES 367-603;                         
COMPND   5 SYNONYM: PLK1, SERINE THREONINE PROTEIN KINASE 13, STKP13;           
COMPND   6 EC: 2.7.1.-;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PEPTIDE;                                                   
COMPND  10 CHAIN: E, F                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PGEX6P1-LIC;                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES                                                       
KEYWDS    KINASE, PHOSPHOPEPTIDE-BINDING DOMAIN, TRANSFERASE                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.RELLOS,A.ELIA,M.B.YAFFE,S.J.SMERDON                                 
REVDAT   2   24-FEB-09 1UMW    1       VERSN                                    
REVDAT   1   16-OCT-03 1UMW    0                                                
JRNL        AUTH   A.ELIA,P.RELLOS,L.HAIRE,J.CHAO,F.IVINS,K.HOEPKER,            
JRNL        AUTH 2 D.MOHAMMAD,L.CANTLEY,S.J.SMERDON,M.B.YAFFE                   
JRNL        TITL   THE MOLECULAR BASIS FOR PHOSPHODEPENDENT SUBSTRATE           
JRNL        TITL 2 TARGETING AND REGULATION OF PLKS BY THE POLO-BOX             
JRNL        TITL 3 DOMAIN                                                       
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 115    83 2003              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   14532005                                                     
JRNL        DOI    10.1016/S0092-8674(03)00725-6                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.9  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 44210                          
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) : 0.229                           
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2352                            
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3278                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2670                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 169                          
REMARK   3   BIN FREE R VALUE                    : 0.3050                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3686                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 22                                      
REMARK   3   SOLVENT ATOMS            : 275                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.25                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.02000                                              
REMARK   3    B22 (A**2) : 0.71000                                              
REMARK   3    B33 (A**2) : -1.88000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.30000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.166         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.153         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.110         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.660         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.935                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.909                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3759 ; 0.007 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5069 ; 1.176 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   447 ; 3.310 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   701 ;17.837 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   566 ; 0.083 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2781 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1778 ; 0.262 ; 0.300       
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):   387 ; 0.181 ; 0.500       
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):    36 ; 0.216 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    19 ; 0.265 ; 0.500       
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):  2273 ; 0.648 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3650 ; 1.211 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1486 ; 1.543 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1419 ; 2.561 ; 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  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    20        A    52                          
REMARK   3    RESIDUE RANGE :   A   155        A   241                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.0060  10.6415  10.5836              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0785 T22:   0.0870                                     
REMARK   3      T33:   0.0697 T12:  -0.0173                                     
REMARK   3      T13:   0.0135 T23:   0.0050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0924 L22:   0.7790                                     
REMARK   3      L33:   0.5890 L12:  -0.0743                                     
REMARK   3      L13:   0.0913 L23:   0.3080                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0026 S12:  -0.0129 S13:  -0.0054                       
REMARK   3      S21:   0.0356 S22:  -0.0427 S23:   0.0298                       
REMARK   3      S31:  -0.0268 S32:   0.0321 S33:   0.0401                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    53        A   146                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.2894  -2.2549  -9.1894              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0880 T22:   0.0761                                     
REMARK   3      T33:   0.0819 T12:   0.0112                                     
REMARK   3      T13:  -0.0087 T23:  -0.0148                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2902 L22:   0.4473                                     
REMARK   3      L33:   0.6825 L12:  -0.1226                                     
REMARK   3      L13:  -0.2699 L23:   0.4066                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0064 S12:   0.0411 S13:  -0.0368                       
REMARK   3      S21:  -0.0572 S22:  -0.0749 S23:   0.0592                       
REMARK   3      S31:  -0.0106 S32:  -0.0714 S33:   0.0684                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   147        A   154                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.2075  15.7888 -11.6201              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1318 T22:   0.1406                                     
REMARK   3      T33:   0.1883 T12:  -0.0809                                     
REMARK   3      T13:  -0.0010 T23:  -0.0395                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6482 L22:  -2.8633                                     
REMARK   3      L33:  23.2865 L12:  -3.4026                                     
REMARK   3      L13:  -7.7728 L23:  -6.9806                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4419 S12:   0.6344 S13:   0.5081                       
REMARK   3      S21:  -0.8781 S22:  -0.3704 S23:  -0.5249                       
REMARK   3      S31:  -0.4815 S32:  -0.3607 S33:  -0.0715                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    20        B    52                          
REMARK   3    RESIDUE RANGE :   B   155        B   241                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.2965  -3.5070 -31.8055              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0812 T22:   0.0601                                     
REMARK   3      T33:   0.0768 T12:   0.0139                                     
REMARK   3      T13:  -0.0081 T23:   0.0167                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8533 L22:   0.3556                                     
REMARK   3      L33:   0.9997 L12:   0.1328                                     
REMARK   3      L13:   0.2718 L23:   0.4472                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0084 S12:   0.0427 S13:   0.0474                       
REMARK   3      S21:   0.0316 S22:   0.0462 S23:  -0.0668                       
REMARK   3      S31:   0.0593 S32:   0.0022 S33:  -0.0378                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    53        B   146                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.4493   4.8280 -26.0810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0037 T22:   0.1227                                     
REMARK   3      T33:   0.1257 T12:  -0.0009                                     
REMARK   3      T13:  -0.0186 T23:  -0.0567                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9540 L22:   1.2176                                     
REMARK   3      L33:   1.1722 L12:   0.7559                                     
REMARK   3      L13:   0.7405 L23:   0.5507                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0286 S12:   0.0798 S13:  -0.0265                       
REMARK   3      S21:  -0.0030 S22:   0.1229 S23:  -0.1348                       
REMARK   3      S31:  -0.0952 S32:   0.2446 S33:  -0.0943                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   147        B   154                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.1027   8.1634 -44.6438              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0907 T22:   0.0903                                     
REMARK   3      T33:   0.0904 T12:   0.0012                                     
REMARK   3      T13:  -0.0014 T23:  -0.0011                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  44.0812 L22:  42.2758                                     
REMARK   3      L33:  29.6575 L12:  36.3444                                     
REMARK   3      L13:   7.2698 L23:   0.3682                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0947 S12:   1.2835 S13:   0.6461                       
REMARK   3      S21:  -1.0429 S22:   1.0736 S23:   0.0736                       
REMARK   3      S31:  -1.2980 S32:   1.3473 S33:  -0.9788                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1UMW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-SEP-03.                  
REMARK 100 THE PDBE ID CODE IS EBI-13396.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX14.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.244                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50058                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.05300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       39.75900            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E                                  
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 BIOMOLECULE:  2                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F                                  
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  MAY BE REQUIRED FOR CELL DIVISION AND MAY HAVE A ROLE               
REMARK 400  DURING G1 OR S PHASE.                                               
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     CYS A   372                                                      
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     ASP B   371                                                      
REMARK 465     CYS B   372                                                      
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 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     HIS A 373    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG A 594    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 595    CA   C    O    CB   OG                              
REMARK 470     HIS B 373    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG B 594    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 595    CA   C    O    CB   OG                              
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   CG   ASP A   447  -  O    HOH A  2054              1.77            
REMARK 500   OD1  ASP A   447  -  O    HOH A  2054              1.62            
REMARK 500   O    ALA A   493  -  O    HOH A  2089              2.19            
REMARK 500   O    ASP B   447  -  N    ASP B   449              1.86            
REMARK 500   NH1  ARG B   557  -  O    HOH B  2068              2.15            
REMARK 500   O    HOH A  2045  -  O    HOH A  2122              1.97            
REMARK 500   O    HOH A  2062  -  O    HOH A  2128              2.12            
REMARK 500   O    HOH B  2003  -  O    HOH B  2045              2.03            
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 B 402   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    SER F   4   O   -  C   -  N   ANGL. DEV. = -14.6 DEGREES          
REMARK 500    PRO F   6   C   -  N   -  CA  ANGL. DEV. = -13.8 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 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    GLU A 391       40.57   -104.63                                   
REMARK 500    LYS A 420      -34.10   -138.16                                   
REMARK 500    ASN A 430       -2.01     82.39                                   
REMARK 500    ASP A 449      -36.39   -138.05                                   
REMARK 500    ASP A 503     -125.12     63.92                                   
REMARK 500    GLU A 504      -18.37    137.47                                   
REMARK 500    ALA A 506       98.35   -172.79                                   
REMARK 500    ARG A 507       12.60   -165.19                                   
REMARK 500    GLU A 575      -69.36    100.01                                   
REMARK 500    GLU B 391       58.02    -98.56                                   
REMARK 500    ALA B 404        0.11    -67.62                                   
REMARK 500    CYS B 428       -7.79    -49.71                                   
REMARK 500    ASN B 430      -10.51     86.68                                   
REMARK 500    SER B 439       -4.79     76.17                                   
REMARK 500    ASN B 446       16.95    -62.03                                   
REMARK 500    ASP B 449      -65.72   -136.30                                   
REMARK 500    SER B 461      120.72   -175.70                                   
REMARK 500    LEU B 463     -155.77   -124.68                                   
REMARK 500    SER B 467       34.05    -96.57                                   
REMARK 500    HIS B 468       69.05     -0.56                                   
REMARK 500    PRO B 499     -178.33    -57.13                                   
REMARK 500    ARG B 500     -161.18   -112.02                                   
REMARK 500    GLU B 504      -37.11    -23.43                                   
REMARK 500    ALA B 506       76.74   -177.27                                   
REMARK 500    LEU B 508      109.21    169.50                                   
REMARK 500    SER B 593       57.42   -106.12                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    SER F   4         21.17                                           
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):                                           
DBREF  1UMW A  367   603  UNP    P53350   PLK_HUMAN      367    603             
DBREF  1UMW B  367   603  UNP    P53350   PLK_HUMAN      367    603             
DBREF  1UMW E    1     7  PDB    1UMW     1UMW             1      7             
DBREF  1UMW F    1     7  PDB    1UMW     1UMW             1      7             
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                                                  
SEQRES   1 E    7  PRO MET GLN SER TPO PRO LEU                                  
SEQRES   1 F    7  PRO MET GLN SER TPO PRO LEU                                  
MODRES 1UMW TPO E    5  THR  PHOSPHOTHREONINE                                   
MODRES 1UMW TPO F    5  THR  PHOSPHOTHREONINE                                   
HET    TPO  E   5      11                                                       
HET    TPO  F   5      11                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   3  TPO    2(C4 H10 N O6 P)                                             
FORMUL   5  HOH   *275(H2 O1)                                                   
HELIX    1   1 HIS A  373  SER A  387  1                                  15    
HELIX    2   2 ARG A  396  ALA A  400  5                                   5    
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 GLU A  575  SER A  593  1                                  19    
HELIX    8   8 HIS B  373  SER B  387  1                                  15    
HELIX    9   9 ARG B  396  ALA B  400  5                                   5    
HELIX   10  10 ASP B  402  ILE B  406  5                                   5    
HELIX   11  11 LEU B  472  LEU B  490  1                                  19    
HELIX   12  12 LEU B  564  GLY B  571  1                                   8    
HELIX   13  13 CYS B  573  SER B  593  1                                  21    
SHEET    1  AA 6 VAL A 411  ASP A 416  0                                        
SHEET    2  AA 6 GLY A 422  LEU A 427 -1  O  GLY A 424   N  VAL A 415           
SHEET    3  AA 6 VAL A 432  PHE A 436 -1  O  GLY A 433   N  TYR A 425           
SHEET    4  AA 6 ARG A 441  LEU A 444 -1  O  LEU A 442   N  VAL A 434           
SHEET    5  AA 6 SER A 450  ILE A 454 -1  O  GLN A 452   N  ILE A 443           
SHEET    6  AA 6 GLU A 460  THR A 464 -1  O  SER A 461   N  TYR A 453           
SHEET    1  AB 6 LEU A 511  ARG A 516  0                                        
SHEET    2  AB 6 ALA A 520  LEU A 525 -1  O  ILE A 522   N  PHE A 515           
SHEET    3  AB 6 VAL A 530  PHE A 534 -1  O  GLN A 531   N  LEU A 523           
SHEET    4  AB 6 LYS A 540  CYS A 544 -1  O  LEU A 541   N  ILE A 532           
SHEET    5  AB 6 ALA A 549  ILE A 553 -1  O  ALA A 549   N  CYS A 544           
SHEET    6  AB 6 PHE A 559  ARG A 563 -1  O  ARG A 560   N  TYR A 552           
SHEET    1  BA 6 VAL B 411  ASP B 416  0                                        
SHEET    2  BA 6 GLY B 422  LEU B 427 -1  O  GLY B 424   N  VAL B 415           
SHEET    3  BA 6 VAL B 432  PHE B 436 -1  O  GLY B 433   N  TYR B 425           
SHEET    4  BA 6 ARG B 441  LEU B 444 -1  O  LEU B 442   N  VAL B 434           
SHEET    5  BA 6 SER B 450  ILE B 454 -1  O  GLN B 452   N  ILE B 443           
SHEET    6  BA 6 TYR B 462  THR B 464 -1  O  LEU B 463   N  LEU B 451           
SHEET    1  BB 6 LEU B 511  ARG B 516  0                                        
SHEET    2  BB 6 ALA B 520  LEU B 525 -1  O  ILE B 522   N  PHE B 515           
SHEET    3  BB 6 VAL B 530  PHE B 534 -1  O  GLN B 531   N  LEU B 523           
SHEET    4  BB 6 LYS B 540  CYS B 544 -1  O  LEU B 541   N  ILE B 532           
SHEET    5  BB 6 ALA B 549  ILE B 553 -1  O  ALA B 549   N  CYS B 544           
SHEET    6  BB 6 PHE B 559  ARG B 563 -1  O  ARG B 560   N  TYR B 552           
LINK         C   SER E   4                 N   TPO E   5     1555   1555  1.33  
LINK         C   TPO E   5                 N   PRO E   6     1555   1555  1.33  
LINK         C   SER F   4                 N   TPO F   5     1555   1555  1.33  
LINK         C   TPO F   5                 N   PRO F   6     1555   1555  1.33  
CRYST1   62.352   79.518   61.993  90.00  93.26  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016038  0.000000  0.000913        0.00000                         
SCALE2      0.000000  0.012576  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016157        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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