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Database: PDB
Entry: 3P37
LinkDB: 3P37
Original site: 3P37 
HEADER    TRANSFERASE                             04-OCT-10   3P37              
TITLE     POLO-LIKE KINASE I POLO-BOX DOMAIN IN COMPLEX WITH FDPPLHSPTA         
TITLE    2 PHOSPHOPEPTIDE FROM PBIP1                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK1;                      
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: POLO-BOX DOMAIN;                                           
COMPND   5 SYNONYM: POLO-LIKE KINASE 1, PLK-1, SERINE/THREONINE-PROTEIN KINASE  
COMPND   6 13, STPK13;                                                          
COMPND   7 EC: 2.7.11.21;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: PHOSPHOPEPTIDE;                                            
COMPND  11 CHAIN: E, D, F;                                                      
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PLK1, PLK;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1;                                
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 OTHER_DETAILS: CHEMICALLY SYNTHESIZED                                
KEYWDS    PHOSPHOPROTEIN BINDING DOMAIN, PLK1, TRANSFERASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.SLEDZ,M.HYVONEN,C.ABELL                                             
REVDAT   1   27-APR-11 3P37    0                                                
JRNL        AUTH   P.SLEDZ,C.J.STUBBS,S.LANG,Y.Q.YANG,G.J.MCKENZIE,             
JRNL        AUTH 2 A.R.VENKITARAMAN,M.HYVONEN,C.ABELL                           
JRNL        TITL   FROM CRYSTAL PACKING TO MOLECULAR RECOGNITION: PREDICTION    
JRNL        TITL 2 AND DISCOVERY OF A BINDING SITE ON THE SURFACE OF POLO-LIKE  
JRNL        TITL 3 KINASE 1                                                     
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.       V.  50  4003 2011              
JRNL        REFN                   ISSN 1433-7851                               
JRNL        PMID   21472932                                                     
JRNL        DOI    10.1002/ANIE.201008019                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.38 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) : 2.38                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 62.02                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 24149                          
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) : 0.235                           
REMARK   3   R VALUE            (WORKING SET) : 0.232                           
REMARK   3   FREE R VALUE                     : 0.288                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1296                            
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) : 2.38                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.45                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1718                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.01                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2830                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 97                           
REMARK   3   BIN FREE R VALUE                    : 0.3440                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5435                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 116                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.89                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.83000                                             
REMARK   3    B22 (A**2) : 1.03000                                              
REMARK   3    B33 (A**2) : -0.39000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.49000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 1.004         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.337         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.277         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.427        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.925                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.890                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5596 ; 0.007 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7597 ; 1.061 ; 1.978       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   688 ; 5.232 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   241 ;31.945 ;22.988       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   913 ;17.171 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    40 ;16.495 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   856 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4185 ; 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):  3466 ; 0.551 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5557 ; 1.003 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2130 ; 0.732 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2038 ; 1.201 ; 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  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   372        A   590                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.5370   1.0490  17.1700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0284 T22:   0.1808                                     
REMARK   3      T33:   0.1262 T12:  -0.0139                                     
REMARK   3      T13:   0.0479 T23:  -0.0279                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5760 L22:   2.9242                                     
REMARK   3      L33:   4.0662 L12:  -0.5672                                     
REMARK   3      L13:   0.9485 L23:  -2.0760                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0944 S12:   0.0264 S13:   0.0529                       
REMARK   3      S21:  -0.0307 S22:  -0.0544 S23:  -0.0803                       
REMARK   3      S31:   0.0678 S32:   0.0905 S33:   0.1489                       
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 :   B   373        B   590                          
REMARK   3    ORIGIN FOR THE GROUP (A):  37.5870   1.7590  -2.5590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0625 T22:   0.2569                                     
REMARK   3      T33:   0.1185 T12:   0.0008                                     
REMARK   3      T13:   0.0470 T23:  -0.0327                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3503 L22:   4.4734                                     
REMARK   3      L33:   2.9012 L12:   0.8160                                     
REMARK   3      L13:   0.3306 L23:  -1.3445                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0055 S12:  -0.1249 S13:  -0.1176                       
REMARK   3      S21:  -0.1676 S22:  -0.1342 S23:   0.2831                       
REMARK   3      S31:   0.0534 S32:  -0.0041 S33:   0.1398                       
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 :   C   373        C   590                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.3050   0.0340  37.9270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0608 T22:   0.3038                                     
REMARK   3      T33:   0.1035 T12:   0.0316                                     
REMARK   3      T13:   0.0431 T23:  -0.0184                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8785 L22:   4.0689                                     
REMARK   3      L33:   2.9841 L12:   0.6993                                     
REMARK   3      L13:  -0.2737 L23:  -0.9003                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2038 S12:  -0.1796 S13:   0.1145                       
REMARK   3      S21:  -0.0543 S22:   0.0306 S23:   0.2845                       
REMARK   3      S31:   0.0090 S32:   0.1315 S33:   0.1732                       
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 3P37 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-OCT-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB061898.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
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                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9334                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25445                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.380                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 62.020                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1UMW (CHAIN A)                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES, 30% PEG 400, 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 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       44.32900            
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, 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: 1460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
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                                                                      
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: 1580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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: 1380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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     GLY A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     PHE A     8                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     GLY B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     PRO B     6                                                      
REMARK 465     GLU B     7                                                      
REMARK 465     PHE B     8                                                      
REMARK 465     ASP B   371                                                      
REMARK 465     CYS B   372                                                      
REMARK 465     GLY B   502                                                      
REMARK 465     ASP B   503                                                      
REMARK 465     GLU B   504                                                      
REMARK 465     GLY C     1                                                      
REMARK 465     PRO C     2                                                      
REMARK 465     LEU C     3                                                      
REMARK 465     GLY C     4                                                      
REMARK 465     SER C     5                                                      
REMARK 465     PRO C     6                                                      
REMARK 465     GLU C     7                                                      
REMARK 465     PHE C     8                                                      
REMARK 465     ASP C   371                                                      
REMARK 465     CYS C   372                                                      
REMARK 465     GLY C   502                                                      
REMARK 465     ASP C   503                                                      
REMARK 465     NH2 E    80                                                      
REMARK 465     NH2 F    80                                                      
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     ASP A 371    CG   OD1  OD2                                       
REMARK 470     LYS A 388    CE   NZ                                             
REMARK 470     GLU A 398    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 420    CD   CE   NZ                                        
REMARK 470     ARG A 456    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS A 468    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASN A 470    CG   OD1                                            
REMARK 470     LYS A 474    CD   CE   NZ                                        
REMARK 470     GLU A 501    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 504    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 505    CG   CD1  CD2                                       
REMARK 470     ARG A 512    NE   CZ   NH1  NH2                                  
REMARK 470     ARG A 518    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 556    CG   CD   CE   NZ                                   
REMARK 470     ARG A 557    NE   CZ   NH1  NH2                                  
REMARK 470     ARG A 563    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 574    CG   CD   CE   NZ                                   
REMARK 470     ARG A 594    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS B 373    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN B 379    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 391    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 398    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 455    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 463    CG   CD1  CD2                                       
REMARK 470     HIS B 468    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASN B 470    CG   OD1                                            
REMARK 470     GLU B 501    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 518    NE   CZ   NH1  NH2                                  
REMARK 470     GLU B 555    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 569    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 574    CG   CD   CE   NZ                                   
REMARK 470     HIS C 373    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN C 379    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 388    CG   CD   CE   NZ                                   
REMARK 470     ASP C 449    CG   OD1  OD2                                       
REMARK 470     LEU C 463    CG   CD1  CD2                                       
REMARK 470     HIS C 468    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASN C 470    CG   OD1                                            
REMARK 470     MET C 473    CG   SD   CE                                        
REMARK 470     LYS C 474    CG   CD   CE   NZ                                   
REMARK 470     LYS C 480    CG   CD   CE   NZ                                   
REMARK 470     GLU C 501    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 504    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 505    CG   CD1  CD2                                       
REMARK 470     ARG C 507    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 516    NE   CZ   NH1  NH2                                  
REMARK 470     ARG C 518    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 556    CD   CE   NZ                                        
REMARK 470     LYS C 574    CG   CD   CE   NZ                                   
REMARK 470     LYS C 589    CE   NZ                                             
REMARK 470     ARG C 594    NE   CZ   NH1  NH2                                  
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    GLU A 391       49.94    -88.78                                   
REMARK 500    LYS A 420      -53.49   -123.54                                   
REMARK 500    ASN A 430        5.02     85.30                                   
REMARK 500    ASP A 449      -43.04   -138.43                                   
REMARK 500    LEU A 463     -159.99   -151.61                                   
REMARK 500    LYS B 388       74.35     50.76                                   
REMARK 500    SER B 418       -9.51    -58.43                                   
REMARK 500    LYS B 420      -55.10   -136.88                                   
REMARK 500    ASP B 449      -47.30   -141.07                                   
REMARK 500    HIS B 468       71.62     54.74                                   
REMARK 500    LYS C 388       72.46     49.84                                   
REMARK 500    GLU C 391       48.39    -92.93                                   
REMARK 500    ARG C 396       72.46   -111.61                                   
REMARK 500    TYR C 421      -49.76   -133.37                                   
REMARK 500    SER C 439       18.84     57.99                                   
REMARK 500    ASP C 449      -44.09   -130.11                                   
REMARK 500    SER E  77     -178.13    -66.47                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 2                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3P2W   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P2Z   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P34   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P35   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P36   RELATED DB: PDB                                   
DBREF  3P37 A  371   594  UNP    P53350   PLK1_HUMAN     371    594             
DBREF  3P37 B  371   594  UNP    P53350   PLK1_HUMAN     371    594             
DBREF  3P37 C  371   594  UNP    P53350   PLK1_HUMAN     371    594             
DBREF  3P37 E   70    80  PDB    3P37     3P37            70     80             
DBREF  3P37 D   70    80  PDB    3P37     3P37            70     80             
DBREF  3P37 F   70    80  PDB    3P37     3P37            70     80             
SEQADV 3P37 GLY A    1  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P37 PRO A    2  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P37 LEU A    3  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P37 GLY A    4  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P37 SER A    5  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P37 PRO A    6  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P37 GLU A    7  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P37 PHE A    8  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P37 GLY B    1  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P37 PRO B    2  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P37 LEU B    3  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P37 GLY B    4  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P37 SER B    5  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P37 PRO B    6  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P37 GLU B    7  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P37 PHE B    8  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P37 GLY C    1  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P37 PRO C    2  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P37 LEU C    3  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P37 GLY C    4  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P37 SER C    5  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P37 PRO C    6  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P37 GLU C    7  UNP  P53350              EXPRESSION TAG                 
SEQADV 3P37 PHE C    8  UNP  P53350              EXPRESSION TAG                 
SEQRES   1 A  232  GLY PRO LEU GLY SER PRO GLU PHE ASP CYS HIS LEU SER          
SEQRES   2 A  232  ASP MET LEU GLN GLN LEU HIS SER VAL ASN ALA SER LYS          
SEQRES   3 A  232  PRO SER GLU ARG GLY LEU VAL ARG GLN GLU GLU ALA GLU          
SEQRES   4 A  232  ASP PRO ALA CYS ILE PRO ILE PHE TRP VAL SER LYS TRP          
SEQRES   5 A  232  VAL ASP TYR SER ASP LYS TYR GLY LEU GLY TYR GLN LEU          
SEQRES   6 A  232  CYS ASP ASN SER VAL GLY VAL LEU PHE ASN ASP SER THR          
SEQRES   7 A  232  ARG LEU ILE LEU TYR ASN ASP GLY ASP SER LEU GLN TYR          
SEQRES   8 A  232  ILE GLU ARG ASP GLY THR GLU SER TYR LEU THR VAL SER          
SEQRES   9 A  232  SER HIS PRO ASN SER LEU MET LYS LYS ILE THR LEU LEU          
SEQRES  10 A  232  LYS TYR PHE ARG ASN TYR MET SER GLU HIS LEU LEU LYS          
SEQRES  11 A  232  ALA GLY ALA ASN ILE THR PRO ARG GLU GLY ASP GLU LEU          
SEQRES  12 A  232  ALA ARG LEU PRO TYR LEU ARG THR TRP PHE ARG THR ARG          
SEQRES  13 A  232  SER ALA ILE ILE LEU HIS LEU SER ASN GLY SER VAL GLN          
SEQRES  14 A  232  ILE ASN PHE PHE GLN ASP HIS THR LYS LEU ILE LEU CYS          
SEQRES  15 A  232  PRO LEU MET ALA ALA VAL THR TYR ILE ASP GLU LYS ARG          
SEQRES  16 A  232  ASP PHE ARG THR TYR ARG LEU SER LEU LEU GLU GLU TYR          
SEQRES  17 A  232  GLY CYS CYS LYS GLU LEU ALA SER ARG LEU ARG TYR ALA          
SEQRES  18 A  232  ARG THR MET VAL ASP LYS LEU LEU SER SER ARG                  
SEQRES   1 B  232  GLY PRO LEU GLY SER PRO GLU PHE ASP CYS HIS LEU SER          
SEQRES   2 B  232  ASP MET LEU GLN GLN LEU HIS SER VAL ASN ALA SER LYS          
SEQRES   3 B  232  PRO SER GLU ARG GLY LEU VAL ARG GLN GLU GLU ALA GLU          
SEQRES   4 B  232  ASP PRO ALA CYS ILE PRO ILE PHE TRP VAL SER LYS TRP          
SEQRES   5 B  232  VAL ASP TYR SER ASP LYS TYR GLY LEU GLY TYR GLN LEU          
SEQRES   6 B  232  CYS ASP ASN SER VAL GLY VAL LEU PHE ASN ASP SER THR          
SEQRES   7 B  232  ARG LEU ILE LEU TYR ASN ASP GLY ASP SER LEU GLN TYR          
SEQRES   8 B  232  ILE GLU ARG ASP GLY THR GLU SER TYR LEU THR VAL SER          
SEQRES   9 B  232  SER HIS PRO ASN SER LEU MET LYS LYS ILE THR LEU LEU          
SEQRES  10 B  232  LYS TYR PHE ARG ASN TYR MET SER GLU HIS LEU LEU LYS          
SEQRES  11 B  232  ALA GLY ALA ASN ILE THR PRO ARG GLU GLY ASP GLU LEU          
SEQRES  12 B  232  ALA ARG LEU PRO TYR LEU ARG THR TRP PHE ARG THR ARG          
SEQRES  13 B  232  SER ALA ILE ILE LEU HIS LEU SER ASN GLY SER VAL GLN          
SEQRES  14 B  232  ILE ASN PHE PHE GLN ASP HIS THR LYS LEU ILE LEU CYS          
SEQRES  15 B  232  PRO LEU MET ALA ALA VAL THR TYR ILE ASP GLU LYS ARG          
SEQRES  16 B  232  ASP PHE ARG THR TYR ARG LEU SER LEU LEU GLU GLU TYR          
SEQRES  17 B  232  GLY CYS CYS LYS GLU LEU ALA SER ARG LEU ARG TYR ALA          
SEQRES  18 B  232  ARG THR MET VAL ASP LYS LEU LEU SER SER ARG                  
SEQRES   1 C  232  GLY PRO LEU GLY SER PRO GLU PHE ASP CYS HIS LEU SER          
SEQRES   2 C  232  ASP MET LEU GLN GLN LEU HIS SER VAL ASN ALA SER LYS          
SEQRES   3 C  232  PRO SER GLU ARG GLY LEU VAL ARG GLN GLU GLU ALA GLU          
SEQRES   4 C  232  ASP PRO ALA CYS ILE PRO ILE PHE TRP VAL SER LYS TRP          
SEQRES   5 C  232  VAL ASP TYR SER ASP LYS TYR GLY LEU GLY TYR GLN LEU          
SEQRES   6 C  232  CYS ASP ASN SER VAL GLY VAL LEU PHE ASN ASP SER THR          
SEQRES   7 C  232  ARG LEU ILE LEU TYR ASN ASP GLY ASP SER LEU GLN TYR          
SEQRES   8 C  232  ILE GLU ARG ASP GLY THR GLU SER TYR LEU THR VAL SER          
SEQRES   9 C  232  SER HIS PRO ASN SER LEU MET LYS LYS ILE THR LEU LEU          
SEQRES  10 C  232  LYS TYR PHE ARG ASN TYR MET SER GLU HIS LEU LEU LYS          
SEQRES  11 C  232  ALA GLY ALA ASN ILE THR PRO ARG GLU GLY ASP GLU LEU          
SEQRES  12 C  232  ALA ARG LEU PRO TYR LEU ARG THR TRP PHE ARG THR ARG          
SEQRES  13 C  232  SER ALA ILE ILE LEU HIS LEU SER ASN GLY SER VAL GLN          
SEQRES  14 C  232  ILE ASN PHE PHE GLN ASP HIS THR LYS LEU ILE LEU CYS          
SEQRES  15 C  232  PRO LEU MET ALA ALA VAL THR TYR ILE ASP GLU LYS ARG          
SEQRES  16 C  232  ASP PHE ARG THR TYR ARG LEU SER LEU LEU GLU GLU TYR          
SEQRES  17 C  232  GLY CYS CYS LYS GLU LEU ALA SER ARG LEU ARG TYR ALA          
SEQRES  18 C  232  ARG THR MET VAL ASP LYS LEU LEU SER SER ARG                  
SEQRES   1 E   11  ACE PHE ASP PRO PRO LEU HIS SER TPO ALA NH2                  
SEQRES   1 D   11  ACE PHE ASP PRO PRO LEU HIS SER TPO ALA NH2                  
SEQRES   1 F   11  ACE PHE ASP PRO PRO LEU HIS SER TPO ALA NH2                  
MODRES 3P37 TPO E   78  THR  PHOSPHOTHREONINE                                   
MODRES 3P37 TPO D   78  THR  PHOSPHOTHREONINE                                   
MODRES 3P37 TPO F   78  THR  PHOSPHOTHREONINE                                   
HET    ACE  E  70       3                                                       
HET    TPO  E  78      11                                                       
HET    ACE  D  70       3                                                       
HET    TPO  D  78      11                                                       
HET    NH2  D  80       1                                                       
HET    ACE  F  70       3                                                       
HET    TPO  F  78      11                                                       
HET    GOL  A   3       6                                                       
HET    GOL  A   5       6                                                       
HET    GOL  B   2       6                                                       
HET    GOL  C   1       6                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     NH2 AMINO GROUP                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   4  ACE    3(C2 H4 O)                                                   
FORMUL   4  TPO    3(C4 H10 N O6 P)                                             
FORMUL   5  NH2    H2 N                                                         
FORMUL   7  GOL    4(C3 H8 O3)                                                  
FORMUL  11  HOH   *116(H2 O)                                                    
HELIX    1   1 ASP A  371  SER A  387  1                                  17    
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    
HELIX    9   9 HIS B  373  SER B  387  1                                  15    
HELIX   10  10 ARG B  396  GLU B  401  5                                   6    
HELIX   11  11 ASP B  402  ILE B  406  5                                   5    
HELIX   12  12 LEU B  472  LEU B  490  1                                  19    
HELIX   13  13 LEU B  564  GLY B  571  1                                   8    
HELIX   14  14 CYS B  573  SER B  593  1                                  21    
HELIX   15  15 HIS C  373  SER C  387  1                                  15    
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 PRO C  469  SER C  471  5                                   3    
HELIX   19  19 LEU C  472  LEU C  490  1                                  19    
HELIX   20  20 LEU C  564  GLY C  571  1                                   8    
HELIX   21  21 CYS C  573  SER C  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  LEU A 451   O  LEU A 463           
SHEET    3   A 7 ARG A 441  LEU A 444 -1  N  ARG A 441   O  ILE A 454           
SHEET    4   A 7 VAL A 432  PHE A 436 -1  N  VAL A 432   O  LEU A 444           
SHEET    5   A 7 GLY A 422  LEU A 427 -1  N  LEU A 423   O  LEU A 435           
SHEET    6   A 7 VAL A 411  ASP A 416 -1  N  VAL A 415   O  GLY A 424           
SHEET    7   A 7 LEU E  75  HIS E  76 -1  O  LEU E  75   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  THR A 551   N  ILE A 542           
SHEET    6   B 6 PHE A 559  ARG A 563 -1  O  TYR A 562   N  VAL A 550           
SHEET    1   C 7 GLU B 460  THR B 464  0                                        
SHEET    2   C 7 SER B 450  ILE B 454 -1  N  LEU B 451   O  LEU B 463           
SHEET    3   C 7 ARG B 441  LEU B 444 -1  N  ARG B 441   O  ILE B 454           
SHEET    4   C 7 VAL B 432  PHE B 436 -1  N  VAL B 432   O  LEU B 444           
SHEET    5   C 7 GLY B 422  LEU B 427 -1  N  LEU B 423   O  LEU B 435           
SHEET    6   C 7 VAL B 411  ASP B 416 -1  N  VAL B 415   O  GLY B 424           
SHEET    7   C 7 LEU D  75  HIS D  76 -1  O  LEU D  75   N  ASP B 416           
SHEET    1   D 6 LEU B 511  ARG B 516  0                                        
SHEET    2   D 6 ALA B 520  LEU B 525 -1  O  ILE B 522   N  PHE B 515           
SHEET    3   D 6 VAL B 530  PHE B 534 -1  O  GLN B 531   N  LEU B 523           
SHEET    4   D 6 LYS B 540  CYS B 544 -1  O  LEU B 543   N  VAL B 530           
SHEET    5   D 6 ALA B 549  ILE B 553 -1  O  ALA B 549   N  CYS B 544           
SHEET    6   D 6 PHE B 559  ARG B 563 -1  O  TYR B 562   N  VAL B 550           
SHEET    1   E 7 GLU C 460  SER C 461  0                                        
SHEET    2   E 7 LEU C 451  ILE C 454 -1  N  TYR C 453   O  SER C 461           
SHEET    3   E 7 ARG C 441  LEU C 444 -1  N  ARG C 441   O  ILE C 454           
SHEET    4   E 7 VAL C 432  PHE C 436 -1  N  VAL C 432   O  LEU C 444           
SHEET    5   E 7 GLY C 422  LEU C 427 -1  N  LEU C 423   O  LEU C 435           
SHEET    6   E 7 VAL C 411  TYR C 417 -1  N  VAL C 415   O  GLY C 424           
SHEET    7   E 7 LEU F  75  HIS F  76 -1  O  LEU F  75   N  ASP C 416           
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  ALA C 549   N  CYS C 544           
SHEET    6   F 6 PHE C 559  ARG C 563 -1  O  TYR C 562   N  VAL C 550           
LINK         C   ACE E  70                 N   PHE E  71     1555   1555  1.34  
LINK         C   SER E  77                 N   TPO E  78     1555   1555  1.34  
LINK         C   TPO E  78                 N   ALA E  79     1555   1555  1.33  
LINK         C   ACE D  70                 N   PHE D  71     1555   1555  1.33  
LINK         C   SER D  77                 N   TPO D  78     1555   1555  1.33  
LINK         C   TPO D  78                 N   ALA D  79     1555   1555  1.34  
LINK         C   ALA D  79                 N   NH2 D  80     1555   1555  1.34  
LINK         C   ACE F  70                 N   PHE F  71     1555   1555  1.34  
LINK         C   SER F  77                 N   TPO F  78     1555   1555  1.33  
LINK         C   TPO F  78                 N   ALA F  79     1555   1555  1.34  
SITE     1 AC1  1 GLU A 455                                                     
SITE     1 AC2  2 HOH A 135  TRP A 514                                          
SITE     1 AC3  4 HOH B 131  ASP B 376  GLN B 380  PRO B 545                    
CRYST1   58.969   88.658   67.590  90.00 113.48  90.00 P 1 21 1      6          
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      0.016958  0.000000  0.007367        0.00000                         
SCALE2      0.000000  0.011279  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016131        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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