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Database: PDB
Entry: 4EOR
LinkDB: 4EOR
Original site: 4EOR 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       14-APR-12   4EOR              
TITLE     THR 160 PHOSPHORYLATED CDK2 WT - HUMAN CYCLIN A3 COMPLEX WITH THE     
TITLE    2 INHIBITOR NU6102                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 2;                                 
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: CELL DIVISION PROTEIN KINASE 2, P33 PROTEIN KINASE;         
COMPND   5 EC: 2.7.11.22;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CYCLIN-A2;                                                 
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: C-TERMINAL FRAGMENT;                                       
COMPND  11 SYNONYM: CYCLIN-A;                                                   
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: 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 4EOR    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.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 64909                          
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) : 0.222                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3443                            
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2784                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 52.93                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2370                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 161                          
REMARK   3   BIN FREE R VALUE                    : 0.2880                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8664                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 129                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.33                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.25000                                             
REMARK   3    B22 (A**2) : -0.79000                                             
REMARK   3    B33 (A**2) : 1.04000                                              
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): 0.282         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.211         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.142         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.088        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.921                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.906                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8995 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12220 ; 1.049 ; 1.985       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1081 ; 4.946 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   385 ;39.544 ;23.818       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1575 ;14.715 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    45 ;16.361 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1379 ; 0.073 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6678 ; 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):  5422 ; 0.350 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8813 ; 0.681 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3573 ; 0.923 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3407 ; 1.563 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     0        A   297                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.1145 -26.6246   9.5952              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0173 T22:   0.0982                                     
REMARK   3      T33:   0.0522 T12:  -0.0090                                     
REMARK   3      T13:  -0.0144 T23:  -0.0098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8499 L22:   0.8606                                     
REMARK   3      L33:   1.1052 L12:  -0.2407                                     
REMARK   3      L13:  -0.3154 L23:   0.0485                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0315 S12:  -0.0135 S13:  -0.0326                       
REMARK   3      S21:   0.0997 S22:  -0.0171 S23:  -0.0878                       
REMARK   3      S31:  -0.0500 S32:   0.0501 S33:  -0.0144                       
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): -22.0634   0.2249  -3.4124              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0435 T22:   0.0895                                     
REMARK   3      T33:   0.0597 T12:   0.0076                                     
REMARK   3      T13:   0.0287 T23:   0.0328                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8689 L22:   1.2332                                     
REMARK   3      L33:   1.1647 L12:   0.0632                                     
REMARK   3      L13:   0.2506 L23:   0.1100                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0272 S12:   0.0601 S13:   0.1209                       
REMARK   3      S21:  -0.0362 S22:   0.0327 S23:   0.0101                       
REMARK   3      S31:  -0.1723 S32:   0.0135 S33:  -0.0055                       
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     0        C   294                          
REMARK   3    ORIGIN FOR THE GROUP (A): -44.8934  14.3451  31.8355              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2045 T22:   0.1957                                     
REMARK   3      T33:   0.1235 T12:   0.0280                                     
REMARK   3      T13:  -0.0205 T23:  -0.0439                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7989 L22:   0.9957                                     
REMARK   3      L33:   0.4557 L12:  -0.1861                                     
REMARK   3      L13:  -0.2561 L23:   0.0445                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0463 S12:  -0.0050 S13:   0.0254                       
REMARK   3      S21:  -0.0590 S22:  -0.0299 S23:   0.0928                       
REMARK   3      S31:  -0.0782 S32:  -0.0801 S33:  -0.0165                       
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   429                          
REMARK   3    ORIGIN FOR THE GROUP (A): -45.0056 -18.4390  35.2157              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1773 T22:   0.1776                                     
REMARK   3      T33:   0.1720 T12:  -0.0620                                     
REMARK   3      T13:   0.0056 T23:  -0.0255                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3076 L22:   1.0148                                     
REMARK   3      L33:   0.6803 L12:  -0.0823                                     
REMARK   3      L13:   0.1234 L23:   0.0775                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0077 S12:  -0.0765 S13:  -0.1602                       
REMARK   3      S21:   0.0059 S22:  -0.0012 S23:   0.2594                       
REMARK   3      S31:   0.0814 S32:  -0.1250 S33:   0.0089                       
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 4EOR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAY-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB071883.                                      
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   : 68352                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.4                               
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   (%): 58.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94                     
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       36.98600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.59500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       67.71750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       74.59500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.98600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       67.71750            
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: 3800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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: 4120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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     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     ASP C   223                                                      
REMARK 465     GLU C   224                                                      
REMARK 465     VAL C   225                                                      
REMARK 465     VAL C   226                                                      
REMARK 465     TRP C   227                                                      
REMARK 465     PRO C   228                                                      
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     GLN C   246                                                      
REMARK 465     HIS C   295                                                      
REMARK 465     LEU C   296                                                      
REMARK 465     ARG C   297                                                      
REMARK 465     LEU D   430                                                      
REMARK 465     ASN D   431                                                      
REMARK 465     LEU D   432                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LEU C 219    CG   CD1  CD2                                       
REMARK 470     ASP C 247    CG   OD1  OD2                                       
REMARK 470     LYS C 250    CG   CD   CE   NZ                                   
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    GLY C 220   N   -  CA  -  C   ANGL. DEV. =  15.4 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    ASN A  74      -14.14     82.22                                   
REMARK 500    ASP A 127       41.73   -154.02                                   
REMARK 500    ASP A 145       78.13     52.60                                   
REMARK 500    VAL A 164      126.45     75.68                                   
REMARK 500    SER A 181     -154.53   -150.39                                   
REMARK 500    ASP A 247      111.86    -38.63                                   
REMARK 500    THR B 303       47.00     38.63                                   
REMARK 500    TRP B 372      115.42    -34.13                                   
REMARK 500    THR C  41      -83.14   -129.94                                   
REMARK 500    ASP C 127       43.98   -153.85                                   
REMARK 500    ASP C 145       76.13     45.83                                   
REMARK 500    VAL C 164      128.22     67.36                                   
REMARK 500    SER C 181     -153.16   -153.52                                   
REMARK 500    THR C 182      -32.53    -38.75                                   
REMARK 500    PHE C 216       -1.54    -55.55                                   
REMARK 500    THR C 221      144.03   -177.15                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4SP A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4SP C 301                 
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: 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: 4EOS   RELATED DB: PDB                                   
DBREF  4EOR A    1   297  UNP    P24941   CDK2_HUMAN       1    297             
DBREF  4EOR B  175   432  UNP    P20248   CCNA2_HUMAN    175    432             
DBREF  4EOR C    1   297  UNP    P24941   CDK2_HUMAN       1    297             
DBREF  4EOR D  175   432  UNP    P20248   CCNA2_HUMAN    175    432             
SEQADV 4EOR SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 4EOR SER C    0  UNP  P24941              EXPRESSION TAG                 
SEQRES   1 A  298  SER MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU          
SEQRES   2 A  298  GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU          
SEQRES   3 A  298  THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP          
SEQRES   4 A  298  THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU          
SEQRES   5 A  298  ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL          
SEQRES   6 A  298  LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR          
SEQRES   7 A  298  LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE          
SEQRES   8 A  298  MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU          
SEQRES   9 A  298  ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA          
SEQRES  10 A  298  PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS          
SEQRES  11 A  298  PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS          
SEQRES  12 A  298  LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO          
SEQRES  13 A  298  VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP TYR          
SEQRES  14 A  298  ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER          
SEQRES  15 A  298  THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA          
SEQRES  16 A  298  GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER          
SEQRES  17 A  298  GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY          
SEQRES  18 A  298  THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET          
SEQRES  19 A  298  PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN          
SEQRES  20 A  298  ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY          
SEQRES  21 A  298  ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN          
SEQRES  22 A  298  LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE          
SEQRES  23 A  298  PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG              
SEQRES   1 B  258  VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU ARG          
SEQRES   2 B  258  GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET          
SEQRES   3 B  258  LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE          
SEQRES   4 B  258  LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS          
SEQRES   5 B  258  LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE          
SEQRES   6 B  258  ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS          
SEQRES   7 B  258  LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER          
SEQRES   8 B  258  LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE          
SEQRES   9 B  258  VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN VAL          
SEQRES  10 B  258  LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR PHE          
SEQRES  11 B  258  ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN          
SEQRES  12 B  258  TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL GLU          
SEQRES  13 B  258  SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP          
SEQRES  14 B  258  ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE ALA          
SEQRES  15 B  258  GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY          
SEQRES  16 B  258  GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY TYR          
SEQRES  17 B  258  THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU HIS          
SEQRES  18 B  258  GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER          
SEQRES  19 B  258  ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY VAL          
SEQRES  20 B  258  SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU                  
SEQRES   1 C  298  SER MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU          
SEQRES   2 C  298  GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU          
SEQRES   3 C  298  THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP          
SEQRES   4 C  298  THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU          
SEQRES   5 C  298  ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL          
SEQRES   6 C  298  LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR          
SEQRES   7 C  298  LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE          
SEQRES   8 C  298  MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU          
SEQRES   9 C  298  ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA          
SEQRES  10 C  298  PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS          
SEQRES  11 C  298  PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS          
SEQRES  12 C  298  LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO          
SEQRES  13 C  298  VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP TYR          
SEQRES  14 C  298  ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER          
SEQRES  15 C  298  THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA          
SEQRES  16 C  298  GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER          
SEQRES  17 C  298  GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY          
SEQRES  18 C  298  THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET          
SEQRES  19 C  298  PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN          
SEQRES  20 C  298  ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY          
SEQRES  21 C  298  ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN          
SEQRES  22 C  298  LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE          
SEQRES  23 C  298  PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG              
SEQRES   1 D  258  VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU ARG          
SEQRES   2 D  258  GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET          
SEQRES   3 D  258  LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE          
SEQRES   4 D  258  LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS          
SEQRES   5 D  258  LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE          
SEQRES   6 D  258  ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS          
SEQRES   7 D  258  LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER          
SEQRES   8 D  258  LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE          
SEQRES   9 D  258  VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN VAL          
SEQRES  10 D  258  LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR PHE          
SEQRES  11 D  258  ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN          
SEQRES  12 D  258  TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL GLU          
SEQRES  13 D  258  SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP          
SEQRES  14 D  258  ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE ALA          
SEQRES  15 D  258  GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY          
SEQRES  16 D  258  GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY TYR          
SEQRES  17 D  258  THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU HIS          
SEQRES  18 D  258  GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER          
SEQRES  19 D  258  ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY VAL          
SEQRES  20 D  258  SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU                  
MODRES 4EOR TPO A  160  THR  PHOSPHOTHREONINE                                   
MODRES 4EOR TPO C  160  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET    4SP  A 301      28                                                       
HET    4SP  C 301      28                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     4SP O6-CYCLOHEXYLMETHOXY-2-(4'-SULPHAMOYLANILINO) PURINE             
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   5  4SP    2(C18 H22 N6 O3 S)                                           
FORMUL   7  HOH   *129(H2 O)                                                    
HELIX    1   1 PRO A   45  LEU A   58  1                                  14    
HELIX    2   2 LEU A   87  SER A   94  1                                   8    
HELIX    3   3 PRO A  100  HIS A  121  1                                  22    
HELIX    4   4 LYS A  129  GLN A  131  5                                   3    
HELIX    5   5 ASP A  145  ALA A  149  5                                   5    
HELIX    6   6 THR A  165  ARG A  169  5                                   5    
HELIX    7   7 ALA A  170  LEU A  175  1                                   6    
HELIX    8   8 THR A  182  ARG A  199  1                                  18    
HELIX    9   9 SER A  207  GLY A  220  1                                  14    
HELIX   10  10 GLY A  229  MET A  233  5                                   5    
HELIX   11  11 ASP A  247  VAL A  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  1                                   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  ILE B  281  1                                   8    
HELIX   22  22 THR B  287  LEU B  302  1                                  16    
HELIX   23  23 THR B  310  LEU B  320  1                                  11    
HELIX   24  24 ASN B  326  SER B  340  1                                  15    
HELIX   25  25 ASP B  343  LEU B  348  1                                   6    
HELIX   26  26 LEU B  351  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 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 ASP C  145  ALA C  149  5                                   5    
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  PHE C  216  1                                  10    
HELIX   41  41 ASP C  256  LEU C  267  1                                  12    
HELIX   42  42 SER C  276  LEU C  281  1                                   6    
HELIX   43  43 ALA C  282  GLN C  287  5                                   6    
HELIX   44  44 TYR D  178  CYS D  193  1                                  16    
HELIX   45  45 GLY D  198  GLN D  203  5                                   6    
HELIX   46  46 THR D  207  TYR D  225  1                                  19    
HELIX   47  47 GLN D  228  SER D  244  1                                  17    
HELIX   48  48 LEU D  249  GLY D  251  5                                   3    
HELIX   49  49 LYS D  252  GLU D  269  1                                  18    
HELIX   50  50 GLU D  274  ILE D  281  1                                   8    
HELIX   51  51 THR D  287  LEU D  302  1                                  16    
HELIX   52  52 THR D  310  PHE D  319  1                                  10    
HELIX   53  53 LEU D  320  GLN D  322  5                                   3    
HELIX   54  54 ASN D  326  SER D  340  1                                  15    
HELIX   55  55 ASP D  343  LEU D  348  1                                   6    
HELIX   56  56 LEU D  351  THR D  368  1                                  18    
HELIX   57  57 PRO D  373  GLY D  381  1                                   9    
HELIX   58  58 LEU D  387  ALA D  401  1                                  15    
HELIX   59  59 PRO D  402  HIS D  404  5                                   3    
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  GLY A  11  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  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 GLN A  85  ASP A  86  0                                        
SHEET    2   B 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3   B 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1   C 2 VAL A 123  LEU A 124  0                                        
SHEET    2   C 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SHEET    1   D 5 PHE C   4  GLY C  11  0                                        
SHEET    2   D 5 VAL C  17  ASN C  23 -1  O  LYS C  20   N  VAL C   7           
SHEET    3   D 5 VAL C  29  ARG C  36 -1  O  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  HIS C  71 -1  N  LEU C  67   O  VAL C  79           
SHEET    1   E 3 GLN C  85  ASP C  86  0                                        
SHEET    2   E 3 LEU C 133  ILE C 135 -1  O  ILE C 135   N  GLN 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  1.34  
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  
CISPEP   1 VAL A  154    PRO A  155          0        -8.47                     
CISPEP   2 GLN B  323    PRO B  324          0        -3.80                     
CISPEP   3 ASP B  345    PRO B  346          0         7.95                     
CISPEP   4 VAL C  154    PRO C  155          0        -4.91                     
CISPEP   5 ARG C  217    THR C  218          0         2.27                     
CISPEP   6 THR C  218    LEU C  219          0       -23.34                     
CISPEP   7 GLN D  323    PRO D  324          0         0.16                     
CISPEP   8 ASP D  345    PRO D  346          0         9.26                     
SITE     1 AC1 13 ILE A  10  ALA A  31  VAL A  64  PHE A  80                    
SITE     2 AC1 13 GLU A  81  LEU A  83  HIS A  84  GLN A  85                    
SITE     3 AC1 13 ASP A  86  LYS A  89  ASN A 132  LEU A 134                    
SITE     4 AC1 13 HOH A 401                                                     
SITE     1 AC2 17 GLU C  12  GLY C  13  VAL C  18  ALA C  31                    
SITE     2 AC2 17 VAL C  64  PHE C  80  GLU C  81  PHE C  82                    
SITE     3 AC2 17 LEU C  83  HIS C  84  GLN C  85  ASP C  86                    
SITE     4 AC2 17 LYS C  89  ASN C 132  LEU C 134  ASP C 145                    
SITE     5 AC2 17 HOH C 412                                                     
CRYST1   73.972  135.435  149.190  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      0.013519  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007384  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006703        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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