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Database: PDB
Entry: 1Q4K
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HEADER    TRANSFERASE                             04-AUG-03   1Q4K              
TITLE     THE POLO-BOX DOMAIN OF PLK1 IN COMPLEX WITH A PHOSPHO-                
TITLE    2 PEPTIDE                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK;                       
COMPND   3 CHAIN: B, A, C;                                                      
COMPND   4 FRAGMENT: POLO BOX DOMAIN OF HUMAN PLK1;                             
COMPND   5 SYNONYM: PLK-1, SERINE-THREONINE PROTEIN KINASE 13, STPK13;          
COMPND   6 EC: 2.7.1.-;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: PHOSPHO-PEPTIDE SEQUENCE                                   
COMPND  11 MET.GLN.SER.PTHR.PRO.LEU;                                            
COMPND  12 CHAIN: D, E, F;                                                      
COMPND  13 FRAGMENT: PHOSPHO-PEPTIDE;                                           
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MUTATION: 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;                                                          
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;                                 
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: CHEMICAL SYNTHESIS                                    
KEYWDS    SIX-STRANDED ANTI-PARALLEL BETA SHEET WITH ONE ALPHA HELIX,           
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.CHENG,E.D.LOWE,J.SINCLAIR,E.A.NIGG,L.N.JOHNSON                      
REVDAT   2   24-FEB-09 1Q4K    1       VERSN                                    
REVDAT   1   11-NOV-03 1Q4K    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.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.36                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 36665                          
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) : 0.248                           
REMARK   3   R VALUE            (WORKING SET) : 0.245                           
REMARK   3   FREE R VALUE                     : 0.312                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1943                            
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2705                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2600                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 153                          
REMARK   3   BIN FREE R VALUE                    : 0.3540                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5516                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 191                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 49.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.65                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : -0.01000                                             
REMARK   3    B12 (A**2) : 0.01000                                              
REMARK   3    B13 (A**2) : -0.01000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.373         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.291         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.196         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.791         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.909                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.861                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5628 ; 0.012 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  5100 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7608 ; 1.591 ; 1.970       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11854 ; 1.269 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   671 ; 7.213 ; 5.000       
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):   842 ; 0.090 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6138 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1185 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1264 ; 0.201 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  6263 ; 0.229 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3546 ; 0.094 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   199 ; 0.194 ; 0.200       
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):    28 ; 0.238 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    95 ; 0.265 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.337 ; 0.200       
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):  3377 ; 0.707 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5450 ; 1.341 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2251 ; 1.778 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2158 ; 3.048 ; 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 : 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: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 1Q4K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-AUG-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB019907.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-JUL-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : SI MONOCHROMATOR                   
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37228                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.360                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY                : 1.900                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : 0.09600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 2.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.25800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: UNLIGANDED POLO BOX DOMAIN                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 20000, MES, PH 6.5, VAPOR            
REMARK 280  DIFFUSION, SITTING DROP, 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, 3                                                 
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: 1050 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 1030 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
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: 3                                                       
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: 1020 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11490 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 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     LYS B   345                                                      
REMARK 465     GLY B   346                                                      
REMARK 465     LEU B   347                                                      
REMARK 465     GLU B   348                                                      
REMARK 465     ASN B   349                                                      
REMARK 465     PRO B   350                                                      
REMARK 465     LEU B   351                                                      
REMARK 465     PRO B   352                                                      
REMARK 465     GLU B   353                                                      
REMARK 465     ARG B   354                                                      
REMARK 465     PRO B   355                                                      
REMARK 465     ARG B   356                                                      
REMARK 465     GLU B   357                                                      
REMARK 465     LYS B   358                                                      
REMARK 465     GLU B   359                                                      
REMARK 465     GLU B   360                                                      
REMARK 465     PRO B   361                                                      
REMARK 465     VAL B   362                                                      
REMARK 465     VAL B   363                                                      
REMARK 465     ARG B   364                                                      
REMARK 465     GLU B   365                                                      
REMARK 465     THR B   366                                                      
REMARK 465     GLY B   367                                                      
REMARK 465     GLU B   368                                                      
REMARK 465     VAL B   369                                                      
REMARK 465     VAL B   370                                                      
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 465     LYS A   345                                                      
REMARK 465     GLY A   346                                                      
REMARK 465     LEU A   347                                                      
REMARK 465     GLU A   348                                                      
REMARK 465     ASN A   349                                                      
REMARK 465     PRO A   350                                                      
REMARK 465     LEU A   351                                                      
REMARK 465     PRO A   352                                                      
REMARK 465     GLU A   353                                                      
REMARK 465     ARG A   354                                                      
REMARK 465     PRO A   355                                                      
REMARK 465     ARG A   356                                                      
REMARK 465     GLU A   357                                                      
REMARK 465     LYS A   358                                                      
REMARK 465     GLU A   359                                                      
REMARK 465     GLU A   360                                                      
REMARK 465     PRO A   361                                                      
REMARK 465     VAL A   362                                                      
REMARK 465     VAL A   363                                                      
REMARK 465     ARG A   364                                                      
REMARK 465     GLU A   365                                                      
REMARK 465     THR A   366                                                      
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     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     LYS C   345                                                      
REMARK 465     GLY C   346                                                      
REMARK 465     LEU C   347                                                      
REMARK 465     GLU C   348                                                      
REMARK 465     ASN C   349                                                      
REMARK 465     PRO C   350                                                      
REMARK 465     LEU C   351                                                      
REMARK 465     PRO C   352                                                      
REMARK 465     GLU C   353                                                      
REMARK 465     ARG C   354                                                      
REMARK 465     PRO C   355                                                      
REMARK 465     ARG C   356                                                      
REMARK 465     GLU C   357                                                      
REMARK 465     LYS C   358                                                      
REMARK 465     GLU C   359                                                      
REMARK 465     GLU C   360                                                      
REMARK 465     PRO C   361                                                      
REMARK 465     VAL C   362                                                      
REMARK 465     VAL C   363                                                      
REMARK 465     ARG C   364                                                      
REMARK 465     GLU C   365                                                      
REMARK 465     THR C   366                                                      
REMARK 465     GLY C   367                                                      
REMARK 465     GLU C   368                                                      
REMARK 465     VAL C   369                                                      
REMARK 465     VAL C   370                                                      
REMARK 465     ASP C   371                                                      
REMARK 465     ALA C   495                                                      
REMARK 465     ASN C   496                                                      
REMARK 465     ILE C   497                                                      
REMARK 465     THR C   498                                                      
REMARK 465     PRO C   499                                                      
REMARK 465     ARG C   500                                                      
REMARK 465     GLU C   501                                                      
REMARK 465     GLY C   502                                                      
REMARK 465     ARG C   594                                                      
REMARK 465     SER C   595                                                      
REMARK 465     ALA C   596                                                      
REMARK 465     SER C   597                                                      
REMARK 465     ASN C   598                                                      
REMARK 465     ARG C   599                                                      
REMARK 465     LEU C   600                                                      
REMARK 465     LYS C   601                                                      
REMARK 465     ALA C   602                                                      
REMARK 465     SER C   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   O    ALA A   493     O    HOH A    21              2.04            
REMARK 500   C    THR B   517     O    HOH B    36              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NZ   LYS C   589     O    HOH B    13     1554     1.91            
REMARK 500   OD2  ASP B   419     OH   TYR A   445     1455     2.19            
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 537   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP B 554   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP A 537   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP C 376   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP C 416   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 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    CYS B 372       -7.82     81.78                                   
REMARK 500    GLU B 391       63.47   -113.26                                   
REMARK 500    TYR B 417       51.71   -110.29                                   
REMARK 500    LYS B 420       -1.97   -153.87                                   
REMARK 500    ASN B 430       -2.80     74.34                                   
REMARK 500    ASP B 438       22.14    -78.34                                   
REMARK 500    ASP B 449      -45.30   -137.49                                   
REMARK 500    ASN B 496       43.21    -94.91                                   
REMARK 500    GLU B 504      114.16     61.51                                   
REMARK 500    THR B 517     -106.62    -99.06                                   
REMARK 500    HIS B 538       17.75     58.77                                   
REMARK 500    GLU A 391       68.63   -101.49                                   
REMARK 500    ARG A 396       56.45   -119.81                                   
REMARK 500    TYR A 421      -61.88   -131.37                                   
REMARK 500    ASN A 430       -1.67     81.50                                   
REMARK 500    ASP A 449      -53.16   -146.58                                   
REMARK 500    SER A 467       25.78    110.55                                   
REMARK 500    GLU A 504      109.55      5.84                                   
REMARK 500    THR A 517      -74.01   -108.33                                   
REMARK 500    CYS A 573      136.11     -5.06                                   
REMARK 500    TYR C 417       46.27   -108.94                                   
REMARK 500    LYS C 420      -45.17   -146.88                                   
REMARK 500    ASN C 430       -0.99     64.20                                   
REMARK 500    ASP C 449      -65.87   -146.16                                   
REMARK 500    GLU C 504      -43.26     50.75                                   
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 THR A  517     ARG A  518                   59.72                    
REMARK 500 CYS A  572     CYS A  573                  149.43                    
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 109        DISTANCE =  6.29 ANGSTROMS                       
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 NO SEQUENCE DATABASE REFERENCE FOUND FOR PHOSPHO-PEPTIDE             
REMARK 999 (ENTITY 2, CHAINS D,E,F)AT THE TIME OF PROCESSING                    
DBREF  1Q4K A  345   603  UNP    P53350   PLK1_HUMAN     345    603             
DBREF  1Q4K B  345   603  UNP    P53350   PLK1_HUMAN     345    603             
DBREF  1Q4K C  345   603  UNP    P53350   PLK1_HUMAN     345    603             
DBREF  1Q4K D    1     6  PDB    1Q4K     1Q4K             1      6             
DBREF  1Q4K E    1     6  PDB    1Q4K     1Q4K             1      6             
DBREF  1Q4K F    1     6  PDB    1Q4K     1Q4K             1      6             
SEQRES   1 B  259  LYS GLY LEU GLU ASN PRO LEU PRO GLU ARG PRO ARG GLU          
SEQRES   2 B  259  LYS GLU GLU PRO VAL VAL ARG GLU THR GLY GLU VAL VAL          
SEQRES   3 B  259  ASP CYS HIS LEU SER ASP MET LEU GLN GLN LEU HIS SER          
SEQRES   4 B  259  VAL ASN ALA SER LYS PRO SER GLU ARG GLY LEU VAL ARG          
SEQRES   5 B  259  GLN GLU GLU ALA GLU ASP PRO ALA CYS ILE PRO ILE PHE          
SEQRES   6 B  259  TRP VAL SER LYS TRP VAL ASP TYR SER ASP LYS TYR GLY          
SEQRES   7 B  259  LEU GLY TYR GLN LEU CYS ASP ASN SER VAL GLY VAL LEU          
SEQRES   8 B  259  PHE ASN ASP SER THR ARG LEU ILE LEU TYR ASN ASP GLY          
SEQRES   9 B  259  ASP SER LEU GLN TYR ILE GLU ARG ASP GLY THR GLU SER          
SEQRES  10 B  259  TYR LEU THR VAL SER SER HIS PRO ASN SER LEU MET LYS          
SEQRES  11 B  259  LYS ILE THR LEU LEU LYS TYR PHE ARG ASN TYR MET SER          
SEQRES  12 B  259  GLU HIS LEU LEU LYS ALA GLY ALA ASN ILE THR PRO ARG          
SEQRES  13 B  259  GLU GLY ASP GLU LEU ALA ARG LEU PRO TYR LEU ARG THR          
SEQRES  14 B  259  TRP PHE ARG THR ARG SER ALA ILE ILE LEU HIS LEU SER          
SEQRES  15 B  259  ASN GLY SER VAL GLN ILE ASN PHE PHE GLN ASP HIS THR          
SEQRES  16 B  259  LYS LEU ILE LEU CYS PRO LEU MET ALA ALA VAL THR TYR          
SEQRES  17 B  259  ILE ASP GLU LYS ARG ASP PHE ARG THR TYR ARG LEU SER          
SEQRES  18 B  259  LEU LEU GLU GLU TYR GLY CYS CYS LYS GLU LEU ALA SER          
SEQRES  19 B  259  ARG LEU ARG TYR ALA ARG THR MET VAL ASP LYS LEU LEU          
SEQRES  20 B  259  SER SER ARG SER ALA SER ASN ARG LEU LYS ALA SER              
SEQRES   1 A  259  LYS GLY LEU GLU ASN PRO LEU PRO GLU ARG PRO ARG GLU          
SEQRES   2 A  259  LYS GLU GLU PRO VAL VAL ARG GLU THR GLY GLU VAL VAL          
SEQRES   3 A  259  ASP CYS HIS LEU SER ASP MET LEU GLN GLN LEU HIS SER          
SEQRES   4 A  259  VAL ASN ALA SER LYS PRO SER GLU ARG GLY LEU VAL ARG          
SEQRES   5 A  259  GLN GLU GLU ALA GLU ASP PRO ALA CYS ILE PRO ILE PHE          
SEQRES   6 A  259  TRP VAL SER LYS TRP VAL ASP TYR SER ASP LYS TYR GLY          
SEQRES   7 A  259  LEU GLY TYR GLN LEU CYS ASP ASN SER VAL GLY VAL LEU          
SEQRES   8 A  259  PHE ASN ASP SER THR ARG LEU ILE LEU TYR ASN ASP GLY          
SEQRES   9 A  259  ASP SER LEU GLN TYR ILE GLU ARG ASP GLY THR GLU SER          
SEQRES  10 A  259  TYR LEU THR VAL SER SER HIS PRO ASN SER LEU MET LYS          
SEQRES  11 A  259  LYS ILE THR LEU LEU LYS TYR PHE ARG ASN TYR MET SER          
SEQRES  12 A  259  GLU HIS LEU LEU LYS ALA GLY ALA ASN ILE THR PRO ARG          
SEQRES  13 A  259  GLU GLY ASP GLU LEU ALA ARG LEU PRO TYR LEU ARG THR          
SEQRES  14 A  259  TRP PHE ARG THR ARG SER ALA ILE ILE LEU HIS LEU SER          
SEQRES  15 A  259  ASN GLY SER VAL GLN ILE ASN PHE PHE GLN ASP HIS THR          
SEQRES  16 A  259  LYS LEU ILE LEU CYS PRO LEU MET ALA ALA VAL THR TYR          
SEQRES  17 A  259  ILE ASP GLU LYS ARG ASP PHE ARG THR TYR ARG LEU SER          
SEQRES  18 A  259  LEU LEU GLU GLU TYR GLY CYS CYS LYS GLU LEU ALA SER          
SEQRES  19 A  259  ARG LEU ARG TYR ALA ARG THR MET VAL ASP LYS LEU LEU          
SEQRES  20 A  259  SER SER ARG SER ALA SER ASN ARG LEU LYS ALA SER              
SEQRES   1 C  259  LYS GLY LEU GLU ASN PRO LEU PRO GLU ARG PRO ARG GLU          
SEQRES   2 C  259  LYS GLU GLU PRO VAL VAL ARG GLU THR GLY GLU VAL VAL          
SEQRES   3 C  259  ASP CYS HIS LEU SER ASP MET LEU GLN GLN LEU HIS SER          
SEQRES   4 C  259  VAL ASN ALA SER LYS PRO SER GLU ARG GLY LEU VAL ARG          
SEQRES   5 C  259  GLN GLU GLU ALA GLU ASP PRO ALA CYS ILE PRO ILE PHE          
SEQRES   6 C  259  TRP VAL SER LYS TRP VAL ASP TYR SER ASP LYS TYR GLY          
SEQRES   7 C  259  LEU GLY TYR GLN LEU CYS ASP ASN SER VAL GLY VAL LEU          
SEQRES   8 C  259  PHE ASN ASP SER THR ARG LEU ILE LEU TYR ASN ASP GLY          
SEQRES   9 C  259  ASP SER LEU GLN TYR ILE GLU ARG ASP GLY THR GLU SER          
SEQRES  10 C  259  TYR LEU THR VAL SER SER HIS PRO ASN SER LEU MET LYS          
SEQRES  11 C  259  LYS ILE THR LEU LEU LYS TYR PHE ARG ASN TYR MET SER          
SEQRES  12 C  259  GLU HIS LEU LEU LYS ALA GLY ALA ASN ILE THR PRO ARG          
SEQRES  13 C  259  GLU GLY ASP GLU LEU ALA ARG LEU PRO TYR LEU ARG THR          
SEQRES  14 C  259  TRP PHE ARG THR ARG SER ALA ILE ILE LEU HIS LEU SER          
SEQRES  15 C  259  ASN GLY SER VAL GLN ILE ASN PHE PHE GLN ASP HIS THR          
SEQRES  16 C  259  LYS LEU ILE LEU CYS PRO LEU MET ALA ALA VAL THR TYR          
SEQRES  17 C  259  ILE ASP GLU LYS ARG ASP PHE ARG THR TYR ARG LEU SER          
SEQRES  18 C  259  LEU LEU GLU GLU TYR GLY CYS CYS LYS GLU LEU ALA SER          
SEQRES  19 C  259  ARG LEU ARG TYR ALA ARG THR MET VAL ASP LYS LEU LEU          
SEQRES  20 C  259  SER SER ARG SER ALA SER ASN ARG LEU LYS ALA SER              
SEQRES   1 D    6  MET GLN SER TPO PRO LEU                                      
SEQRES   1 E    6  MET GLN SER TPO PRO LEU                                      
SEQRES   1 F    6  MET GLN SER TPO PRO LEU                                      
MODRES 1Q4K TPO D    4  THR  PHOSPHOTHREONINE                                   
MODRES 1Q4K TPO E    4  THR  PHOSPHOTHREONINE                                   
MODRES 1Q4K TPO F    4  THR  PHOSPHOTHREONINE                                   
HET    TPO  D   4      11                                                       
HET    TPO  E   4      11                                                       
HET    TPO  F   4      11                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   4  TPO    3(C4 H10 N O6 P)                                             
FORMUL   7  HOH   *191(H2 O)                                                    
HELIX    1   1 CYS B  372  SER B  387  1                                  16    
HELIX    2   2 ARG B  396  GLU B  401  5                                   6    
HELIX    3   3 ASP B  402  ILE B  406  5                                   5    
HELIX    4   4 PRO B  469  SER B  471  5                                   3    
HELIX    5   5 LEU B  472  LEU B  490  1                                  19    
HELIX    6   6 LEU B  564  GLY B  571  1                                   8    
HELIX    7   7 CYS B  573  SER B  593  1                                  21    
HELIX    8   8 CYS A  372  SER A  387  1                                  16    
HELIX    9   9 ARG A  396  GLU A  401  5                                   6    
HELIX   10  10 ASP A  402  ILE A  406  5                                   5    
HELIX   11  11 PRO A  469  SER A  471  5                                   3    
HELIX   12  12 LEU A  472  LEU A  490  1                                  19    
HELIX   13  13 LEU A  564  GLY A  571  1                                   8    
HELIX   14  14 CYS A  573  SER A  593  1                                  21    
HELIX   15  15 CYS C  372  SER C  387  1                                  16    
HELIX   16  16 ARG C  396  GLU C  401  5                                   6    
HELIX   17  17 ASP C  402  ILE C  406  5                                   5    
HELIX   18  18 LEU C  472  LEU C  490  1                                  19    
HELIX   19  19 LEU C  564  GLY C  571  1                                   8    
HELIX   20  20 CYS C  573  SER C  593  1                                  21    
SHEET    1   A 6 VAL B 411  TYR B 417  0                                        
SHEET    2   A 6 GLY B 422  LEU B 427 -1  O  GLY B 424   N  VAL B 415           
SHEET    3   A 6 VAL B 432  PHE B 436 -1  O  GLY B 433   N  TYR B 425           
SHEET    4   A 6 ARG B 441  LEU B 444 -1  O  LEU B 444   N  VAL B 432           
SHEET    5   A 6 SER B 450  ILE B 454 -1  O  ILE B 454   N  ARG B 441           
SHEET    6   A 6 GLU B 460  THR B 464 -1  O  LEU B 463   N  LEU B 451           
SHEET    1   B 6 LEU B 511  ARG B 516  0                                        
SHEET    2   B 6 ALA B 520  LEU B 525 -1  O  HIS B 524   N  THR B 513           
SHEET    3   B 6 VAL B 530  PHE B 534 -1  O  GLN B 531   N  LEU B 523           
SHEET    4   B 6 LYS B 540  CYS B 544 -1  O  LEU B 543   N  VAL B 530           
SHEET    5   B 6 ALA B 549  ILE B 553 -1  O  ILE B 553   N  LYS B 540           
SHEET    6   B 6 PHE B 559  ARG B 563 -1  O  TYR B 562   N  VAL B 550           
SHEET    1   C 6 VAL A 411  ASP A 416  0                                        
SHEET    2   C 6 GLY A 422  LEU A 427 -1  O  GLY A 424   N  VAL A 415           
SHEET    3   C 6 VAL A 432  PHE A 436 -1  O  LEU A 435   N  LEU A 423           
SHEET    4   C 6 ARG A 441  LEU A 444 -1  O  LEU A 444   N  VAL A 432           
SHEET    5   C 6 SER A 450  ILE A 454 -1  O  ILE A 454   N  ARG A 441           
SHEET    6   C 6 GLU A 460  THR A 464 -1  O  SER A 461   N  TYR A 453           
SHEET    1   D 6 LEU A 511  ARG A 516  0                                        
SHEET    2   D 6 ALA A 520  LEU A 525 -1  O  ILE A 522   N  PHE A 515           
SHEET    3   D 6 VAL A 530  PHE A 534 -1  O  GLN A 531   N  LEU A 523           
SHEET    4   D 6 LYS A 540  CYS A 544 -1  O  LEU A 543   N  VAL A 530           
SHEET    5   D 6 ALA A 549  ILE A 553 -1  O  ALA A 549   N  CYS A 544           
SHEET    6   D 6 PHE A 559  ARG A 563 -1  O  TYR A 562   N  VAL A 550           
SHEET    1   E 6 VAL C 411  ASP C 416  0                                        
SHEET    2   E 6 GLY C 422  LEU C 427 -1  O  GLY C 424   N  VAL C 415           
SHEET    3   E 6 VAL C 432  PHE C 436 -1  O  GLY C 433   N  TYR C 425           
SHEET    4   E 6 ARG C 441  LEU C 444 -1  O  LEU C 444   N  VAL C 432           
SHEET    5   E 6 SER C 450  ILE C 454 -1  O  GLN C 452   N  ILE C 443           
SHEET    6   E 6 SER C 461  THR C 464 -1  O  LEU C 463   N  LEU C 451           
SHEET    1   F 6 LEU C 511  ARG C 516  0                                        
SHEET    2   F 6 ALA C 520  LEU C 525 -1  O  ILE C 522   N  PHE C 515           
SHEET    3   F 6 VAL C 530  PHE C 534 -1  O  GLN C 531   N  LEU C 523           
SHEET    4   F 6 LYS C 540  CYS C 544 -1  O  LEU C 543   N  VAL C 530           
SHEET    5   F 6 ALA C 549  ILE C 553 -1  O  ILE C 553   N  LYS C 540           
SHEET    6   F 6 PHE C 559  ARG C 563 -1  O  TYR C 562   N  VAL C 550           
LINK         C   SER D   3                 N   TPO D   4     1555   1555  1.33  
LINK         C   TPO D   4                 N   PRO D   5     1555   1555  1.35  
LINK         C   SER E   3                 N   TPO E   4     1555   1555  1.34  
LINK         C   TPO E   4                 N   PRO E   5     1555   1555  1.34  
LINK         C   SER F   3                 N   TPO F   4     1555   1555  1.34  
LINK         C   TPO F   4                 N   PRO F   5     1555   1555  1.33  
CRYST1   57.071   56.888   85.050  91.45 103.21 118.50 P 1           3          
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      0.017522  0.009515  0.005679        0.00000                         
SCALE2      0.000000  0.020003  0.003183        0.00000                         
SCALE3      0.000000  0.000000  0.012229        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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