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Database: PDB
Entry: 4EOJ
LinkDB: 4EOJ
Original site: 4EOJ 
HEADER    TRANSFERASE, CELL CYCLE                 14-APR-12   4EOJ              
TITLE     THR 160 PHOSPHORYLATED CDK2 H84S, Q85M, K89D - HUMAN CYCLIN A3 COMPLEX
TITLE    2 WITH ATP                                                             
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, COMPLEX, PHOSPHORYLATION, TRANSFERASE     
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 4EOJ    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.    1.65 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) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 166429                         
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) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8767                            
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) : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 12168                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.23                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2780                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 649                          
REMARK   3   BIN FREE R VALUE                    : 0.3050                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8781                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 76                                      
REMARK   3   SOLVENT ATOMS            : 670                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.72                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.04000                                              
REMARK   3    B22 (A**2) : -0.23000                                             
REMARK   3    B33 (A**2) : 0.19000                                              
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): 0.091         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.087         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.058         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.707         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.946                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9253 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12600 ; 1.191 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1126 ; 5.497 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   392 ;40.153 ;23.929       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1619 ;14.269 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    45 ;17.191 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1424 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6876 ; 0.006 ; 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):  5593 ; 0.578 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9109 ; 1.132 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3660 ; 1.779 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3491 ; 2.894 ; 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 : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   401        A   629                          
REMARK   3    RESIDUE RANGE :   A    -1        A   298                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.9420 -26.3040  -9.3660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0250 T22:   0.1394                                     
REMARK   3      T33:   0.1189 T12:   0.0098                                     
REMARK   3      T13:  -0.0205 T23:   0.0206                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9942 L22:   0.7589                                     
REMARK   3      L33:   0.9857 L12:   0.2319                                     
REMARK   3      L13:  -0.3297 L23:  -0.0465                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0136 S12:  -0.0189 S13:   0.0011                       
REMARK   3      S21:  -0.0819 S22:   0.0168 S23:   0.0811                       
REMARK   3      S31:  -0.0834 S32:  -0.0828 S33:  -0.0304                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   176        B   432                          
REMARK   3    RESIDUE RANGE :   B   601        B   777                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.0270   0.3490   3.3900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0940 T22:   0.1448                                     
REMARK   3      T33:   0.0991 T12:  -0.0007                                     
REMARK   3      T13:   0.0329 T23:  -0.0332                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8857 L22:   1.2315                                     
REMARK   3      L33:   1.1236 L12:  -0.3210                                     
REMARK   3      L13:   0.2843 L23:  -0.1060                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0431 S12:  -0.1217 S13:   0.0953                       
REMARK   3      S21:   0.0501 S22:   0.0675 S23:  -0.0135                       
REMARK   3      S31:  -0.2198 S32:  -0.0240 S33:  -0.0244                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    -3        C   296                          
REMARK   3    RESIDUE RANGE :   C   401        C   535                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.2550  14.2890 -31.6800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2078 T22:   0.1329                                     
REMARK   3      T33:   0.1343 T12:  -0.0123                                     
REMARK   3      T13:  -0.0309 T23:   0.0352                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1029 L22:   1.1372                                     
REMARK   3      L33:   0.8602 L12:   0.2932                                     
REMARK   3      L13:  -0.2693 L23:  -0.1857                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0515 S12:   0.0221 S13:   0.0805                       
REMARK   3      S21:   0.1327 S22:  -0.0345 S23:  -0.0313                       
REMARK   3      S31:  -0.0871 S32:   0.0579 S33:  -0.0169                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   176        D   431                          
REMARK   3    RESIDUE RANGE :   D   501        D   629                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.7210 -18.6110 -34.9570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1787 T22:   0.1144                                     
REMARK   3      T33:   0.1781 T12:   0.0404                                     
REMARK   3      T13:  -0.0164 T23:   0.0276                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4600 L22:   1.3410                                     
REMARK   3      L33:   0.9107 L12:   0.1515                                     
REMARK   3      L13:   0.0894 L23:  -0.0389                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0307 S12:   0.0530 S13:  -0.2281                       
REMARK   3      S21:   0.0573 S22:  -0.0169 S23:  -0.2470                       
REMARK   3      S31:   0.0963 S32:   0.1482 S33:   0.0476                       
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 4EOJ 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 RCSB071875.                                      
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   : 175189                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.280                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
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) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
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   (%): 57.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87                     
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       36.78000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.51000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       66.92500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       74.51000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.78000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       66.92500            
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: 4590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 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: 3910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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     PRO A    -3                                                      
REMARK 465     LEU A    -2                                                      
REMARK 465     ASP A    38                                                      
REMARK 465     THR A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 465     THR A    41                                                      
REMARK 465     VAL B   175                                                      
REMARK 465     GLY C   229                                                      
REMARK 465     VAL C   230                                                      
REMARK 465     THR C   231                                                      
REMARK 465     SER C   232                                                      
REMARK 465     MET C   233                                                      
REMARK 465     PRO C   234                                                      
REMARK 465     ASP C   235                                                      
REMARK 465     TYR C   236                                                      
REMARK 465     LYS C   237                                                      
REMARK 465     PRO C   238                                                      
REMARK 465     SER C   239                                                      
REMARK 465     PHE C   240                                                      
REMARK 465     PRO C   241                                                      
REMARK 465     LYS C   242                                                      
REMARK 465     TRP C   243                                                      
REMARK 465     ALA C   244                                                      
REMARK 465     ARG C   245                                                      
REMARK 465     ARG C   297                                                      
REMARK 465     LEU C   298                                                      
REMARK 465     VAL D   175                                                      
REMARK 465     LEU D   432                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     HIS B  179   N    CA   C    O    CB   CG   ND1                   
REMARK 480     HIS B  179   CD2  CE1  NE2                                       
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   O1B  ATP A   301    MG     MG A   302              1.57            
REMARK 500   O1A  ATP A   301    MG     MG A   302              1.64            
REMARK 500   O    LEU C   255     NH1  ARG C   260              2.11            
REMARK 500   OD2  ASP A   210     O    HOH A   539              2.12            
REMARK 500   ND1  HIS B   179     O    HOH B   675              2.12            
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    SER C 249   CB  -  CA  -  C   ANGL. DEV. =  13.7 DEGREES          
REMARK 500    SER C 249   N   -  CA  -  C   ANGL. DEV. = -24.5 DEGREES          
REMARK 500    PRO C 253   N   -  CA  -  C   ANGL. DEV. = -17.9 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    TYR A  15      -42.97     78.10                                   
REMARK 500    ASP A 127       46.74   -150.50                                   
REMARK 500    ASP A 145       78.08     53.88                                   
REMARK 500    VAL A 164      131.84     76.84                                   
REMARK 500    SER A 181     -146.50   -148.98                                   
REMARK 500    TRP B 372      117.63    -33.95                                   
REMARK 500    TYR C  15      -37.19     67.20                                   
REMARK 500    THR C  41      -81.68   -132.05                                   
REMARK 500    ASP C 127       45.08   -149.65                                   
REMARK 500    ASP C 145       75.47     51.71                                   
REMARK 500    VAL C 164      126.49     67.15                                   
REMARK 500    SER C 181     -142.42   -151.48                                   
REMARK 500    ASP C 247     -159.78    -86.91                                   
REMARK 500    PRO C 253     -178.58    -52.53                                   
REMARK 500    LEU C 255      112.23    -39.17                                   
REMARK 500    ASP D 283     -122.28     61.20                                   
REMARK 500    TRP D 372      116.27    -33.51                                   
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 A  162     VAL A  163                 -129.49                    
REMARK 500 LYS C  250     VAL C  251                   36.29                    
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    THR C 221        23.2      L          L   OUTSIDE RANGE           
REMARK 500    SER C 249        46.4      L          L   OUTSIDE RANGE           
REMARK 500    PRO C 253        50.0      L          L   OUTSIDE RANGE           
REMARK 500    LEU C 255        24.9      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 A 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 132   OD1                                                    
REMARK 620 2 ATP A 301   O3A 137.1                                              
REMARK 620 3 ASP A 145   OD2  85.0  64.2                                        
REMARK 620 4 ATP A 301   O3B 171.0  51.9 100.5                                  
REMARK 620 N                    1     2     3                                   
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    93.3                                              
REMARK 620 3 MET B 200   O    87.5 105.2                                        
REMARK 620 4 HOH B 722   O   170.9  95.3  87.3                                  
REMARK 620 5 HOH B 775   O    77.4 164.1  87.4  94.9                            
REMARK 620 6 HOH B 718   O    87.6  75.4 175.1  97.6  91.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGM B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGM B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP C 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4EOI   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: 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  4EOJ A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4EOJ B  175   432  UNP    P20248   CCNA2_HUMAN    175    432             
DBREF  4EOJ C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4EOJ D  175   432  UNP    P20248   CCNA2_HUMAN    175    432             
SEQADV 4EOJ PRO A   -3  UNP  P24941              EXPRESSION TAG                 
SEQADV 4EOJ LEU A   -2  UNP  P24941              EXPRESSION TAG                 
SEQADV 4EOJ GLY A   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 4EOJ SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 4EOJ SER A   84  UNP  P24941    HIS    84 ENGINEERED MUTATION            
SEQADV 4EOJ MET A   85  UNP  P24941    GLN    85 ENGINEERED MUTATION            
SEQADV 4EOJ ASP A   89  UNP  P24941    LYS    89 ENGINEERED MUTATION            
SEQADV 4EOJ PRO C   -3  UNP  P24941              EXPRESSION TAG                 
SEQADV 4EOJ LEU C   -2  UNP  P24941              EXPRESSION TAG                 
SEQADV 4EOJ GLY C   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 4EOJ SER C    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 4EOJ SER C   84  UNP  P24941    HIS    84 ENGINEERED MUTATION            
SEQADV 4EOJ MET C   85  UNP  P24941    GLN    85 ENGINEERED MUTATION            
SEQADV 4EOJ ASP C   89  UNP  P24941    LYS    89 ENGINEERED MUTATION            
SEQRES   1 A  302  PRO LEU GLY SER MET GLU ASN PHE GLN LYS VAL GLU LYS          
SEQRES   2 A  302  ILE GLY GLU GLY THR TYR GLY VAL VAL TYR LYS ALA ARG          
SEQRES   3 A  302  ASN LYS LEU THR GLY GLU VAL VAL ALA LEU LYS LYS ILE          
SEQRES   4 A  302  ARG LEU ASP THR GLU THR GLU GLY VAL PRO SER THR ALA          
SEQRES   5 A  302  ILE ARG GLU ILE SER LEU LEU LYS GLU LEU ASN HIS PRO          
SEQRES   6 A  302  ASN ILE VAL LYS LEU LEU ASP VAL ILE HIS THR GLU ASN          
SEQRES   7 A  302  LYS LEU TYR LEU VAL PHE GLU PHE LEU SER MET ASP LEU          
SEQRES   8 A  302  LYS ASP PHE MET ASP ALA SER ALA LEU THR GLY ILE PRO          
SEQRES   9 A  302  LEU PRO LEU ILE LYS SER TYR LEU PHE GLN LEU LEU GLN          
SEQRES  10 A  302  GLY LEU ALA PHE CYS HIS SER HIS ARG VAL LEU HIS ARG          
SEQRES  11 A  302  ASP LEU LYS PRO GLN ASN LEU LEU ILE ASN THR GLU GLY          
SEQRES  12 A  302  ALA ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE          
SEQRES  13 A  302  GLY VAL PRO VAL ARG THR TYR TPO HIS GLU VAL VAL THR          
SEQRES  14 A  302  LEU TRP TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS          
SEQRES  15 A  302  TYR TYR SER THR ALA VAL ASP ILE TRP SER LEU GLY CYS          
SEQRES  16 A  302  ILE PHE ALA GLU MET VAL THR ARG ARG ALA LEU PHE PRO          
SEQRES  17 A  302  GLY ASP SER GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG          
SEQRES  18 A  302  THR LEU GLY THR PRO ASP GLU VAL VAL TRP PRO GLY VAL          
SEQRES  19 A  302  THR SER MET PRO ASP TYR LYS PRO SER PHE PRO LYS TRP          
SEQRES  20 A  302  ALA ARG GLN ASP PHE SER LYS VAL VAL PRO PRO LEU ASP          
SEQRES  21 A  302  GLU ASP GLY ARG SER LEU LEU SER GLN MET LEU HIS TYR          
SEQRES  22 A  302  ASP PRO ASN LYS ARG ILE SER ALA LYS ALA ALA LEU ALA          
SEQRES  23 A  302  HIS PRO PHE PHE GLN ASP VAL THR LYS PRO VAL PRO HIS          
SEQRES  24 A  302  LEU ARG 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  302  PRO LEU GLY SER MET GLU ASN PHE GLN LYS VAL GLU LYS          
SEQRES   2 C  302  ILE GLY GLU GLY THR TYR GLY VAL VAL TYR LYS ALA ARG          
SEQRES   3 C  302  ASN LYS LEU THR GLY GLU VAL VAL ALA LEU LYS LYS ILE          
SEQRES   4 C  302  ARG LEU ASP THR GLU THR GLU GLY VAL PRO SER THR ALA          
SEQRES   5 C  302  ILE ARG GLU ILE SER LEU LEU LYS GLU LEU ASN HIS PRO          
SEQRES   6 C  302  ASN ILE VAL LYS LEU LEU ASP VAL ILE HIS THR GLU ASN          
SEQRES   7 C  302  LYS LEU TYR LEU VAL PHE GLU PHE LEU SER MET ASP LEU          
SEQRES   8 C  302  LYS ASP PHE MET ASP ALA SER ALA LEU THR GLY ILE PRO          
SEQRES   9 C  302  LEU PRO LEU ILE LYS SER TYR LEU PHE GLN LEU LEU GLN          
SEQRES  10 C  302  GLY LEU ALA PHE CYS HIS SER HIS ARG VAL LEU HIS ARG          
SEQRES  11 C  302  ASP LEU LYS PRO GLN ASN LEU LEU ILE ASN THR GLU GLY          
SEQRES  12 C  302  ALA ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE          
SEQRES  13 C  302  GLY VAL PRO VAL ARG THR TYR TPO HIS GLU VAL VAL THR          
SEQRES  14 C  302  LEU TRP TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS          
SEQRES  15 C  302  TYR TYR SER THR ALA VAL ASP ILE TRP SER LEU GLY CYS          
SEQRES  16 C  302  ILE PHE ALA GLU MET VAL THR ARG ARG ALA LEU PHE PRO          
SEQRES  17 C  302  GLY ASP SER GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG          
SEQRES  18 C  302  THR LEU GLY THR PRO ASP GLU VAL VAL TRP PRO GLY VAL          
SEQRES  19 C  302  THR SER MET PRO ASP TYR LYS PRO SER PHE PRO LYS TRP          
SEQRES  20 C  302  ALA ARG GLN ASP PHE SER LYS VAL VAL PRO PRO LEU ASP          
SEQRES  21 C  302  GLU ASP GLY ARG SER LEU LEU SER GLN MET LEU HIS TYR          
SEQRES  22 C  302  ASP PRO ASN LYS ARG ILE SER ALA LYS ALA ALA LEU ALA          
SEQRES  23 C  302  HIS PRO PHE PHE GLN ASP VAL THR LYS PRO VAL PRO HIS          
SEQRES  24 C  302  LEU ARG 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 4EOJ TPO A  160  THR  PHOSPHOTHREONINE                                   
MODRES 4EOJ TPO C  160  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET    ATP  A 301      31                                                       
HET     MG  A 302       1                                                       
HET     MG  B 501       1                                                       
HET    SGM  B 502       6                                                       
HET    SGM  B 503       6                                                       
HET    ATP  C 301      31                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     SGM MONOTHIOGLYCEROL                                                 
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   5  ATP    2(C10 H16 N5 O13 P3)                                         
FORMUL   6   MG    2(MG 2+)                                                     
FORMUL   8  SGM    2(C3 H8 O2 S)                                                
FORMUL  11  HOH   *670(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  HIS A  121  1                                  22    
HELIX    5   5 LYS A  129  GLN 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  251  5                                   5    
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 GLY B  198  GLN B  203  5                                   6    
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  ASP B  343  1                                  18    
HELIX   25  25 ASP B  343  LEU B  348  1                                   6    
HELIX   26  26 LEU B  351  GLY B  369  1                                  19    
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 LYS C  129  GLN C  131  5                                   3    
HELIX   38  38 ASP C  145  ALA C  149  5                                   5    
HELIX   39  39 THR C  165  ARG C  169  5                                   5    
HELIX   40  40 ALA C  170  LEU C  175  1                                   6    
HELIX   41  41 THR C  182  ARG C  199  1                                  18    
HELIX   42  42 SER C  207  LEU C  219  1                                  13    
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  GLN D  203  5                                   6    
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 LEU D  249  GLY D  251  5                                   3    
HELIX   51  51 LYS D  252  GLU D  269  1                                  18    
HELIX   52  52 GLU D  274  THR D  282  1                                   9    
HELIX   53  53 THR D  287  LEU D  302  1                                  16    
HELIX   54  54 THR D  310  LEU D  320  1                                  11    
HELIX   55  55 ASN D  326  ASP D  343  1                                  18    
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  ALA D  401  1                                  19    
HELIX   60  60 PRO D  402  HIS D  404  5                                   3    
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  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  LEU A  32   N  TYR A  19           
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  HIS A  71 -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  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  LEU C  32   N  TYR C  19           
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  HIS C  71 -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  AHIS A 161     1555   1555  1.34  
LINK         C   TPO A 160                 N  BHIS 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  1.33  
LINK         OD1 ASN A 132                MG    MG A 302     1555   1555  2.18  
LINK         O   GLN B 203                MG    MG B 501     1555   1555  2.40  
LINK         O   ILE B 206                MG    MG B 501     1555   1555  2.53  
LINK         O   MET B 200                MG    MG B 501     1555   1555  2.67  
LINK         O3A ATP A 301                MG    MG A 302     1555   1555  2.87  
LINK         OD2 ASP A 145                MG    MG A 302     1555   1555  2.97  
LINK         O3B ATP A 301                MG    MG A 302     1555   1555  2.97  
LINK        MG    MG B 501                 O   HOH B 722     1555   1555  2.26  
LINK        MG    MG B 501                 O   HOH B 775     1555   1555  2.32  
LINK        MG    MG B 501                 O   HOH B 718     1555   1555  2.71  
CISPEP   1 VAL A  154    PRO A  155          0        -8.71                     
CISPEP   2 GLN B  323    PRO B  324          0        -6.00                     
CISPEP   3 ASP B  345    PRO B  346          0        12.51                     
CISPEP   4 PRO C   -3    LEU C   -2          0         6.46                     
CISPEP   5 VAL C  154    PRO C  155          0        -4.59                     
CISPEP   6 TRP C  227    PRO C  228          0         0.85                     
CISPEP   7 SER C  249    LYS C  250          0        12.66                     
CISPEP   8 GLN D  323    PRO D  324          0        -5.97                     
CISPEP   9 ASP D  345    PRO D  346          0        10.04                     
SITE     1 AC1 19 ILE A  10  GLU A  12  GLY A  13  THR A  14                    
SITE     2 AC1 19 ALA A  31  LYS A  33  PHE A  80  GLU A  81                    
SITE     3 AC1 19 LEU A  83  ASP A  86  GLN A 131  ASN A 132                    
SITE     4 AC1 19 LEU A 134  ASP A 145   MG A 302  HOH A 471                    
SITE     5 AC1 19 HOH A 517  HOH A 579  HOH A 622                               
SITE     1 AC2  3 ASN A 132  ASP A 145  ATP A 301                               
SITE     1 AC3  6 MET B 200  GLN B 203  ILE B 206  HOH B 718                    
SITE     2 AC3  6 HOH B 722  HOH B 775                                          
SITE     1 AC4  5 MET B 189  CYS B 193  ARG B 241  ASP B 305                    
SITE     2 AC4  5 HOH B 749                                                     
SITE     1 AC5  2 CYS B 327  GLU B 330                                          
SITE     1 AC6 14 ILE C  10  GLU C  12  GLY C  13  ALA C  31                    
SITE     2 AC6 14 PHE C  80  GLU C  81  PHE C  82  LEU C  83                    
SITE     3 AC6 14 ASP C  86  GLN C 131  ASN C 132  LEU C 134                    
SITE     4 AC6 14 ASP C 145  HOH C 493                                          
CRYST1   73.560  133.850  149.020  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      0.013594  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007471  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006711        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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