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Database: PDB
Entry: 4EOK
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Original site: 4EOK 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       14-APR-12   4EOK              
TITLE     THR 160 PHOSPHORYLATED CDK2 H84S, Q85M, K89D - HUMAN CYCLIN A3 COMPLEX
TITLE    2 WITH THE INHIBITOR NU6102                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 2;                                 
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: CELL DIVISION PROTEIN KINASE 2, P33 PROTEIN KINASE;         
COMPND   5 EC: 2.7.11.22;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CYCLIN-A2;                                                 
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 FRAGMENT: C-TERMINAL FRAGMENT;                                       
COMPND  12 SYNONYM: CYCLIN-A;                                                   
COMPND  13 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: CDK2, CDKN2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: CCNA2, CCN1, CCNA;                                             
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROTEIN KINASE, CELL CYCLE, PHOSPHORYLATION, TRANSFERASE-TRANSFERASE  
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.ECHALIER,E.COT,A.CAMASSES,E.HODIMONT,F.HOH,F.SHEINERMAN,            
AUTHOR   2 L.KRASINSKA,D.FISHER                                                 
REVDAT   1   06-FEB-13 4EOK    0                                                
JRNL        AUTH   A.ECHALIER,E.COT,A.CAMASSES,E.HODIMONT,F.HOH,P.JAY,          
JRNL        AUTH 2 F.SHEINERMAN,L.KRASINSKA,D.FISHER                            
JRNL        TITL   AN INTEGRATED CHEMICAL BIOLOGY APPROACH PROVIDES INSIGHT     
JRNL        TITL 2 INTO CDK2 FUNCTIONAL REDUNDANCY AND INHIBITOR SENSITIVITY.   
JRNL        REF    CHEM.BIOL.                    V.  19  1028 2012              
JRNL        REFN                   ISSN 1074-5521                               
JRNL        PMID   22921070                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2012.06.015                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.57 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) : 2.57                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 52814                          
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) : 0.225                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2820                            
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) : 2.57                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.64                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3859                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.88                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3370                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 207                          
REMARK   3   BIN FREE R VALUE                    : 0.3440                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8918                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 68                                      
REMARK   3   SOLVENT ATOMS            : 8                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 64.18                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.52000                                             
REMARK   3    B22 (A**2) : -3.46000                                             
REMARK   3    B33 (A**2) : 5.98000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.429         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.281         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.265         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.692        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.915                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9225 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12525 ; 1.080 ; 1.987       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1105 ; 5.157 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   392 ;39.528 ;23.878       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1612 ;16.502 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    46 ;17.818 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1415 ; 0.072 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6832 ; 0.004 ; 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):  5561 ; 0.320 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9036 ; 0.611 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3664 ; 0.790 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3489 ; 1.347 ; 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  : 4                                          
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     0        A   297                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.2190  28.0656  10.3828              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0406 T22:   0.1203                                     
REMARK   3      T33:   0.0127 T12:  -0.0037                                     
REMARK   3      T13:   0.0222 T23:  -0.0076                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9816 L22:   1.4119                                     
REMARK   3      L33:   1.7317 L12:  -0.3253                                     
REMARK   3      L13:   0.6557 L23:  -0.0637                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0599 S12:  -0.1056 S13:  -0.0443                       
REMARK   3      S21:   0.2104 S22:   0.0171 S23:   0.1210                       
REMARK   3      S31:   0.1040 S32:  -0.1643 S33:   0.0428                       
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   175        B   432                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.8293  -0.2191   1.4767              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1507 T22:   0.1031                                     
REMARK   3      T33:   0.1235 T12:   0.0013                                     
REMARK   3      T13:  -0.0070 T23:  -0.0599                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0310 L22:   2.0113                                     
REMARK   3      L33:   2.2426 L12:   0.3504                                     
REMARK   3      L13:  -0.5732 L23:  -0.2934                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0873 S12:   0.1480 S13:  -0.4046                       
REMARK   3      S21:  -0.0830 S22:   0.0307 S23:   0.0027                       
REMARK   3      S31:   0.4588 S32:  -0.0901 S33:   0.0565                       
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    -2        C   297                          
REMARK   3    ORIGIN FOR THE GROUP (A):  48.5575  -8.9132  42.2368              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4106 T22:   0.2946                                     
REMARK   3      T33:   0.2524 T12:   0.0707                                     
REMARK   3      T13:   0.0554 T23:   0.1377                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1556 L22:   3.8191                                     
REMARK   3      L33:   1.6800 L12:  -0.4362                                     
REMARK   3      L13:   1.0937 L23:  -0.5818                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0916 S12:  -0.2577 S13:  -0.1131                       
REMARK   3      S21:   0.1873 S22:   0.0393 S23:  -0.3664                       
REMARK   3      S31:   0.1398 S32:   0.1297 S33:   0.0523                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   176        D   431                          
REMARK   3    ORIGIN FOR THE GROUP (A):  45.9884  24.2383  40.8107              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3895 T22:   0.2488                                     
REMARK   3      T33:   0.4255 T12:   0.0273                                     
REMARK   3      T13:  -0.0150 T23:   0.0435                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9365 L22:   4.1673                                     
REMARK   3      L33:   1.5908 L12:  -0.4226                                     
REMARK   3      L13:   0.0507 L23:   0.7323                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1007 S12:  -0.2619 S13:   0.5916                       
REMARK   3      S21:   0.0568 S22:   0.0546 S23:  -1.1235                       
REMARK   3      S31:  -0.0386 S32:   0.2904 S33:   0.0461                       
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 4EOK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAY-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB071876.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-MAR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9801                             
REMARK 200  MONOCHROMATOR                  : SI CHANNEL CUT                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55627                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.570                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.57                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, POTASSIUM CHLORIDE,    
REMARK 280  HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       37.11500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       85.77500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       68.00500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       85.77500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.11500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       68.00500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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: 4360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 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     LEU A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     ASP A    38                                                      
REMARK 465     THR A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 465     THR A    41                                                      
REMARK 465     VAL D   175                                                      
REMARK 465     LEU D   432                                                      
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   OE2  GLU C   224     OG1  THR C   231              1.64            
REMARK 500   O    ASP C   223     O    VAL C   225              1.97            
REMARK 500   NZ   LYS A   278     O    ASP B   177              2.13            
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    PRO B 176   C   -  N   -  CD  ANGL. DEV. = -17.3 DEGREES          
REMARK 500    LEU C 296   CB  -  CA  -  C   ANGL. DEV. = -19.0 DEGREES          
REMARK 500    ARG C 297   N   -  CA  -  CB  ANGL. DEV. =  15.6 DEGREES          
REMARK 500    PRO D 373   C   -  N   -  CD  ANGL. DEV. = -17.3 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    THR A  14      -54.39     70.85                                   
REMARK 500    HIS A  71      -86.68   -105.41                                   
REMARK 500    THR A  72      -52.95     71.82                                   
REMARK 500    GLU A  73      138.08     69.77                                   
REMARK 500    ASN A  74       40.42    -94.66                                   
REMARK 500    ASP A 127       35.10   -146.00                                   
REMARK 500    ASP A 145       76.35     46.41                                   
REMARK 500    VAL A 163      159.15    -48.80                                   
REMARK 500    VAL A 164      123.71     69.58                                   
REMARK 500    SER A 181     -155.93   -137.24                                   
REMARK 500    TRP A 227       87.26   -153.06                                   
REMARK 500    ASP A 256      153.43    -48.69                                   
REMARK 500    HIS A 295       71.01     53.08                                   
REMARK 500    PRO B 176     -165.22     22.48                                   
REMARK 500    TRP B 372      126.76    -35.24                                   
REMARK 500    ASN B 431       -9.27     67.72                                   
REMARK 500    VAL C   7      -62.42    -95.80                                   
REMARK 500    THR C  14      -59.34     75.09                                   
REMARK 500    THR C  41      -75.44   -114.94                                   
REMARK 500    HIS C  71       75.05   -118.99                                   
REMARK 500    ASP C 127       30.44   -152.64                                   
REMARK 500    ASP C 145       77.33     49.75                                   
REMARK 500    VAL C 164      135.16     67.77                                   
REMARK 500    SER C 181     -154.25   -141.98                                   
REMARK 500    THR C 182      -27.75    -39.97                                   
REMARK 500    VAL C 225      141.45     65.68                                   
REMARK 500    VAL C 226      -58.36     69.79                                   
REMARK 500    SER C 239        2.78    -68.13                                   
REMARK 500    PRO C 284       -8.30    -58.67                                   
REMARK 500    LEU C 296       18.38     47.40                                   
REMARK 500    ASP D 177      -46.67   -131.59                                   
REMARK 500    ILE D 281       29.02    -76.09                                   
REMARK 500    ASP D 283     -117.84     69.33                                   
REMARK 500    HIS D 321       30.45    -92.31                                   
REMARK 500    PRO D 324     -159.39    -97.85                                   
REMARK 500    GLN D 370     -165.72    -71.77                                   
REMARK 500    TRP D 372      125.18    -32.88                                   
REMARK 500    SER D 416        0.21    -65.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ARG C 297        23.8      L          L   OUTSIDE RANGE           
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 4SP A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGM B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4SP C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGM D 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4EOI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EOJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EOL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EOM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EON   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EOO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EOP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EOQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EOR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EOS   RELATED DB: PDB                                   
DBREF  4EOK A    1   297  UNP    P24941   CDK2_HUMAN       1    297             
DBREF  4EOK B  175   432  UNP    P20248   CCNA2_HUMAN    175    432             
DBREF  4EOK C    1   297  UNP    P24941   CDK2_HUMAN       1    297             
DBREF  4EOK D  175   432  UNP    P20248   CCNA2_HUMAN    175    432             
SEQADV 4EOK LEU A   -2  UNP  P24941              EXPRESSION TAG                 
SEQADV 4EOK GLY A   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 4EOK SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 4EOK SER A   84  UNP  P24941    HIS    84 ENGINEERED MUTATION            
SEQADV 4EOK MET A   85  UNP  P24941    GLN    85 ENGINEERED MUTATION            
SEQADV 4EOK ASP A   89  UNP  P24941    LYS    89 ENGINEERED MUTATION            
SEQADV 4EOK LEU C   -2  UNP  P24941              EXPRESSION TAG                 
SEQADV 4EOK GLY C   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 4EOK SER C    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 4EOK SER C   84  UNP  P24941    HIS    84 ENGINEERED MUTATION            
SEQADV 4EOK MET C   85  UNP  P24941    GLN    85 ENGINEERED MUTATION            
SEQADV 4EOK ASP C   89  UNP  P24941    LYS    89 ENGINEERED MUTATION            
SEQRES   1 A  300  LEU GLY SER MET GLU ASN PHE GLN LYS VAL GLU LYS ILE          
SEQRES   2 A  300  GLY GLU GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN          
SEQRES   3 A  300  LYS LEU THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG          
SEQRES   4 A  300  LEU ASP THR GLU THR GLU GLY VAL PRO SER THR ALA ILE          
SEQRES   5 A  300  ARG GLU ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN          
SEQRES   6 A  300  ILE VAL LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS          
SEQRES   7 A  300  LEU TYR LEU VAL PHE GLU PHE LEU SER MET ASP LEU LYS          
SEQRES   8 A  300  ASP PHE MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU          
SEQRES   9 A  300  PRO LEU ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY          
SEQRES  10 A  300  LEU ALA PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP          
SEQRES  11 A  300  LEU LYS PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA          
SEQRES  12 A  300  ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY          
SEQRES  13 A  300  VAL PRO VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU          
SEQRES  14 A  300  TRP TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR          
SEQRES  15 A  300  TYR SER THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE          
SEQRES  16 A  300  PHE ALA GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY          
SEQRES  17 A  300  ASP SER GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR          
SEQRES  18 A  300  LEU GLY THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR          
SEQRES  19 A  300  SER MET PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA          
SEQRES  20 A  300  ARG GLN ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU          
SEQRES  21 A  300  ASP GLY ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP          
SEQRES  22 A  300  PRO ASN LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS          
SEQRES  23 A  300  PRO PHE PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU          
SEQRES  24 A  300  ARG                                                          
SEQRES   1 B  258  VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU ARG          
SEQRES   2 B  258  GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET          
SEQRES   3 B  258  LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE          
SEQRES   4 B  258  LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS          
SEQRES   5 B  258  LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE          
SEQRES   6 B  258  ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS          
SEQRES   7 B  258  LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER          
SEQRES   8 B  258  LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE          
SEQRES   9 B  258  VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN VAL          
SEQRES  10 B  258  LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR PHE          
SEQRES  11 B  258  ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN          
SEQRES  12 B  258  TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL GLU          
SEQRES  13 B  258  SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP          
SEQRES  14 B  258  ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE ALA          
SEQRES  15 B  258  GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY          
SEQRES  16 B  258  GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY TYR          
SEQRES  17 B  258  THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU HIS          
SEQRES  18 B  258  GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER          
SEQRES  19 B  258  ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY VAL          
SEQRES  20 B  258  SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU                  
SEQRES   1 C  300  LEU GLY SER MET GLU ASN PHE GLN LYS VAL GLU LYS ILE          
SEQRES   2 C  300  GLY GLU GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN          
SEQRES   3 C  300  LYS LEU THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG          
SEQRES   4 C  300  LEU ASP THR GLU THR GLU GLY VAL PRO SER THR ALA ILE          
SEQRES   5 C  300  ARG GLU ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN          
SEQRES   6 C  300  ILE VAL LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS          
SEQRES   7 C  300  LEU TYR LEU VAL PHE GLU PHE LEU SER MET ASP LEU LYS          
SEQRES   8 C  300  ASP PHE MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU          
SEQRES   9 C  300  PRO LEU ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY          
SEQRES  10 C  300  LEU ALA PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP          
SEQRES  11 C  300  LEU LYS PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA          
SEQRES  12 C  300  ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY          
SEQRES  13 C  300  VAL PRO VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU          
SEQRES  14 C  300  TRP TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR          
SEQRES  15 C  300  TYR SER THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE          
SEQRES  16 C  300  PHE ALA GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY          
SEQRES  17 C  300  ASP SER GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR          
SEQRES  18 C  300  LEU GLY THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR          
SEQRES  19 C  300  SER MET PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA          
SEQRES  20 C  300  ARG GLN ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU          
SEQRES  21 C  300  ASP GLY ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP          
SEQRES  22 C  300  PRO ASN LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS          
SEQRES  23 C  300  PRO PHE PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU          
SEQRES  24 C  300  ARG                                                          
SEQRES   1 D  258  VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU ARG          
SEQRES   2 D  258  GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET          
SEQRES   3 D  258  LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE          
SEQRES   4 D  258  LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS          
SEQRES   5 D  258  LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE          
SEQRES   6 D  258  ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS          
SEQRES   7 D  258  LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER          
SEQRES   8 D  258  LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE          
SEQRES   9 D  258  VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN VAL          
SEQRES  10 D  258  LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR PHE          
SEQRES  11 D  258  ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN          
SEQRES  12 D  258  TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL GLU          
SEQRES  13 D  258  SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP          
SEQRES  14 D  258  ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE ALA          
SEQRES  15 D  258  GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY          
SEQRES  16 D  258  GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY TYR          
SEQRES  17 D  258  THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU HIS          
SEQRES  18 D  258  GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER          
SEQRES  19 D  258  ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY VAL          
SEQRES  20 D  258  SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU                  
MODRES 4EOK TPO A  160  THR  PHOSPHOTHREONINE                                   
MODRES 4EOK TPO C  160  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET    4SP  A 301      28                                                       
HET    SGM  B 501       6                                                       
HET    4SP  C 301      28                                                       
HET    SGM  D 501       6                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     4SP O6-CYCLOHEXYLMETHOXY-2-(4'-SULPHAMOYLANILINO) PURINE             
HETNAM     SGM MONOTHIOGLYCEROL                                                 
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   5  4SP    2(C18 H22 N6 O3 S)                                           
FORMUL   6  SGM    2(C3 H8 O2 S)                                                
FORMUL   9  HOH   *8(H2 O)                                                      
HELIX    1   1 PRO A   45  LEU A   58  1                                  14    
HELIX    2   2 LEU A   87  SER A   94  1                                   8    
HELIX    3   3 PRO A  100  HIS A  121  1                                  22    
HELIX    4   4 LYS A  129  GLN A  131  5                                   3    
HELIX    5   5 ASP A  145  ALA A  149  5                                   5    
HELIX    6   6 THR A  165  ARG A  169  5                                   5    
HELIX    7   7 ALA A  170  LEU A  175  1                                   6    
HELIX    8   8 THR A  182  ARG A  199  1                                  18    
HELIX    9   9 SER A  207  GLY A  220  1                                  14    
HELIX   10  10 GLY A  229  MET A  233  5                                   5    
HELIX   11  11 ASP A  247  VAL A  252  1                                   6    
HELIX   12  12 ASP A  256  LEU A  267  1                                  12    
HELIX   13  13 SER A  276  LEU A  281  1                                   6    
HELIX   14  14 ALA A  282  GLN A  287  5                                   6    
HELIX   15  15 TYR B  178  CYS B  193  1                                  16    
HELIX   16  16 TYR B  199  GLN B  203  5                                   5    
HELIX   17  17 THR B  207  TYR B  225  1                                  19    
HELIX   18  18 GLN B  228  SER B  244  1                                  17    
HELIX   19  19 LEU B  249  GLY B  251  5                                   3    
HELIX   20  20 LYS B  252  GLU B  269  1                                  18    
HELIX   21  21 GLU B  274  THR B  282  1                                   9    
HELIX   22  22 THR B  287  LEU B  302  1                                  16    
HELIX   23  23 THR B  310  LEU B  320  1                                  11    
HELIX   24  24 ASN B  326  SER B  340  1                                  15    
HELIX   25  25 ASP B  343  LEU B  348  1                                   6    
HELIX   26  26 LEU B  351  THR B  368  1                                  18    
HELIX   27  27 PRO B  373  GLY B  381  1                                   9    
HELIX   28  28 THR B  383  ALA B  401  1                                  19    
HELIX   29  29 PRO B  402  HIS B  404  5                                   3    
HELIX   30  30 GLN B  407  TYR B  413  1                                   7    
HELIX   31  31 LYS B  414  HIS B  419  5                                   6    
HELIX   32  32 GLY B  420  LEU B  424  5                                   5    
HELIX   33  33 SER C    0  GLU C    2  5                                   3    
HELIX   34  34 PRO C   45  LEU C   58  1                                  14    
HELIX   35  35 LEU C   87  SER C   94  1                                   8    
HELIX   36  36 PRO C  100  HIS C  121  1                                  22    
HELIX   37  37 THR C  165  ARG C  169  5                                   5    
HELIX   38  38 ALA C  170  LEU C  175  1                                   6    
HELIX   39  39 THR C  182  ARG C  199  1                                  18    
HELIX   40  40 SER C  207  LEU C  219  1                                  13    
HELIX   41  41 GLY C  229  MET C  233  5                                   5    
HELIX   42  42 ASP C  247  VAL C  252  1                                   6    
HELIX   43  43 ASP C  256  LEU C  267  1                                  12    
HELIX   44  44 SER C  276  LEU C  281  1                                   6    
HELIX   45  45 ALA C  282  GLN C  287  5                                   6    
HELIX   46  46 TYR D  178  CYS D  193  1                                  16    
HELIX   47  47 GLY D  198  LYS D  202  5                                   5    
HELIX   48  48 THR D  207  TYR D  225  1                                  19    
HELIX   49  49 GLN D  228  SER D  244  1                                  17    
HELIX   50  50 LEU D  249  GLU D  269  1                                  21    
HELIX   51  51 GLU D  274  ILE D  281  1                                   8    
HELIX   52  52 THR D  287  LEU D  302  1                                  16    
HELIX   53  53 THR D  310  PHE D  319  1                                  10    
HELIX   54  54 LEU D  320  GLN D  322  5                                   3    
HELIX   55  55 ASN D  326  SER D  340  1                                  15    
HELIX   56  56 ASP D  343  LEU D  348  1                                   6    
HELIX   57  57 LEU D  351  THR D  368  1                                  18    
HELIX   58  58 PRO D  373  GLY D  381  1                                   9    
HELIX   59  59 THR D  383  LYS D  400  1                                  18    
HELIX   60  60 ALA D  401  HIS D  404  5                                   4    
HELIX   61  61 GLN D  407  TYR D  413  1                                   7    
HELIX   62  62 LYS D  414  HIS D  419  5                                   6    
HELIX   63  63 GLY D  420  LEU D  424  5                                   5    
SHEET    1   A 5 PHE A   4  GLY A  11  0                                        
SHEET    2   A 5 VAL A  17  ASN A  23 -1  O  LYS A  20   N  GLU A   8           
SHEET    3   A 5 VAL A  29  ARG A  36 -1  O  VAL A  30   N  ALA A  21           
SHEET    4   A 5 LYS A  75  GLU A  81 -1  O  LEU A  78   N  LYS A  33           
SHEET    5   A 5 LEU A  66  ILE A  70 -1  N  LEU A  67   O  VAL A  79           
SHEET    1   B 3 MET A  85  ASP A  86  0                                        
SHEET    2   B 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  MET A  85           
SHEET    3   B 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1   C 2 VAL A 123  LEU A 124  0                                        
SHEET    2   C 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SHEET    1   D 5 PHE C   4  GLY C  11  0                                        
SHEET    2   D 5 VAL C  17  ASN C  23 -1  O  LYS C  20   N  VAL C   7           
SHEET    3   D 5 VAL C  29  ARG C  36 -1  O  LYS C  34   N  VAL C  17           
SHEET    4   D 5 LYS C  75  GLU C  81 -1  O  PHE C  80   N  ALA C  31           
SHEET    5   D 5 LEU C  66  HIS C  71 -1  N  LEU C  67   O  VAL C  79           
SHEET    1   E 3 MET C  85  ASP C  86  0                                        
SHEET    2   E 3 LEU C 133  ILE C 135 -1  O  ILE C 135   N  MET C  85           
SHEET    3   E 3 ILE C 141  LEU C 143 -1  O  LYS C 142   N  LEU C 134           
SHEET    1   F 2 VAL C 123  LEU C 124  0                                        
SHEET    2   F 2 ARG C 150  ALA C 151 -1  O  ARG C 150   N  LEU C 124           
LINK         C   TYR A 159                 N   TPO A 160     1555   1555  1.33  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.33  
LINK         C   TYR C 159                 N   TPO C 160     1555   1555  1.33  
LINK         C   TPO C 160                 N   HIS C 161     1555   1555  1.34  
CISPEP   1 GLU A   73    ASN A   74          0         9.49                     
CISPEP   2 VAL A  154    PRO A  155          0        -6.86                     
CISPEP   3 GLN B  323    PRO B  324          0        -3.50                     
CISPEP   4 ASP B  345    PRO B  346          0         7.03                     
CISPEP   5 VAL C  154    PRO C  155          0        -1.84                     
CISPEP   6 GLN D  323    PRO D  324          0        -5.59                     
CISPEP   7 ASP D  345    PRO D  346          0         7.70                     
SITE     1 AC1 13 GLU A  12  ALA A  31  VAL A  64  PHE A  80                    
SITE     2 AC1 13 GLU A  81  LEU A  83  SER A  84  MET A  85                    
SITE     3 AC1 13 ASP A  86  ASP A  89  ASN A 132  LEU A 134                    
SITE     4 AC1 13 ASP A 145                                                     
SITE     1 AC2  2 MET B 189  CYS B 193                                          
SITE     1 AC3 15 ILE C  10  ALA C  31  VAL C  64  PHE C  80                    
SITE     2 AC3 15 GLU C  81  PHE C  82  LEU C  83  SER C  84                    
SITE     3 AC3 15 MET C  85  ASP C  86  ASP C  89  GLN C 131                    
SITE     4 AC3 15 ASN C 132  LEU C 134  ASP C 145                               
SITE     1 AC4  4 LYS D 192  CYS D 193  ARG D 241  ASP D 305                    
CRYST1   74.230  136.010  171.550  90.00  90.00  90.00 P 21 21 21    8          
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      0.013472  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007352  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005829        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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