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Database: PDB
Entry: 4EON
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HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       14-APR-12   4EON              
TITLE     THR 160 PHOSPHORYLATED CDK2 H84S, Q85M, Q131E - HUMAN CYCLIN A3       
TITLE    2 COMPLEX WITH THE INHIBITOR RO3306                                    
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 4EON    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.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.86                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 64435                          
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) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.219                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3431                            
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4132                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.60                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3500                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 221                          
REMARK   3   BIN FREE R VALUE                    : 0.4090                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8955                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 50                                      
REMARK   3   SOLVENT ATOMS            : 130                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.08000                                              
REMARK   3    B22 (A**2) : -0.09000                                             
REMARK   3    B33 (A**2) : 0.00000                                              
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): 0.309         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.236         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.205         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.621        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.938                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.914                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9294 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12637 ; 1.215 ; 1.984       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1122 ; 5.012 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   403 ;39.628 ;23.970       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1616 ;15.921 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    47 ;14.764 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1422 ; 0.074 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6957 ; 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):  5616 ; 0.371 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9137 ; 0.714 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3678 ; 0.890 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3500 ; 1.558 ; 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    -1        A   298                          
REMARK   3    ORIGIN FOR THE GROUP (A): -48.6635  10.8071  43.2627              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1747 T22:   0.0622                                     
REMARK   3      T33:   0.0799 T12:   0.0234                                     
REMARK   3      T13:  -0.0199 T23:  -0.0698                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5844 L22:   0.8362                                     
REMARK   3      L33:   0.3885 L12:  -0.0895                                     
REMARK   3      L13:  -0.4536 L23:   0.2358                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0369 S12:  -0.0377 S13:   0.0213                       
REMARK   3      S21:  -0.0106 S22:  -0.0319 S23:   0.0612                       
REMARK   3      S31:  -0.0060 S32:   0.0256 S33:  -0.0050                       
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   176        B   432                          
REMARK   3    ORIGIN FOR THE GROUP (A): -46.3633 -22.5473  42.3480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2038 T22:   0.0206                                     
REMARK   3      T33:   0.1106 T12:  -0.0138                                     
REMARK   3      T13:  -0.0458 T23:  -0.0081                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3508 L22:   0.8631                                     
REMARK   3      L33:   0.4437 L12:  -0.1948                                     
REMARK   3      L13:  -0.2130 L23:  -0.2330                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0419 S12:  -0.1035 S13:  -0.1508                       
REMARK   3      S21:  -0.0599 S22:   0.0259 S23:   0.1726                       
REMARK   3      S31:   0.0572 S32:   0.0084 S33:   0.0160                       
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    -1        C   297                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.7365 -26.7922  10.5268              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0724 T22:   0.1750                                     
REMARK   3      T33:   0.1123 T12:   0.0022                                     
REMARK   3      T13:  -0.0113 T23:  -0.0337                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4097 L22:   0.2905                                     
REMARK   3      L33:   0.4419 L12:  -0.2734                                     
REMARK   3      L13:  -0.3403 L23:   0.1783                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0156 S12:   0.0488 S13:  -0.0126                       
REMARK   3      S21:   0.0780 S22:   0.0357 S23:  -0.0323                       
REMARK   3      S31:  -0.0470 S32:   0.0483 S33:  -0.0201                       
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   175        D   431                          
REMARK   3    ORIGIN FOR THE GROUP (A): -26.3325   1.1550   1.4676              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1294 T22:   0.1303                                     
REMARK   3      T33:   0.0746 T12:   0.0169                                     
REMARK   3      T13:   0.0049 T23:   0.0102                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4320 L22:   0.8331                                     
REMARK   3      L33:   0.8067 L12:   0.1813                                     
REMARK   3      L13:   0.2978 L23:   0.1132                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0050 S12:   0.1231 S13:   0.0306                       
REMARK   3      S21:  -0.0113 S22:   0.0330 S23:  -0.0101                       
REMARK   3      S31:  -0.1493 S32:   0.0008 S33:  -0.0381                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4EON COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB071879.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JUL-10                          
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               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : SI CHANNEL CUT                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 64435                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 132.980                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
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) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
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   (%): 63.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.39                     
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       36.81300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       88.36350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       66.48950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       88.36350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.81300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       66.48950            
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: 3250 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24050 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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: 3250 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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     VAL B   175                                                      
REMARK 465     LEU C   298                                                      
REMARK 465     LEU D   432                                                      
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    VAL C 163   N   -  CA  -  C   ANGL. DEV. =  22.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
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    SER A   0      160.11    -49.87                                   
REMARK 500    THR A  39      -48.24     71.52                                   
REMARK 500    ASN A  74      -61.20    -91.20                                   
REMARK 500    LEU A  83     -159.19    -94.77                                   
REMARK 500    MET A  85      146.66   -170.36                                   
REMARK 500    ASP A 127       46.90   -148.15                                   
REMARK 500    ASP A 145       80.61     48.80                                   
REMARK 500    VAL A 164      130.44     76.94                                   
REMARK 500    SER A 181     -155.86   -150.01                                   
REMARK 500    ASP A 223     -167.38   -128.76                                   
REMARK 500    PRO A 228      108.97    -59.38                                   
REMARK 500    TRP B 372      116.84    -36.83                                   
REMARK 500    HIS B 404      136.38    -39.98                                   
REMARK 500    THR C  41      -74.14   -107.35                                   
REMARK 500    GLU C  73      124.86    -20.16                                   
REMARK 500    ASN C  74       -7.30     79.35                                   
REMARK 500    LEU C  83     -160.95   -108.56                                   
REMARK 500    SER C  94       31.18    -94.34                                   
REMARK 500    ASP C 127       43.53   -147.96                                   
REMARK 500    ASP C 145       76.36     50.46                                   
REMARK 500    GLU C 162      -70.72    -68.09                                   
REMARK 500    VAL C 163       -8.92     64.41                                   
REMARK 500    SER C 181     -155.55   -148.50                                   
REMARK 500    THR C 290     -168.09   -123.18                                   
REMARK 500    HIS C 295       85.80     65.82                                   
REMARK 500    LEU C 296      -80.46   -100.44                                   
REMARK 500    ASP D 284       10.81     55.10                                   
REMARK 500    LEU D 320        0.95    -67.37                                   
REMARK 500    TRP D 372      117.32    -32.51                                   
REMARK 500    LEU D 430      -88.01   -111.76                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU C  162     VAL C  163                  146.13                    
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    VAL C 163        16.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 501  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN B 203   O                                                      
REMARK 620 2 ILE B 206   O    91.3                                              
REMARK 620 3 MET B 200   O    84.1  97.0                                        
REMARK 620 4 HOH B 617   O    84.3  88.8 167.2                                  
REMARK 620 5 HOH B 618   O   157.4 104.3  77.9 111.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 501  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN D 203   O                                                      
REMARK 620 2 MET D 200   O    79.3                                              
REMARK 620 3 ILE D 206   O    94.4 105.8                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1RO A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1RO C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 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: 4EOK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EOL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EOM   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  4EON A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4EON B  175   432  UNP    P20248   CCNA2_HUMAN    175    432             
DBREF  4EON C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4EON D  175   432  UNP    P20248   CCNA2_HUMAN    175    432             
SEQADV 4EON GLY A   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 4EON SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 4EON SER A   84  UNP  P24941    HIS    84 ENGINEERED MUTATION            
SEQADV 4EON MET A   85  UNP  P24941    GLN    85 ENGINEERED MUTATION            
SEQADV 4EON GLU A  131  UNP  P24941    GLN   131 ENGINEERED MUTATION            
SEQADV 4EON GLY C   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 4EON SER C    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 4EON SER C   84  UNP  P24941    HIS    84 ENGINEERED MUTATION            
SEQADV 4EON MET C   85  UNP  P24941    GLN    85 ENGINEERED MUTATION            
SEQADV 4EON GLU C  131  UNP  P24941    GLN   131 ENGINEERED MUTATION            
SEQRES   1 A  300  GLY SER MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY          
SEQRES   2 A  300  GLU GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS          
SEQRES   3 A  300  LEU THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU          
SEQRES   4 A  300  ASP THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG          
SEQRES   5 A  300  GLU ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE          
SEQRES   6 A  300  VAL LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU          
SEQRES   7 A  300  TYR LEU VAL PHE GLU PHE LEU SER MET ASP LEU LYS LYS          
SEQRES   8 A  300  PHE MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO          
SEQRES   9 A  300  LEU ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU          
SEQRES  10 A  300  ALA PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU          
SEQRES  11 A  300  LYS PRO GLU ASN LEU LEU ILE ASN THR GLU GLY ALA ILE          
SEQRES  12 A  300  LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL          
SEQRES  13 A  300  PRO VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP          
SEQRES  14 A  300  TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR          
SEQRES  15 A  300  SER THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE          
SEQRES  16 A  300  ALA GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP          
SEQRES  17 A  300  SER GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU          
SEQRES  18 A  300  GLY THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER          
SEQRES  19 A  300  MET PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG          
SEQRES  20 A  300  GLN ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP          
SEQRES  21 A  300  GLY ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO          
SEQRES  22 A  300  ASN LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO          
SEQRES  23 A  300  PHE PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG          
SEQRES  24 A  300  LEU                                                          
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  GLY SER MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY          
SEQRES   2 C  300  GLU GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS          
SEQRES   3 C  300  LEU THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU          
SEQRES   4 C  300  ASP THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG          
SEQRES   5 C  300  GLU ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE          
SEQRES   6 C  300  VAL LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU          
SEQRES   7 C  300  TYR LEU VAL PHE GLU PHE LEU SER MET ASP LEU LYS LYS          
SEQRES   8 C  300  PHE MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO          
SEQRES   9 C  300  LEU ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU          
SEQRES  10 C  300  ALA PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU          
SEQRES  11 C  300  LYS PRO GLU ASN LEU LEU ILE ASN THR GLU GLY ALA ILE          
SEQRES  12 C  300  LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL          
SEQRES  13 C  300  PRO VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP          
SEQRES  14 C  300  TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR          
SEQRES  15 C  300  SER THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE          
SEQRES  16 C  300  ALA GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP          
SEQRES  17 C  300  SER GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU          
SEQRES  18 C  300  GLY THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER          
SEQRES  19 C  300  MET PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG          
SEQRES  20 C  300  GLN ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP          
SEQRES  21 C  300  GLY ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO          
SEQRES  22 C  300  ASN LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO          
SEQRES  23 C  300  PHE PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG          
SEQRES  24 C  300  LEU                                                          
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 4EON TPO A  160  THR  PHOSPHOTHREONINE                                   
MODRES 4EON TPO C  160  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET    1RO  A 301      24                                                       
HET     MG  B 501       1                                                       
HET    1RO  C 301      24                                                       
HET     MG  D 501       1                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     1RO (5E)-5-(QUINOLIN-6-YLMETHYLIDENE)-2-[(THIOPHEN-2-                
HETNAM   2 1RO  YLMETHYL)AMINO]-1,3-THIAZOL-4(5H)-ONE                           
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   5  1RO    2(C18 H13 N3 O S2)                                           
FORMUL   6   MG    2(MG 2+)                                                     
FORMUL   9  HOH   *130(H2 O)                                                    
HELIX    1   1 SER A    0  GLU A    2  5                                   3    
HELIX    2   2 PRO A   45  LEU A   58  1                                  14    
HELIX    3   3 LEU A   87  SER A   94  1                                   8    
HELIX    4   4 PRO A  100  SER A  120  1                                  21    
HELIX    5   5 LYS A  129  GLU A  131  5                                   3    
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  MET B  246  1                                  19    
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  ILE B  281  1                                   8    
HELIX   22  22 THR B  287  THR B  303  1                                  17    
HELIX   23  23 THR B  310  PHE B  319  1                                  10    
HELIX   24  24 LEU B  320  GLN B  322  5                                   3    
HELIX   25  25 ASN B  326  ASP B  343  1                                  18    
HELIX   26  26 ASP B  343  LEU B  348  1                                   6    
HELIX   27  27 LEU B  351  THR B  368  1                                  18    
HELIX   28  28 PRO B  373  GLY B  381  1                                   9    
HELIX   29  29 THR B  383  LYS B  400  1                                  18    
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 PRO C   45  LEU C   58  1                                  14    
HELIX   34  34 LEU C   87  SER C   94  1                                   8    
HELIX   35  35 PRO C  100  HIS C  121  1                                  22    
HELIX   36  36 LYS C  129  GLU C  131  5                                   3    
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  GLY C  220  1                                  14    
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  VAL C  289  5                                   8    
HELIX   46  46 TYR D  178  CYS D  193  1                                  16    
HELIX   47  47 TYR D  199  GLN D  203  5                                   5    
HELIX   48  48 THR D  207  TYR D  225  1                                  19    
HELIX   49  49 GLN D  228  MET D  246  1                                  19    
HELIX   50  50 LYS D  252  GLU D  269  1                                  18    
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  GLY D  369  1                                  19    
HELIX   58  58 PRO D  373  GLY D  381  1                                   9    
HELIX   59  59 THR D  383  ALA D  401  1                                  19    
HELIX   60  60 GLN D  407  TYR D  413  1                                   7    
HELIX   61  61 LYS D  414  HIS D  419  5                                   6    
HELIX   62  62 GLY D  420  LEU D  424  5                                   5    
SHEET    1   A 5 PHE A   4  GLU A  12  0                                        
SHEET    2   A 5 VAL A  17  ASN A  23 -1  O  LYS A  20   N  VAL A   7           
SHEET    3   A 5 VAL A  29  ARG A  36 -1  O  LYS A  34   N  VAL A  17           
SHEET    4   A 5 LYS A  75  GLU A  81 -1  O  PHE A  80   N  ALA A  31           
SHEET    5   A 5 LEU A  66  HIS A  71 -1  N  ASP A  68   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  GLU C  12  0                                        
SHEET    2   D 5 VAL C  17  ASN C  23 -1  O  LYS C  20   N  GLU C   8           
SHEET    3   D 5 VAL C  29  ARG C  36 -1  O  VAL C  30   N  ALA C  21           
SHEET    4   D 5 LYS C  75  GLU C  81 -1  O  LEU C  76   N  ILE C  35           
SHEET    5   D 5 LEU C  66  THR C  72 -1  N  ILE C  70   O  TYR C  77           
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  
LINK         O   GLN B 203                MG    MG B 501     1555   1555  2.56  
LINK         O   ILE B 206                MG    MG B 501     1555   1555  2.67  
LINK         O   GLN D 203                MG    MG D 501     1555   1555  2.55  
LINK         O   MET D 200                MG    MG D 501     1555   1555  2.71  
LINK         O   ILE D 206                MG    MG D 501     1555   1555  2.67  
LINK         O   MET B 200                MG    MG B 501     1555   1555  2.71  
LINK        MG    MG B 501                 O   HOH B 617     1555   1555  2.46  
LINK        MG    MG B 501                 O   HOH B 618     1555   1555  2.47  
CISPEP   1 VAL A  154    PRO A  155          0        -8.19                     
CISPEP   2 GLN B  323    PRO B  324          0        -5.33                     
CISPEP   3 ASP B  345    PRO B  346          0         6.17                     
CISPEP   4 LEU C   37    ASP C   38          0         7.43                     
CISPEP   5 VAL C  154    PRO C  155          0        -5.33                     
CISPEP   6 GLN D  323    PRO D  324          0        -5.20                     
CISPEP   7 ASP D  345    PRO D  346          0         6.10                     
SITE     1 AC1 11 GLU A  12  ALA A  31  LYS A  33  GLU A  81                    
SITE     2 AC1 11 PHE A  82  LEU A  83  ASP A  86  GLU A 131                    
SITE     3 AC1 11 ASN A 132  LEU A 134  ASP A 145                               
SITE     1 AC2  5 MET B 200  GLN B 203  ILE B 206  HOH B 617                    
SITE     2 AC2  5 HOH B 618                                                     
SITE     1 AC3 11 GLY C  11  GLU C  12  GLY C  13  VAL C  18                    
SITE     2 AC3 11 GLU C  81  PHE C  82  LEU C  83  GLU C 131                    
SITE     3 AC3 11 ASN C 132  LEU C 134  ASP C 145                               
SITE     1 AC4  3 MET D 200  GLN D 203  ILE D 206                               
CRYST1   73.626  132.979  176.727  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      0.013582  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007520  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005658        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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