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Database: PDB
Entry: 2G9X
LinkDB: 2G9X
Original site: 2G9X 
HEADER    TRANSFERASE/CELL CYCLE                  07-MAR-06   2G9X              
TITLE     STRUCTURE OF THR 160 PHOSPHORYLATED CDK2/CYCLIN A IN COMPLEX WITH THE 
TITLE    2 INHIBITOR NU6271                                                     
CAVEAT     2G9X    CHIRALITY ERROR AT CA CENTER OF GLN 378D                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION PROTEIN KINASE 2;                            
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: P33 PROTEIN KINASE;                                         
COMPND   5 EC: 2.7.1.37;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CYCLIN-A2;                                                 
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 SYNONYM: CYCLIN-A;                                                   
COMPND  11 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;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: B834PLYSS;                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX;                                     
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  13 ORGANISM_COMMON: CATTLE;                                             
SOURCE  14 ORGANISM_TAXID: 9913;                                                
SOURCE  15 GENE: CCNA2, CCNA;                                                   
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: B834PLYSS;                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET                                       
KEYWDS    TRANSFERASE, SERINE/THREONINE PROTEIN KINASE, ATP-BINDING, CELL       
KEYWDS   2 CYCLE, PHOSPHORYLATION, TRANSFERASE-CELL CYCLE COMPLEX               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.ECHALIER,J.A.ENDICOTT,M.E.NOBLE                                     
REVDAT   3   13-JUL-11 2G9X    1       VERSN                                    
REVDAT   2   24-FEB-09 2G9X    1       VERSN                                    
REVDAT   1   23-MAY-06 2G9X    0                                                
JRNL        AUTH   R.J.GRIFFIN,A.HENDERSON,N.J.CURTIN,A.ECHALIER,J.A.ENDICOTT,  
JRNL        AUTH 2 I.R.HARDCASTLE,D.R.NEWELL,M.E.NOBLE,L.Z.WANG,B.T.GOLDING     
JRNL        TITL   SEARCHING FOR CYCLIN-DEPENDENT KINASE INHIBITORS USING A NEW 
JRNL        TITL 2 VARIANT OF THE COPE ELIMINATION.                             
JRNL        REF    J.AM.CHEM.SOC.                V. 128  6012 2006              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   16669651                                                     
JRNL        DOI    10.1021/JA060595J                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.20                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 46238                          
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) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.265                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2488                            
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3365                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.84                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3730                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 171                          
REMARK   3   BIN FREE R VALUE                    : 0.4550                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8837                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 68                                      
REMARK   3   SOLVENT ATOMS            : 161                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 7.67                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.40000                                             
REMARK   3    B22 (A**2) : 0.66000                                              
REMARK   3    B33 (A**2) : 0.74000                                              
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): 0.540         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.307         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.231         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.358        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.916                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.870                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9124 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12391 ; 1.190 ; 1.987       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1093 ; 5.389 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   393 ;39.417 ;23.995       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1596 ;16.749 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    45 ;16.161 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1407 ; 0.082 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6754 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4198 ; 0.205 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  6226 ; 0.305 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   319 ; 0.138 ; 0.200       
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):    36 ; 0.179 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.176 ; 0.200       
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):  5648 ; 0.388 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8933 ; 0.687 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4064 ; 0.813 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3458 ; 1.351 ; 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    10        A   298                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.9640 -26.6710   9.0010              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1967 T22:  -0.1397                                     
REMARK   3      T33:  -0.1405 T12:  -0.0218                                     
REMARK   3      T13:  -0.0175 T23:  -0.0091                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7783 L22:   0.6279                                     
REMARK   3      L33:   1.0519 L12:  -0.1846                                     
REMARK   3      L13:  -0.3405 L23:   0.0036                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0157 S12:  -0.0106 S13:  -0.0302                       
REMARK   3      S21:   0.0568 S22:  -0.0038 S23:  -0.0428                       
REMARK   3      S31:  -0.0929 S32:   0.0795 S33:  -0.0119                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   175        B   425                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.4820   0.2890  -2.8480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1610 T22:  -0.1628                                     
REMARK   3      T33:  -0.1847 T12:   0.0174                                     
REMARK   3      T13:   0.0377 T23:   0.0412                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8883 L22:   1.4942                                     
REMARK   3      L33:   1.5574 L12:   0.2884                                     
REMARK   3      L13:   0.3120 L23:   0.1890                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0392 S12:   0.1220 S13:   0.0814                       
REMARK   3      S21:  -0.0212 S22:   0.0549 S23:   0.0375                       
REMARK   3      S31:  -0.1913 S32:  -0.0237 S33:  -0.0941                       
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    10        C   298                          
REMARK   3    ORIGIN FOR THE GROUP (A): -48.1610  14.3900  32.6040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1132 T22:  -0.0891                                     
REMARK   3      T33:  -0.2130 T12:   0.0674                                     
REMARK   3      T13:  -0.0520 T23:  -0.0992                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3694 L22:   1.8008                                     
REMARK   3      L33:   1.2172 L12:  -0.5185                                     
REMARK   3      L13:  -0.3959 L23:   0.2950                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0469 S12:  -0.0795 S13:  -0.0184                       
REMARK   3      S21:  -0.1338 S22:  -0.1409 S23:   0.1959                       
REMARK   3      S31:  -0.1638 S32:  -0.3033 S33:   0.0940                       
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   425                          
REMARK   3    ORIGIN FOR THE GROUP (A): -44.9451 -18.5454  34.7559              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0519 T22:   0.0051                                     
REMARK   3      T33:   0.0661 T12:  -0.1264                                     
REMARK   3      T13:  -0.0132 T23:  -0.0261                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1961 L22:   2.4604                                     
REMARK   3      L33:   1.7315 L12:  -0.8144                                     
REMARK   3      L13:   0.1922 L23:   0.1912                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0642 S12:  -0.0688 S13:  -0.4118                       
REMARK   3      S21:  -0.0708 S22:  -0.0950 S23:   0.6004                       
REMARK   3      S31:   0.3302 S32:  -0.4271 S33:   0.0308                       
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2G9X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAR-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB036872.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-JUL-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.931                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (TRUNCATE)                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46238                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY                : 2.400                              
REMARK 200  R MERGE                    (I) : 0.11300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
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: PDB ENTRY 1H1R                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, POTASSIUM CHLORIDE,   
REMARK 280  HEPES, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K, PH 7.00     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       37.29000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.25650            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       67.49300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       74.25650            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.29000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       67.49300            
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: 4580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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: 4650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22720 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     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     ASP C   247                                                      
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   SG   CYS B   193     O    HOH B   105              2.12            
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    LEU A  37       73.36   -119.76                                   
REMARK 500    ASP A  38       -7.61    -58.72                                   
REMARK 500    THR A  39      -62.15     78.83                                   
REMARK 500    GLU A  40      -12.98    -47.73                                   
REMARK 500    THR A  41     -108.84    -65.83                                   
REMARK 500    GLU A  42       36.33   -144.10                                   
REMARK 500    THR A  72      160.90    -44.87                                   
REMARK 500    SER A  94       30.52    -93.70                                   
REMARK 500    ASP A 127       34.78   -158.09                                   
REMARK 500    LYS A 129      156.23    175.16                                   
REMARK 500    ASP A 145       82.20     48.86                                   
REMARK 500    GLU A 162       79.28    -66.65                                   
REMARK 500    VAL A 164      137.87     70.21                                   
REMARK 500    SER A 181     -157.40   -138.79                                   
REMARK 500    ASP A 247      107.48    -33.99                                   
REMARK 500    TRP B 372      112.70    -34.90                                   
REMARK 500    ASP C  38       11.42     96.67                                   
REMARK 500    GLU C  40      -14.13     65.84                                   
REMARK 500    THR C  41      -95.95   -129.95                                   
REMARK 500    ALA C  95      -37.97    -39.04                                   
REMARK 500    ASP C 127       48.96   -161.39                                   
REMARK 500    ASP C 145       84.31     32.06                                   
REMARK 500    TYR C 159     -169.09   -116.80                                   
REMARK 500    GLU C 162       84.26    -67.90                                   
REMARK 500    VAL C 164      127.50     74.92                                   
REMARK 500    SER C 181     -153.91   -145.41                                   
REMARK 500    VAL D 175       84.99     38.45                                   
REMARK 500    TYR D 271       75.72   -118.33                                   
REMARK 500    ASP D 283       49.73     35.98                                   
REMARK 500    TRP D 372      109.92    -48.01                                   
REMARK 500    HIS D 419       14.38     58.69                                   
REMARK 500    GLU D 428      -66.32     -7.71                                   
REMARK 500    ASN D 431      115.84     62.02                                   
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 NU5 A 299                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NU5 C 299                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999                                                                      
REMARK 999 AUTHOR STATES THAT RESIDUE 432 IS INDEED A LEU.                      
DBREF  2G9X A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  2G9X C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  2G9X B  172   432  UNP    P30274   CCNA2_BOVIN    146    406             
DBREF  2G9X D  172   432  UNP    P30274   CCNA2_BOVIN    146    406             
SEQADV 2G9X SER A    0  UNP  P24941              CLONING ARTIFACT               
SEQADV 2G9X TPO A  160  UNP  P24941    THR   160 MODIFIED RESIDUE               
SEQADV 2G9X SER C    0  UNP  P24941              CLONING ARTIFACT               
SEQADV 2G9X TPO C  160  UNP  P24941    THR   160 MODIFIED RESIDUE               
SEQADV 2G9X GLY B  171  UNP  P30274              CLONING ARTIFACT               
SEQADV 2G9X LEU B  432  UNP  P30274    VAL   406 SEE REMARK 999                 
SEQADV 2G9X GLY D  171  UNP  P30274              CLONING ARTIFACT               
SEQADV 2G9X LEU D  432  UNP  P30274    VAL   406 SEE REMARK 999                 
SEQRES   1 A  299  SER MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU          
SEQRES   2 A  299  GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU          
SEQRES   3 A  299  THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP          
SEQRES   4 A  299  THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU          
SEQRES   5 A  299  ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL          
SEQRES   6 A  299  LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR          
SEQRES   7 A  299  LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE          
SEQRES   8 A  299  MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU          
SEQRES   9 A  299  ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA          
SEQRES  10 A  299  PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS          
SEQRES  11 A  299  PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS          
SEQRES  12 A  299  LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO          
SEQRES  13 A  299  VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP TYR          
SEQRES  14 A  299  ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER          
SEQRES  15 A  299  THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA          
SEQRES  16 A  299  GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER          
SEQRES  17 A  299  GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY          
SEQRES  18 A  299  THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET          
SEQRES  19 A  299  PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN          
SEQRES  20 A  299  ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY          
SEQRES  21 A  299  ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN          
SEQRES  22 A  299  LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE          
SEQRES  23 A  299  PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU          
SEQRES   1 B  262  GLY VAL ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS          
SEQRES   2 B  262  THR TYR LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS          
SEQRES   3 B  262  VAL GLY TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER          
SEQRES   4 B  262  MET ARG ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY          
SEQRES   5 B  262  GLU GLU TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA          
SEQRES   6 B  262  VAL ASN TYR ILE ASP ARG PHE LEU SER SER MET SER VAL          
SEQRES   7 B  262  LEU ARG GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET          
SEQRES   8 B  262  LEU LEU ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU          
SEQRES   9 B  262  VAL ALA GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR          
SEQRES  10 B  262  LYS LYS GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS          
SEQRES  11 B  262  VAL LEU ALA PHE ASP LEU ALA ALA PRO THR ILE ASN GLN          
SEQRES  12 B  262  PHE LEU THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN          
SEQRES  13 B  262  CYS LYS VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU          
SEQRES  14 B  262  SER LEU ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO          
SEQRES  15 B  262  SER VAL ILE ALA ALA ALA ALA PHE HIS LEU ALA LEU TYR          
SEQRES  16 B  262  THR VAL THR GLY GLN SER TRP PRO GLU SER LEU VAL GLN          
SEQRES  17 B  262  LYS THR GLY TYR THR LEU GLU THR LEU LYS PRO CYS LEU          
SEQRES  18 B  262  LEU ASP LEU HIS GLN THR TYR LEU ARG ALA PRO GLN HIS          
SEQRES  19 B  262  ALA GLN GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS          
SEQRES  20 B  262  TYR HIS GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU          
SEQRES  21 B  262  ASN LEU                                                      
SEQRES   1 C  299  SER MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU          
SEQRES   2 C  299  GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU          
SEQRES   3 C  299  THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP          
SEQRES   4 C  299  THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU          
SEQRES   5 C  299  ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL          
SEQRES   6 C  299  LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR          
SEQRES   7 C  299  LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE          
SEQRES   8 C  299  MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU          
SEQRES   9 C  299  ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA          
SEQRES  10 C  299  PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS          
SEQRES  11 C  299  PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS          
SEQRES  12 C  299  LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO          
SEQRES  13 C  299  VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP TYR          
SEQRES  14 C  299  ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER          
SEQRES  15 C  299  THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA          
SEQRES  16 C  299  GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER          
SEQRES  17 C  299  GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY          
SEQRES  18 C  299  THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET          
SEQRES  19 C  299  PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN          
SEQRES  20 C  299  ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY          
SEQRES  21 C  299  ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN          
SEQRES  22 C  299  LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE          
SEQRES  23 C  299  PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU          
SEQRES   1 D  262  GLY VAL ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS          
SEQRES   2 D  262  THR TYR LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS          
SEQRES   3 D  262  VAL GLY TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER          
SEQRES   4 D  262  MET ARG ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY          
SEQRES   5 D  262  GLU GLU TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA          
SEQRES   6 D  262  VAL ASN TYR ILE ASP ARG PHE LEU SER SER MET SER VAL          
SEQRES   7 D  262  LEU ARG GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET          
SEQRES   8 D  262  LEU LEU ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU          
SEQRES   9 D  262  VAL ALA GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR          
SEQRES  10 D  262  LYS LYS GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS          
SEQRES  11 D  262  VAL LEU ALA PHE ASP LEU ALA ALA PRO THR ILE ASN GLN          
SEQRES  12 D  262  PHE LEU THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN          
SEQRES  13 D  262  CYS LYS VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU          
SEQRES  14 D  262  SER LEU ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO          
SEQRES  15 D  262  SER VAL ILE ALA ALA ALA ALA PHE HIS LEU ALA LEU TYR          
SEQRES  16 D  262  THR VAL THR GLY GLN SER TRP PRO GLU SER LEU VAL GLN          
SEQRES  17 D  262  LYS THR GLY TYR THR LEU GLU THR LEU LYS PRO CYS LEU          
SEQRES  18 D  262  LEU ASP LEU HIS GLN THR TYR LEU ARG ALA PRO GLN HIS          
SEQRES  19 D  262  ALA GLN GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS          
SEQRES  20 D  262  TYR HIS GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU          
SEQRES  21 D  262  ASN LEU                                                      
MODRES 2G9X TPO A  160  THR  PHOSPHOTHREONINE                                   
MODRES 2G9X TPO C  160  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET    NU5  A 299      34                                                       
HET    NU5  C 299      34                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     NU5 3-({2-[(4-{[6-(CYCLOHEXYLMETHOXY)-9H-PURIN-2-                    
HETNAM   2 NU5  YL]AMINO}PHENYL)SULFONYL]ETHYL}AMINO)PROPAN-1-OL                
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   5  NU5    2(C23 H32 N6 O4 S)                                           
FORMUL   7  HOH   *161(H2 O)                                                    
HELIX    1   1 SER A    0  GLU A    2  5                                   3    
HELIX    2   2 PRO A   45  LYS A   56  1                                  12    
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 ASP A  256  LEU A  267  1                                  12    
HELIX   11  11 SER A  276  LEU A  281  1                                   6    
HELIX   12  12 ALA A  282  GLN A  287  5                                   6    
HELIX   13  13 GLY B  171  VAL B  175  5                                   5    
HELIX   14  14 TYR B  178  CYS B  193  1                                  16    
HELIX   15  15 THR B  207  TYR B  225  1                                  19    
HELIX   16  16 GLN B  228  MET B  246  1                                  19    
HELIX   17  17 LEU B  249  GLY B  251  5                                   3    
HELIX   18  18 LYS B  252  GLU B  269  1                                  18    
HELIX   19  19 GLU B  274  THR B  282  1                                   9    
HELIX   20  20 THR B  287  LEU B  302  1                                  16    
HELIX   21  21 THR B  310  PHE B  319  1                                  10    
HELIX   22  22 LEU B  320  GLN B  322  5                                   3    
HELIX   23  23 ASN B  326  LEU B  341  1                                  16    
HELIX   24  24 ASP B  343  LEU B  348  1                                   6    
HELIX   25  25 LEU B  351  GLY B  369  1                                  19    
HELIX   26  26 PRO B  373  GLY B  381  1                                   9    
HELIX   27  27 THR B  383  ALA B  401  1                                  19    
HELIX   28  28 PRO B  402  HIS B  404  5                                   3    
HELIX   29  29 GLN B  407  TYR B  413  1                                   7    
HELIX   30  30 LYS B  414  HIS B  419  5                                   6    
HELIX   31  31 GLY B  420  LEU B  424  5                                   5    
HELIX   32  32 PRO C   45  LYS C   56  1                                  12    
HELIX   33  33 LEU C   87  ALA C   95  1                                   9    
HELIX   34  34 PRO C  100  HIS C  121  1                                  22    
HELIX   35  35 LYS C  129  GLN C  131  5                                   3    
HELIX   36  36 THR C  165  ARG C  169  5                                   5    
HELIX   37  37 ALA C  170  LEU C  175  1                                   6    
HELIX   38  38 THR C  182  ARG C  199  1                                  18    
HELIX   39  39 SER C  207  LEU C  219  1                                  13    
HELIX   40  40 ASP C  256  LEU C  267  1                                  12    
HELIX   41  41 SER C  276  LEU C  281  1                                   6    
HELIX   42  42 ALA C  282  GLN C  287  5                                   6    
HELIX   43  43 GLY D  171  VAL D  175  5                                   5    
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  ASP D  343  1                                  18    
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 LEU D  376  GLY D  381  1                                   6    
HELIX   58  58 LEU D  387  ARG D  400  1                                  14    
HELIX   59  59 ALA D  401  HIS D  404  5                                   4    
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  VAL A  30   N  ALA A  21           
SHEET    4   A 5 LYS A  75  GLU A  81 -1  O  LEU A  78   N  LYS A  33           
SHEET    5   A 5 LEU A  66  ILE A  70 -1  N  ILE A  70   O  TYR A  77           
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  LYS C  34   N  VAL C  17           
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 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  1.33  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.34  
LINK         C   TYR C 159                 N   TPO C 160     1555   1555  1.34  
LINK         C   TPO C 160                 N   HIS C 161     1555   1555  1.33  
CISPEP   1 VAL A  154    PRO A  155          0        -2.42                     
CISPEP   2 GLN B  323    PRO B  324          0       -10.47                     
CISPEP   3 ASP B  345    PRO B  346          0         3.69                     
CISPEP   4 LEU C   37    ASP C   38          0        10.11                     
CISPEP   5 VAL C  154    PRO C  155          0         7.90                     
CISPEP   6 GLN D  323    PRO D  324          0        -5.04                     
CISPEP   7 ASP D  345    PRO D  346          0         3.26                     
SITE     1 AC1 13 ILE A  10  GLU A  12  GLY A  13  ALA A  31                    
SITE     2 AC1 13 PHE A  80  GLU A  81  LEU A  83  HIS A  84                    
SITE     3 AC1 13 GLN A  85  ASP A  86  LYS A  89  ASN A 132                    
SITE     4 AC1 13 LEU A 134                                                     
SITE     1 AC2 14 ILE C  10  GLU C  12  GLY C  13  ALA C  31                    
SITE     2 AC2 14 VAL C  64  PHE C  80  GLU C  81  LEU C  83                    
SITE     3 AC2 14 HIS C  84  GLN C  85  ASP C  86  LYS C  89                    
SITE     4 AC2 14 ASN C 132  LEU C 134                                          
CRYST1   74.580  134.986  148.513  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      0.013408  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007408  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006733        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system