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Database: PDB
Entry: 4E67
LinkDB: 4E67
Original site: 4E67 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       15-MAR-12   4E67              
TITLE     THE STRUCTURE OF THE POLO-BOX DOMAIN (PBD) OF POLO-LIKE KINASE 1      
TITLE    2 (PLK1) IN COMPLEX WITH HYDROCINNAMOYL-DERIVATIZED PLHSPTA PEPTIDE    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK1;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: POLO BOX DOMAIN (PBD), RESIDUES 371-594;                   
COMPND   5 SYNONYM: POLO-LIKE KINASE 1, PLK-1, SERINE/THREONINE-PROTEIN KINASE  
COMPND   6 13, STPK13;                                                          
COMPND   7 EC: 2.7.11.21;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: HYDROCINNAMOYL-DERIVATIZED PLHSPTA PEPTIDE;                
COMPND  11 CHAIN: B;                                                            
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PLK1, PLK;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 OTHER_DETAILS: SOLID-STATE PEPTIDE SYNTHESIS                         
KEYWDS    SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE, PHOSPHOPROTEIN-BINDING  
KEYWDS   2 DOMAIN, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.SLEDZ,M.HYVONEN,Y.S.TAN,S.LANG,D.SPRING,C.ABELL,R.B.BEST            
REVDAT   1   10-OCT-12 4E67    0                                                
JRNL        AUTH   Y.S.TAN,P.SLEDZ,S.LANG,C.J.STUBBS,D.R.SPRING,C.ABELL,        
JRNL        AUTH 2 R.B.BEST                                                     
JRNL        TITL   USING LIGAND-MAPPING SIMULATIONS TO DESIGN A LIGAND          
JRNL        TITL 2 SELECTIVELY TARGETING A CRYPTIC SURFACE POCKET OF POLO-LIKE  
JRNL        TITL 3 KINASE 1.                                                    
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.       V.  51 10078 2012              
JRNL        REFN                   ISSN 1433-7851                               
JRNL        PMID   22961729                                                     
JRNL        DOI    10.1002/ANIE.201205676                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 56.84                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 11235                          
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) : 0.218                           
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.265                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 562                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 700                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 84.81                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2550                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 37                           
REMARK   3   BIN FREE R VALUE                    : 0.2810                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1768                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 76                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.27                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.322         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.231         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.156         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.669         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.926                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.885                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1815 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2463 ; 1.034 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   221 ; 5.355 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    82 ;29.562 ;22.683       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   307 ;15.614 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;19.755 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   277 ; 0.067 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1361 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1103 ; 0.358 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1777 ; 0.692 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   712 ; 0.941 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   684 ; 1.530 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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 4E67 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAR-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB071219.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : BRUKER AXS MICROSTAR               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5406                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : BRUKER PLATINUM 135                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : PROTEUM PLUS                       
REMARK 200  DATA SCALING SOFTWARE          : PROTEUM PLUS                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11821                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 56.840                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3P2Z                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 33.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES (PH 7.5), 0.1 M SODIUM       
REMARK 280  AZIDE AND 22% PEG 4000, VAPOR DIFFUSION, SITTING DROP,              
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       25.45300            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400                                                                      
REMARK 400 THE HYDROCINNAMOYL-DERIVATIZED PLHSPTA PEPTIDE IS PEPTIDE-LIKE, A    
REMARK 400 MEMBER OF ENZYME INHIBITOR CLASS.                                    
REMARK 400                                                                      
REMARK 400  GROUP: 1                                                            
REMARK 400   NAME: HYDROCINNAMOYL-DERIVATIZED PLHSPTA PEPTIDE                   
REMARK 400   CHAIN: B                                                           
REMARK 400   COMPONENT_1: PEPTIDE LIKE POLYMER                                  
REMARK 400   DESCRIPTION: NULL                                                  
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   363                                                      
REMARK 465     PRO A   364                                                      
REMARK 465     LEU A   365                                                      
REMARK 465     GLY A   366                                                      
REMARK 465     SER A   367                                                      
REMARK 465     PRO A   368                                                      
REMARK 465     GLU A   369                                                      
REMARK 465     PHE A   370                                                      
REMARK 465     ASP A   371                                                      
REMARK 465     CYS A   372                                                      
REMARK 465     HIS A   373                                                      
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 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     LYS A 388    CG   CD   CE   NZ                                   
REMARK 470     GLU A 398    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 555    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 556    CG   CD   CE   NZ                                   
REMARK 470     LYS A 574    CG   CD   CE   NZ                                   
REMARK 470     GLU A 575    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 392       46.59   -141.84                                   
REMARK 500    TYR A 421      -51.35   -120.59                                   
REMARK 500    ASP A 449      -42.66   -134.80                                   
REMARK 500    LEU A 463     -159.67   -157.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF HYDROCINNAMOYL-        
REMARK 800  DERIVATIZED PLHSPTA PEPTIDE                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4E9C   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4E9D   RELATED DB: PDB                                   
DBREF  4E67 A  371   594  UNP    P53350   PLK1_HUMAN     371    594             
DBREF  4E67 B    0     7  PDB    4E67     4E67             0      7             
SEQADV 4E67 GLY A  363  UNP  P53350              EXPRESSION TAG                 
SEQADV 4E67 PRO A  364  UNP  P53350              EXPRESSION TAG                 
SEQADV 4E67 LEU A  365  UNP  P53350              EXPRESSION TAG                 
SEQADV 4E67 GLY A  366  UNP  P53350              EXPRESSION TAG                 
SEQADV 4E67 SER A  367  UNP  P53350              EXPRESSION TAG                 
SEQADV 4E67 PRO A  368  UNP  P53350              EXPRESSION TAG                 
SEQADV 4E67 GLU A  369  UNP  P53350              EXPRESSION TAG                 
SEQADV 4E67 PHE A  370  UNP  P53350              EXPRESSION TAG                 
SEQRES   1 A  232  GLY PRO LEU GLY SER PRO GLU PHE ASP CYS HIS LEU SER          
SEQRES   2 A  232  ASP MET LEU GLN GLN LEU HIS SER VAL ASN ALA SER LYS          
SEQRES   3 A  232  PRO SER GLU ARG GLY LEU VAL ARG GLN GLU GLU ALA GLU          
SEQRES   4 A  232  ASP PRO ALA CYS ILE PRO ILE PHE TRP VAL SER LYS TRP          
SEQRES   5 A  232  VAL ASP TYR SER ASP LYS TYR GLY LEU GLY TYR GLN LEU          
SEQRES   6 A  232  CYS ASP ASN SER VAL GLY VAL LEU PHE ASN ASP SER THR          
SEQRES   7 A  232  ARG LEU ILE LEU TYR ASN ASP GLY ASP SER LEU GLN TYR          
SEQRES   8 A  232  ILE GLU ARG ASP GLY THR GLU SER TYR LEU THR VAL SER          
SEQRES   9 A  232  SER HIS PRO ASN SER LEU MET LYS LYS ILE THR LEU LEU          
SEQRES  10 A  232  LYS TYR PHE ARG ASN TYR MET SER GLU HIS LEU LEU LYS          
SEQRES  11 A  232  ALA GLY ALA ASN ILE THR PRO ARG GLU GLY ASP GLU LEU          
SEQRES  12 A  232  ALA ARG LEU PRO TYR LEU ARG THR TRP PHE ARG THR ARG          
SEQRES  13 A  232  SER ALA ILE ILE LEU HIS LEU SER ASN GLY SER VAL GLN          
SEQRES  14 A  232  ILE ASN PHE PHE GLN ASP HIS THR LYS LEU ILE LEU CYS          
SEQRES  15 A  232  PRO LEU MET ALA ALA VAL THR TYR ILE ASP GLU LYS ARG          
SEQRES  16 A  232  ASP PHE ARG THR TYR ARG LEU SER LEU LEU GLU GLU TYR          
SEQRES  17 A  232  GLY CYS CYS LYS GLU LEU ALA SER ARG LEU ARG TYR ALA          
SEQRES  18 A  232  ARG THR MET VAL ASP LYS LEU LEU SER SER ARG                  
SEQRES   1 B    8  HCI PRO LEU HIS SER TPO ALA NH2                              
MODRES 4E67 TPO B    5  THR  PHOSPHOTHREONINE                                   
HET    HCI  B   0      10                                                       
HET    TPO  B   5      11                                                       
HET    NH2  B   7       1                                                       
HETNAM     HCI HYDROCINNAMIC ACID                                               
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     NH2 AMINO GROUP                                                      
HETSYN     HCI 3PP; 3-PHENYLPROPIONIC ACID                                      
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   2  HCI    C9 H10 O2                                                    
FORMUL   2  TPO    C4 H10 N O6 P                                                
FORMUL   2  NH2    H2 N                                                         
FORMUL   3  HOH   *76(H2 O)                                                     
HELIX    1   1 LEU A  374  SER A  387  1                                  14    
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 SER A  466  HIS A  468  5                                   3    
HELIX    5   5 PRO A  469  SER A  471  5                                   3    
HELIX    6   6 LEU A  472  LEU A  490  1                                  19    
HELIX    7   7 LEU A  564  GLY A  571  1                                   8    
HELIX    8   8 CYS A  573  SER A  593  1                                  21    
SHEET    1   A 7 GLU A 460  THR A 464  0                                        
SHEET    2   A 7 SER A 450  ILE A 454 -1  N  TYR A 453   O  SER A 461           
SHEET    3   A 7 ARG A 441  LEU A 444 -1  N  ILE A 443   O  GLN A 452           
SHEET    4   A 7 VAL A 432  PHE A 436 -1  N  VAL A 432   O  LEU A 444           
SHEET    5   A 7 GLY A 422  LEU A 427 -1  N  TYR A 425   O  GLY A 433           
SHEET    6   A 7 VAL A 411  ASP A 416 -1  N  VAL A 415   O  GLY A 424           
SHEET    7   A 7 LEU B   2  HIS B   3 -1  O  LEU B   2   N  ASP A 416           
SHEET    1   B 6 LEU A 511  ARG A 516  0                                        
SHEET    2   B 6 ALA A 520  LEU A 525 -1  O  ILE A 522   N  PHE A 515           
SHEET    3   B 6 VAL A 530  PHE A 534 -1  O  GLN A 531   N  LEU A 523           
SHEET    4   B 6 LYS A 540  CYS A 544 -1  O  LEU A 543   N  VAL A 530           
SHEET    5   B 6 ALA A 549  ILE A 553 -1  O  ILE A 553   N  LYS A 540           
SHEET    6   B 6 PHE A 559  ARG A 563 -1  O  TYR A 562   N  VAL A 550           
LINK         C   SER B   4                 N   TPO B   5     1555   1555  1.33  
LINK         C   TPO B   5                 N   ALA B   6     1555   1555  1.33  
LINK         C   ALA B   6                 N   NH2 B   7     1555   1555  1.26  
LINK         C1  HCI B   0                 N   PRO B   1     1555   1555  1.35  
SITE     1 AC1 22 LYS A 413  TRP A 414  VAL A 415  ASP A 416                    
SITE     2 AC1 22 TYR A 417  ASP A 419  TYR A 481  PHE A 482                    
SITE     3 AC1 22 TYR A 485  HIS A 489  LEU A 490  LEU A 491                    
SITE     4 AC1 22 ARG A 516  HIS A 538  LYS A 540  HOH A 601                    
SITE     5 AC1 22 HOH A 605  HOH B 101  HOH B 102  HOH B 103                    
SITE     6 AC1 22 HOH B 104  HOH B 105                                          
CRYST1   35.492   50.906   57.910  90.00 101.01  90.00 P 1 21 1      2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.028175  0.000000  0.005483        0.00000                         
SCALE2      0.000000  0.019644  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017592        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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