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Database: PDB
Entry: 5NEV
LinkDB: 5NEV
Original site: 5NEV 
HEADER    TRANSFERASE                             12-MAR-17   5NEV              
TITLE     CDK2/CYCLIN A IN COMPLEX WITH COMPOUND 73                             
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 SYNONYM: CYCLIN-A,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, CDKN2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: CCNA2, CCN1, CCNA;                                             
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    CDK2 CYCLIN A, CDK2 SELECTIVE TRANSFERASE, TRANSFERASE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.R.COXON,E.ANSCOMBE,S.J.HARNOR,M.P.MARTIN,B.CARBAIN,I.R.HARDCASTLE,  
AUTHOR   2 L.K.HARLOW,S.KOROLCHUK,C.J.MATHESON,M.E.M.NOBLE,D.R.NEWELL,D.TURNER, 
AUTHOR   3 M.SIVAPRAKASAM,L.Z.WANG,C.WONG,B.T.GOLDING,R.J.GRIFFIN,G.CANO        
REVDAT   1   29-MAR-17 5NEV    0                                                
SPRSDE     29-MAR-17 5NEV      5LQE                                             
JRNL        AUTH   C.R.COXON,E.ANSCOMBE,S.J.HARNOR,M.P.MARTIN,B.CARBAIN,        
JRNL        AUTH 2 B.T.GOLDING,I.R.HARDCASTLE,L.K.HARLOW,S.KOROLCHUK,           
JRNL        AUTH 3 C.J.MATHESON,D.R.NEWELL,M.E.NOBLE,M.SIVAPRAKASAM,            
JRNL        AUTH 4 S.J.TUDHOPE,D.M.TURNER,L.Z.WANG,S.R.WEDGE,C.WONG,            
JRNL        AUTH 5 R.J.GRIFFIN,J.A.ENDICOTT,C.CANO                              
JRNL        TITL   CYCLIN-DEPENDENT KINASE (CDK) INHIBITORS: STRUCTURE-ACTIVITY 
JRNL        TITL 2 RELATIONSHIPS AND INSIGHTS INTO THE CDK-2 SELECTIVITY OF     
JRNL        TITL 3 6-SUBSTITUTED 2-ARYLAMINOPURINES.                            
JRNL        REF    J. MED. CHEM.                 V.  60  1746 2017              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   28005359                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.6B01254                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.97 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.97                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 66.03                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 29173                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1544                            
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) : 2.97                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2135                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3370                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 110                          
REMARK   3   BIN FREE R VALUE                    : 0.3670                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8886                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 64                                      
REMARK   3   SOLVENT ATOMS            : 16                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 80.24                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.42000                                             
REMARK   3    B22 (A**2) : -1.63000                                             
REMARK   3    B33 (A**2) : 2.05000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.438         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.423         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 52.790        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.924                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.908                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9182 ; 0.017 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  8677 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12471 ; 1.944 ; 1.982       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 20146 ; 1.341 ; 2.996       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1099 ; 7.086 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   392 ;41.246 ;23.929       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1604 ;18.442 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    44 ;19.116 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1400 ; 0.107 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9915 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1831 ; 0.002 ; 0.020       
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):  4412 ; 0.629 ; 1.295       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4413 ; 0.629 ; 1.295       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5505 ; 1.145 ; 1.942       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  5506 ; 1.145 ; 1.941       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4770 ; 0.540 ; 1.318       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  4771 ; 0.540 ; 1.318       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  6967 ; 0.971 ; 1.960       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 10177 ; 2.612 ;14.732       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 10178 ; 2.612 ;14.731       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 2                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     0    294       C     0    294   18724  0.07  0.05     
REMARK   3    2     B   175    429       D   175    429   17042  0.05  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
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   295                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.7880 -25.7430  10.0310              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0895 T22:   0.6300                                     
REMARK   3      T33:   0.5459 T12:  -0.0216                                     
REMARK   3      T13:  -0.0789 T23:   0.0029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3951 L22:   3.2265                                     
REMARK   3      L33:   3.1330 L12:  -0.9791                                     
REMARK   3      L13:  -1.9045 L23:   0.1569                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0005 S12:  -0.2596 S13:  -0.2162                       
REMARK   3      S21:   0.4453 S22:   0.1164 S23:  -0.2792                       
REMARK   3      S31:  -0.2394 S32:   0.3684 S33:  -0.1169                       
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   429                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.9340   1.0790  -1.6270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2698 T22:   0.5794                                     
REMARK   3      T33:   0.5170 T12:   0.0270                                     
REMARK   3      T13:   0.0526 T23:   0.0843                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0566 L22:   3.4336                                     
REMARK   3      L33:   3.4263 L12:   0.5627                                     
REMARK   3      L13:   0.6793 L23:   0.6967                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0092 S12:   0.3425 S13:   0.3448                       
REMARK   3      S21:  -0.2671 S22:   0.0338 S23:   0.0415                       
REMARK   3      S31:  -0.5478 S32:   0.1251 S33:  -0.0431                       
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   296                          
REMARK   3    ORIGIN FOR THE GROUP (A): -47.2870  11.5220  33.4340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8724 T22:   0.8632                                     
REMARK   3      T33:   0.6329 T12:   0.0418                                     
REMARK   3      T13:   0.0890 T23:  -0.1852                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6817 L22:   3.6902                                     
REMARK   3      L33:   2.0484 L12:  -0.3566                                     
REMARK   3      L13:  -0.9654 L23:  -0.6038                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3045 S12:  -0.2918 S13:   0.0099                       
REMARK   3      S21:   0.3765 S22:   0.3084 S23:   0.3640                       
REMARK   3      S31:  -0.2464 S32:  -0.5584 S33:  -0.0038                       
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): -42.6170 -21.3000  35.0160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0515 T22:   0.7071                                     
REMARK   3      T33:   0.8885 T12:  -0.2259                                     
REMARK   3      T13:   0.3752 T23:  -0.1331                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4271 L22:   4.9015                                     
REMARK   3      L33:   2.8193 L12:   0.0936                                     
REMARK   3      L13:   0.0454 L23:  -1.2030                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3472 S12:   0.0281 S13:  -0.7376                       
REMARK   3      S21:   0.0670 S22:   0.2347 S23:   0.9383                       
REMARK   3      S31:   0.6908 S32:  -0.6088 S33:   0.1125                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     1        E     2                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.8180  -3.7270  28.3240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5701 T22:   1.3049                                     
REMARK   3      T33:   1.0425 T12:   0.1349                                     
REMARK   3      T13:  -0.6622 T23:  -0.7333                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8991 L22:   2.9625                                     
REMARK   3      L33:   3.9754 L12:   1.6242                                     
REMARK   3      L13:  -1.8884 L23:  -3.4266                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1871 S12:  -0.0865 S13:  -0.1610                       
REMARK   3      S21:   0.5235 S22:  -0.4290 S23:  -0.2315                       
REMARK   3      S31:  -0.6189 S32:   0.2657 S33:   0.2419                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5NEV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-MAR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003990.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-OCT-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.969                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30773                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.970                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 66.030                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 704.0                              
REMARK 200  R MERGE                    (I) : 0.08600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.97                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.13                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1H1S                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN AT 5MG PER ML. 0.6 TO 0.8M       
REMARK 280  KCL, 0.9 TO 1.2M (NH402SO4, AND 100MM HEPES (PH 7.0), VAPOR         
REMARK 280  DIFFUSION, SITTING 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       36.76350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.61000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       66.02650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       74.61000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.76350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       66.02650            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3260 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23400 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -4                                                      
REMARK 465     PRO A    -3                                                      
REMARK 465     LEU A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     LEU A   296                                                      
REMARK 465     ARG A   297                                                      
REMARK 465     LEU A   298                                                      
REMARK 465     MET B   173                                                      
REMARK 465     GLU B   174                                                      
REMARK 465     LEU B   430                                                      
REMARK 465     ASN B   431                                                      
REMARK 465     LEU B   432                                                      
REMARK 465     GLY C    -4                                                      
REMARK 465     PRO C    -3                                                      
REMARK 465     LEU C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     ARG C   297                                                      
REMARK 465     LEU C   298                                                      
REMARK 465     MET D   173                                                      
REMARK 465     GLU D   174                                                      
REMARK 465     LEU D   430                                                      
REMARK 465     ASN D   431                                                      
REMARK 465     LEU D   432                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OH   TYR A    15     OE1  GLU A    51              1.83            
REMARK 500   O    GLU C    40     N    GLU C    42              1.99            
REMARK 500   OH   TYR C    15     OE1  GLU C    51              2.05            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TYR A 168   CE1   TYR A 168   CZ     -0.087                       
REMARK 500    GLU A 257   CG    GLU A 257   CD      0.115                       
REMARK 500    GLU B 374   CD    GLU B 374   OE2     0.066                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 217   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    CYS B 327   CA  -  CB  -  SG  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    ARG B 378   CG  -  CD  -  NE  ANGL. DEV. =  15.7 DEGREES          
REMARK 500    ARG C  22   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG D 187   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG D 187   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    LEU D 232   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  15       53.45   -150.36                                   
REMARK 500    THR A  39       52.04    -59.45                                   
REMARK 500    GLU A  40      -46.13   -166.05                                   
REMARK 500    THR A  41       20.60    -55.27                                   
REMARK 500    THR A  72     -158.33   -113.15                                   
REMARK 500    ASP A 127       42.79   -158.09                                   
REMARK 500    HIS A 161      -69.39    -90.88                                   
REMARK 500    VAL A 163      -38.47   -133.01                                   
REMARK 500    CYS A 177      152.19    -38.62                                   
REMARK 500    SER A 181     -149.50   -142.29                                   
REMARK 500    THR A 290     -155.51   -142.15                                   
REMARK 500    PRO B 176      -25.03    -35.56                                   
REMARK 500    LYS B 226       48.92     38.70                                   
REMARK 500    PHE B 304       12.29     52.76                                   
REMARK 500    VAL B 367      -68.39    -97.81                                   
REMARK 500    TRP B 372      115.73    -34.85                                   
REMARK 500    TYR C  15       46.62   -153.33                                   
REMARK 500    THR C  39      -15.17    -30.15                                   
REMARK 500    GLU C  40      -41.13   -141.48                                   
REMARK 500    THR C  41       24.42    -41.87                                   
REMARK 500    THR C  72     -164.77   -107.74                                   
REMARK 500    ARG C 126       48.01    -92.19                                   
REMARK 500    ASP C 127       46.00   -165.63                                   
REMARK 500    ALA C 144      -12.19   -143.97                                   
REMARK 500    HIS C 161      -69.59    -94.61                                   
REMARK 500    VAL C 163      -51.50   -141.27                                   
REMARK 500    CYS C 177      154.15    -43.63                                   
REMARK 500    SER C 181     -151.50   -142.13                                   
REMARK 500    ARG C 199       53.40    -90.83                                   
REMARK 500    THR C 290     -158.06   -138.42                                   
REMARK 500    PRO D 176      -27.96    -28.00                                   
REMARK 500    CYS D 193       30.53    -91.70                                   
REMARK 500    LYS D 226       48.05     38.80                                   
REMARK 500    PHE D 304       11.61     53.70                                   
REMARK 500    ALA D 307       59.47    -90.81                                   
REMARK 500    VAL D 367      -68.99    -98.10                                   
REMARK 500    TRP D 372      116.49    -37.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY C   16     VAL C   17                 -149.29                    
REMARK 500 HIS C   71     THR C   72                  147.48                    
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 72L A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 72L C 301                 
DBREF  5NEV A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  5NEV B  174   432  UNP    P20248   CCNA2_HUMAN    174    432             
DBREF  5NEV C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  5NEV D  174   432  UNP    P20248   CCNA2_HUMAN    174    432             
SEQADV 5NEV GLY A   -4  UNP  P24941              EXPRESSION TAG                 
SEQADV 5NEV PRO A   -3  UNP  P24941              EXPRESSION TAG                 
SEQADV 5NEV LEU A   -2  UNP  P24941              EXPRESSION TAG                 
SEQADV 5NEV GLY A   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 5NEV SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 5NEV MET B  173  UNP  P20248              INITIATING METHIONINE          
SEQADV 5NEV GLY C   -4  UNP  P24941              EXPRESSION TAG                 
SEQADV 5NEV PRO C   -3  UNP  P24941              EXPRESSION TAG                 
SEQADV 5NEV LEU C   -2  UNP  P24941              EXPRESSION TAG                 
SEQADV 5NEV GLY C   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 5NEV SER C    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 5NEV MET D  173  UNP  P20248              INITIATING METHIONINE          
SEQRES   1 A  303  GLY PRO LEU GLY SER MET GLU ASN PHE GLN LYS VAL GLU          
SEQRES   2 A  303  LYS ILE GLY GLU GLY THR TYR GLY VAL VAL TYR LYS ALA          
SEQRES   3 A  303  ARG ASN LYS LEU THR GLY GLU VAL VAL ALA LEU LYS LYS          
SEQRES   4 A  303  ILE ARG LEU ASP THR GLU THR GLU GLY VAL PRO SER THR          
SEQRES   5 A  303  ALA ILE ARG GLU ILE SER LEU LEU LYS GLU LEU ASN HIS          
SEQRES   6 A  303  PRO ASN ILE VAL LYS LEU LEU ASP VAL ILE HIS THR GLU          
SEQRES   7 A  303  ASN LYS LEU TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP          
SEQRES   8 A  303  LEU LYS LYS PHE MET ASP ALA SER ALA LEU THR GLY ILE          
SEQRES   9 A  303  PRO LEU PRO LEU ILE LYS SER TYR LEU PHE GLN LEU LEU          
SEQRES  10 A  303  GLN GLY LEU ALA PHE CYS HIS SER HIS ARG VAL LEU HIS          
SEQRES  11 A  303  ARG ASP LEU LYS PRO GLN ASN LEU LEU ILE ASN THR GLU          
SEQRES  12 A  303  GLY ALA ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA          
SEQRES  13 A  303  PHE GLY VAL PRO VAL ARG THR TYR TPO HIS GLU VAL VAL          
SEQRES  14 A  303  THR LEU TRP TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS          
SEQRES  15 A  303  LYS TYR TYR SER THR ALA VAL ASP ILE TRP SER LEU GLY          
SEQRES  16 A  303  CYS ILE PHE ALA GLU MET VAL THR ARG ARG ALA LEU PHE          
SEQRES  17 A  303  PRO GLY ASP SER GLU ILE ASP GLN LEU PHE ARG ILE PHE          
SEQRES  18 A  303  ARG THR LEU GLY THR PRO ASP GLU VAL VAL TRP PRO GLY          
SEQRES  19 A  303  VAL THR SER MET PRO ASP TYR LYS PRO SER PHE PRO LYS          
SEQRES  20 A  303  TRP ALA ARG GLN ASP PHE SER LYS VAL VAL PRO PRO LEU          
SEQRES  21 A  303  ASP GLU ASP GLY ARG SER LEU LEU SER GLN MET LEU HIS          
SEQRES  22 A  303  TYR ASP PRO ASN LYS ARG ILE SER ALA LYS ALA ALA LEU          
SEQRES  23 A  303  ALA HIS PRO PHE PHE GLN ASP VAL THR LYS PRO VAL PRO          
SEQRES  24 A  303  HIS LEU ARG LEU                                              
SEQRES   1 B  260  MET GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR          
SEQRES   2 B  260  LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY          
SEQRES   3 B  260  TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG          
SEQRES   4 B  260  ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU          
SEQRES   5 B  260  TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN          
SEQRES   6 B  260  TYR ILE ASP ARG PHE LEU SER SER MET SER VAL LEU ARG          
SEQRES   7 B  260  GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU          
SEQRES   8 B  260  ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA          
SEQRES   9 B  260  GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS          
SEQRES  10 B  260  GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU          
SEQRES  11 B  260  THR PHE ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU          
SEQRES  12 B  260  THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS          
SEQRES  13 B  260  VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU          
SEQRES  14 B  260  ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL          
SEQRES  15 B  260  ILE ALA GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL          
SEQRES  16 B  260  THR GLY GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR          
SEQRES  17 B  260  GLY TYR THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP          
SEQRES  18 B  260  LEU HIS GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN          
SEQRES  19 B  260  GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS          
SEQRES  20 B  260  GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU          
SEQRES   1 C  303  GLY PRO LEU GLY SER MET GLU ASN PHE GLN LYS VAL GLU          
SEQRES   2 C  303  LYS ILE GLY GLU GLY THR TYR GLY VAL VAL TYR LYS ALA          
SEQRES   3 C  303  ARG ASN LYS LEU THR GLY GLU VAL VAL ALA LEU LYS LYS          
SEQRES   4 C  303  ILE ARG LEU ASP THR GLU THR GLU GLY VAL PRO SER THR          
SEQRES   5 C  303  ALA ILE ARG GLU ILE SER LEU LEU LYS GLU LEU ASN HIS          
SEQRES   6 C  303  PRO ASN ILE VAL LYS LEU LEU ASP VAL ILE HIS THR GLU          
SEQRES   7 C  303  ASN LYS LEU TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP          
SEQRES   8 C  303  LEU LYS LYS PHE MET ASP ALA SER ALA LEU THR GLY ILE          
SEQRES   9 C  303  PRO LEU PRO LEU ILE LYS SER TYR LEU PHE GLN LEU LEU          
SEQRES  10 C  303  GLN GLY LEU ALA PHE CYS HIS SER HIS ARG VAL LEU HIS          
SEQRES  11 C  303  ARG ASP LEU LYS PRO GLN ASN LEU LEU ILE ASN THR GLU          
SEQRES  12 C  303  GLY ALA ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA          
SEQRES  13 C  303  PHE GLY VAL PRO VAL ARG THR TYR TPO HIS GLU VAL VAL          
SEQRES  14 C  303  THR LEU TRP TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS          
SEQRES  15 C  303  LYS TYR TYR SER THR ALA VAL ASP ILE TRP SER LEU GLY          
SEQRES  16 C  303  CYS ILE PHE ALA GLU MET VAL THR ARG ARG ALA LEU PHE          
SEQRES  17 C  303  PRO GLY ASP SER GLU ILE ASP GLN LEU PHE ARG ILE PHE          
SEQRES  18 C  303  ARG THR LEU GLY THR PRO ASP GLU VAL VAL TRP PRO GLY          
SEQRES  19 C  303  VAL THR SER MET PRO ASP TYR LYS PRO SER PHE PRO LYS          
SEQRES  20 C  303  TRP ALA ARG GLN ASP PHE SER LYS VAL VAL PRO PRO LEU          
SEQRES  21 C  303  ASP GLU ASP GLY ARG SER LEU LEU SER GLN MET LEU HIS          
SEQRES  22 C  303  TYR ASP PRO ASN LYS ARG ILE SER ALA LYS ALA ALA LEU          
SEQRES  23 C  303  ALA HIS PRO PHE PHE GLN ASP VAL THR LYS PRO VAL PRO          
SEQRES  24 C  303  HIS LEU ARG LEU                                              
SEQRES   1 D  260  MET GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR          
SEQRES   2 D  260  LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY          
SEQRES   3 D  260  TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG          
SEQRES   4 D  260  ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU          
SEQRES   5 D  260  TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN          
SEQRES   6 D  260  TYR ILE ASP ARG PHE LEU SER SER MET SER VAL LEU ARG          
SEQRES   7 D  260  GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU          
SEQRES   8 D  260  ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA          
SEQRES   9 D  260  GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS          
SEQRES  10 D  260  GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU          
SEQRES  11 D  260  THR PHE ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU          
SEQRES  12 D  260  THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS          
SEQRES  13 D  260  VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU          
SEQRES  14 D  260  ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL          
SEQRES  15 D  260  ILE ALA GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL          
SEQRES  16 D  260  THR GLY GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR          
SEQRES  17 D  260  GLY TYR THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP          
SEQRES  18 D  260  LEU HIS GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN          
SEQRES  19 D  260  GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS          
SEQRES  20 D  260  GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU          
MODRES 5NEV TPO A  160  THR  MODIFIED RESIDUE                                   
MODRES 5NEV TPO C  160  THR  MODIFIED RESIDUE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET    72L  A 301      32                                                       
HET    72L  C 301      32                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     72L 4-[[6-(3-PHENYLPHENYL)-7~{H}-PURIN-2-                            
HETNAM   2 72L  YL]AMINO]BENZENESULFONAMIDE                                     
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   5  72L    2(C23 H18 N6 O2 S)                                           
FORMUL   7  HOH   *16(H2 O)                                                     
HELIX    1 AA1 PRO A   45  GLU A   57  1                                  13    
HELIX    2 AA2 LEU A   87  SER A   94  1                                   8    
HELIX    3 AA3 PRO A  100  HIS A  121  1                                  22    
HELIX    4 AA4 LYS A  129  GLN A  131  5                                   3    
HELIX    5 AA5 ASP A  145  ALA A  149  5                                   5    
HELIX    6 AA6 THR A  165  ARG A  169  5                                   5    
HELIX    7 AA7 ALA A  170  LEU A  175  1                                   6    
HELIX    8 AA8 THR A  182  ARG A  199  1                                  18    
HELIX    9 AA9 SER A  207  GLY A  220  1                                  14    
HELIX   10 AB1 GLY A  229  MET A  233  5                                   5    
HELIX   11 AB2 ASP A  247  VAL A  252  1                                   6    
HELIX   12 AB3 ASP A  256  LEU A  267  1                                  12    
HELIX   13 AB4 SER A  276  LEU A  281  1                                   6    
HELIX   14 AB5 ALA A  282  GLN A  287  5                                   6    
HELIX   15 AB6 TYR B  178  CYS B  193  1                                  16    
HELIX   16 AB7 GLY B  198  GLN B  203  1                                   6    
HELIX   17 AB8 THR B  207  TYR B  225  1                                  19    
HELIX   18 AB9 GLN B  228  MET B  246  1                                  19    
HELIX   19 AC1 LEU B  249  GLU B  269  1                                  21    
HELIX   20 AC2 GLU B  274  THR B  282  1                                   9    
HELIX   21 AC3 THR B  287  LEU B  302  1                                  16    
HELIX   22 AC4 THR B  310  PHE B  319  1                                  10    
HELIX   23 AC5 LEU B  320  GLN B  322  5                                   3    
HELIX   24 AC6 ASN B  326  SER B  340  1                                  15    
HELIX   25 AC7 ASP B  343  LEU B  348  1                                   6    
HELIX   26 AC8 LEU B  351  VAL B  367  1                                  17    
HELIX   27 AC9 PRO B  373  GLY B  381  1                                   9    
HELIX   28 AD1 THR B  383  LYS B  400  1                                  18    
HELIX   29 AD2 GLN B  407  TYR B  413  1                                   7    
HELIX   30 AD3 LYS B  414  HIS B  419  5                                   6    
HELIX   31 AD4 PRO C   45  GLU C   57  1                                  13    
HELIX   32 AD5 LEU C   87  SER C   94  1                                   8    
HELIX   33 AD6 PRO C  100  SER C  120  1                                  21    
HELIX   34 AD7 LYS C  129  GLN C  131  5                                   3    
HELIX   35 AD8 ASP C  145  ALA C  149  5                                   5    
HELIX   36 AD9 THR C  165  ARG C  169  5                                   5    
HELIX   37 AE1 ALA C  170  LEU C  175  1                                   6    
HELIX   38 AE2 THR C  182  THR C  198  1                                  17    
HELIX   39 AE3 SER C  207  GLY C  220  1                                  14    
HELIX   40 AE4 GLY C  229  MET C  233  5                                   5    
HELIX   41 AE5 ASP C  247  VAL C  252  1                                   6    
HELIX   42 AE6 ASP C  256  LEU C  267  1                                  12    
HELIX   43 AE7 SER C  276  LEU C  281  1                                   6    
HELIX   44 AE8 ALA C  282  GLN C  287  5                                   6    
HELIX   45 AE9 TYR D  178  CYS D  193  1                                  16    
HELIX   46 AF1 GLY D  198  GLN D  203  1                                   6    
HELIX   47 AF2 THR D  207  TYR D  225  1                                  19    
HELIX   48 AF3 GLN D  228  MET D  246  1                                  19    
HELIX   49 AF4 LEU D  249  GLU D  269  1                                  21    
HELIX   50 AF5 GLU D  274  THR D  282  1                                   9    
HELIX   51 AF6 THR D  287  LEU D  302  1                                  16    
HELIX   52 AF7 THR D  310  PHE D  319  1                                  10    
HELIX   53 AF8 LEU D  320  GLN D  322  5                                   3    
HELIX   54 AF9 ASN D  326  SER D  340  1                                  15    
HELIX   55 AG1 ASP D  343  LEU D  348  1                                   6    
HELIX   56 AG2 LEU D  351  VAL D  367  1                                  17    
HELIX   57 AG3 PRO D  373  GLY D  381  1                                   9    
HELIX   58 AG4 THR D  383  LYS D  400  1                                  18    
HELIX   59 AG5 GLN D  407  TYR D  413  1                                   7    
HELIX   60 AG6 LYS D  414  HIS D  419  5                                   6    
SHEET    1 AA1 5 PHE A   4  GLY A  13  0                                        
SHEET    2 AA1 5 GLY A  16  ASN A  23 -1  O  LYS A  20   N  GLU A   8           
SHEET    3 AA1 5 VAL A  29  ARG A  36 -1  O  LYS A  34   N  VAL A  17           
SHEET    4 AA1 5 LYS A  75  GLU A  81 -1  O  LEU A  76   N  ILE A  35           
SHEET    5 AA1 5 LEU A  66  HIS A  71 -1  N  ILE A  70   O  TYR A  77           
SHEET    1 AA2 3 GLN A  85  ASP A  86  0                                        
SHEET    2 AA2 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3 AA2 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1 AA3 2 VAL A 123  LEU A 124  0                                        
SHEET    2 AA3 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SHEET    1 AA4 5 PHE C   4  GLU C  12  0                                        
SHEET    2 AA4 5 VAL C  17  ASN C  23 -1  O  LYS C  20   N  GLU C   8           
SHEET    3 AA4 5 VAL C  29  ARG C  36 -1  O  LYS C  34   N  VAL C  17           
SHEET    4 AA4 5 LYS C  75  GLU C  81 -1  O  LEU C  76   N  ILE C  35           
SHEET    5 AA4 5 LEU C  66  HIS C  71 -1  N  ILE C  70   O  TYR C  77           
SHEET    1 AA5 3 GLN C  85  ASP C  86  0                                        
SHEET    2 AA5 3 LEU C 133  ILE C 135 -1  O  ILE C 135   N  GLN C  85           
SHEET    3 AA5 3 ILE C 141  LEU C 143 -1  O  LYS C 142   N  LEU C 134           
SHEET    1 AA6 2 VAL C 123  LEU C 124  0                                        
SHEET    2 AA6 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  1.35  
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        -6.73                     
CISPEP   2 GLN B  323    PRO B  324          0        -7.76                     
CISPEP   3 ASP B  345    PRO B  346          0        11.60                     
CISPEP   4 VAL C  154    PRO C  155          0        -3.96                     
CISPEP   5 GLN D  323    PRO D  324          0        -6.27                     
CISPEP   6 ASP D  345    PRO D  346          0        10.31                     
SITE     1 AC1 15 GLY A  11  GLU A  12  ALA A  31  VAL A  64                    
SITE     2 AC1 15 PHE A  80  GLU A  81  PHE A  82  LEU A  83                    
SITE     3 AC1 15 HIS A  84  GLN A  85  ASP A  86  LYS A  89                    
SITE     4 AC1 15 GLN A 131  LEU A 134  ASP A 145                               
SITE     1 AC2 15 ILE C  10  GLY C  11  LYS C  33  VAL C  64                    
SITE     2 AC2 15 PHE C  80  GLU C  81  LEU C  83  HIS C  84                    
SITE     3 AC2 15 GLN C  85  ASP C  86  LYS C  89  GLN C 131                    
SITE     4 AC2 15 LEU C 134  ASP C 145  GLN D 403                               
CRYST1   73.527  132.053  149.220  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      0.013600  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007573  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006702        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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