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Database: PDB
Entry: 2CCI
LinkDB: 2CCI
Original site: 2CCI 
HEADER    CELL CYCLE                              16-JAN-06   2CCI              
TITLE     CRYSTAL STRUCTURE OF PHOSPHO-CDK2 CYCLIN A IN COMPLEX WITH A PEPTIDE  
TITLE    2 CONTAINING BOTH THE SUBSTRATE AND RECRUITMENT SITES OF CDC6          
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 OTHER_DETAILS: PHOSPHORYLATED AT RESIDUE T160;                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CYCLIN-A2;                                                 
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 FRAGMENT: RESIDUES 175-432;                                          
COMPND  12 SYNONYM: CYCLIN-A,CYCLIN A;                                          
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: CELL DIVISION CONTROL PROTEIN 6 HOMOLOG;                   
COMPND  16 CHAIN: F, I;                                                         
COMPND  17 FRAGMENT: RESIDUES 71-100;                                           
COMPND  18 SYNONYM: CDC6-RELATED PROTEIN,CDC18-RELATED PROTEIN,HSCDC18,         
COMPND  19 P62(CDC6),HSCDC6;                                                    
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 MUTATION: YES;                                                       
COMPND  22 OTHER_DETAILS: PEPTIDE MODIFIED TO GENERATE ACTIVE SITE SEQUENCE     
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CDK2, CDKN2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: B834;                                      
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX;                                     
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: CCNA2, CCN1, CCNA;                                             
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: B834;                                      
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET21D;                                   
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 SYNTHETIC: YES;                                                      
SOURCE  21 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  22 ORGANISM_COMMON: HUMAN;                                              
SOURCE  23 ORGANISM_TAXID: 9606                                                 
KEYWDS    COMPLEX (TRANSFERASE-CELL DIVISION), PROTEIN KINASES, CELL CYCLE,     
KEYWDS   2 RECRUITMENT, SUBSTRATE RECOGNITION, ATP-BINDING, CELL DIVISION,      
KEYWDS   3 KINASE, MITOSIS, NUCLEOTIDE-BINDING, PHOSPHORYLATION,                
KEYWDS   4 SERINE/THREONINE- PROTEIN KINASE, TRANSFERASE, CYCLIN, DNA           
KEYWDS   5 REPLICATION, NUCLEAR PROTEIN, COMPLEX                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.Y.CHENG,M.E.M.NOBLE,V.SKAMNAKI,N.R.BROWN,E.D.LOWE,L.KONTOGIANNIS,   
AUTHOR   2 K.SHEN,P.A.COLE,G.SILIGARDI,L.N.JOHNSON                              
REVDAT   5   06-JUN-18 2CCI    1       COMPND SOURCE JRNL   DBREF               
REVDAT   5 2                   1       SEQADV                                   
REVDAT   4   13-JUL-11 2CCI    1       VERSN                                    
REVDAT   3   24-FEB-09 2CCI    1       VERSN                                    
REVDAT   2   09-AUG-06 2CCI    1       JRNL                                     
REVDAT   1   03-MAY-06 2CCI    0                                                
JRNL        AUTH   K.Y.CHENG,M.E.NOBLE,V.SKAMNAKI,N.R.BROWN,E.D.LOWE,           
JRNL        AUTH 2 L.KONTOGIANNIS,K.SHEN,P.A.COLE,G.SILIGARDI,L.N.JOHNSON       
JRNL        TITL   THE ROLE OF THE PHOSPHO-CDK2/CYCLIN A RECRUITMENT SITE IN    
JRNL        TITL 2 SUBSTRATE RECOGNITION.                                       
JRNL        REF    J. BIOL. CHEM.                V. 281 23167 2006              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   16707497                                                     
JRNL        DOI    10.1074/JBC.M600480200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 94.92                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 37597                          
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) : 0.264                           
REMARK   3   R VALUE            (WORKING SET) : 0.261                           
REMARK   3   FREE R VALUE                     : 0.321                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1996                            
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) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2760                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3560                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 154                          
REMARK   3   BIN FREE R VALUE                    : 0.4320                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9216                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 64                                      
REMARK   3   SOLVENT ATOMS            : 111                                     
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) : 37.66                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.57000                                             
REMARK   3    B22 (A**2) : 0.50000                                              
REMARK   3    B33 (A**2) : 1.07000                                              
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): 12.217        
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.446         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.347         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.164        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.838                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.775                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9509 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12917 ; 1.146 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1135 ; 5.337 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   407 ;39.457 ;23.735       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1671 ;17.130 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    50 ;17.830 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1459 ; 0.077 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7024 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4507 ; 0.200 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  6433 ; 0.303 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   337 ; 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):    86 ; 0.179 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.278 ; 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):  5888 ; 0.285 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9300 ; 0.506 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4105 ; 0.657 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3617 ; 1.104 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     0        A   296                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.3755  40.8399   3.3747              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2853 T22:  -0.1761                                     
REMARK   3      T33:  -0.1829 T12:   0.0320                                     
REMARK   3      T13:  -0.0210 T23:  -0.0102                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5096 L22:   1.9782                                     
REMARK   3      L33:   1.3512 L12:   0.7549                                     
REMARK   3      L13:   0.2030 L23:  -0.1575                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0873 S12:   0.0857 S13:   0.2090                       
REMARK   3      S21:   0.0409 S22:   0.0382 S23:   0.1389                       
REMARK   3      S31:  -0.2132 S32:  -0.1091 S33:   0.0491                       
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   432                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.1468  38.4769  32.4078              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2469 T22:  -0.1294                                     
REMARK   3      T33:  -0.2906 T12:  -0.0097                                     
REMARK   3      T13:  -0.0175 T23:  -0.0090                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6144 L22:   2.3564                                     
REMARK   3      L33:   1.6912 L12:  -0.6575                                     
REMARK   3      L13:  -0.5265 L23:   0.3242                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0607 S12:  -0.1652 S13:  -0.0443                       
REMARK   3      S21:   0.1825 S22:   0.0320 S23:   0.0236                       
REMARK   3      S31:  -0.0259 S32:   0.0618 S33:   0.0287                       
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):   8.7375  21.7896  54.1547              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0435 T22:   0.0710                                     
REMARK   3      T33:  -0.0152 T12:   0.1156                                     
REMARK   3      T13:  -0.0422 T23:  -0.0075                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1107 L22:   1.8822                                     
REMARK   3      L33:   1.9067 L12:  -0.7020                                     
REMARK   3      L13:  -1.2662 L23:   0.2110                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0583 S12:   0.2798 S13:   0.2579                       
REMARK   3      S21:  -0.2011 S22:  -0.1004 S23:   0.2718                       
REMARK   3      S31:  -0.4407 S32:  -0.4593 S33:   0.0421                       
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   432                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.8716  10.6441  85.3526              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1141 T22:  -0.0672                                     
REMARK   3      T33:  -0.0501 T12:   0.0551                                     
REMARK   3      T13:   0.1119 T23:   0.0140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3876 L22:   2.3707                                     
REMARK   3      L33:   1.5269 L12:  -0.2582                                     
REMARK   3      L13:  -0.2503 L23:   0.1664                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2111 S12:  -0.1738 S13:  -0.1159                       
REMARK   3      S21:   0.4579 S22:   0.0835 S23:   0.4207                       
REMARK   3      S31:   0.0126 S32:  -0.3151 S33:   0.1276                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2CCI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-JAN-06.                  
REMARK 100 THE DEPOSITION ID IS D_1290027145.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-NOV-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.60                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39629                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 2.200                              
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
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 1QMZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-17% (V/V) PEG MONOMETHYLETHER 5000,   
REMARK 280  0.2 M AMMONIUM SULPHATE AND 0.1 M MES PH 5.0-6.5, PH 5.60           
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       37.21000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       85.35450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.19450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       85.35450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.21000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.19450            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, F                               
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, I                               
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 INVOLVED IN THE CONTROL OF THE CELL CYCLE                            
REMARK 400  ENGINEERED RESIDUE IN CHAIN F, PRO 71 TO HIS                        
REMARK 400  ENGINEERED RESIDUE IN CHAIN F, PRO 72 TO HIS                        
REMARK 400  ENGINEERED RESIDUE IN CHAIN F, CYS 73 TO ALA                        
REMARK 400  ENGINEERED RESIDUE IN CHAIN F, PRO 76 TO ARG                        
REMARK 400  ENGINEERED RESIDUE IN CHAIN I, PRO 71 TO HIS                        
REMARK 400  ENGINEERED RESIDUE IN CHAIN I, PRO 72 TO HIS                        
REMARK 400  ENGINEERED RESIDUE IN CHAIN I, CYS 73 TO ALA                        
REMARK 400  ENGINEERED RESIDUE IN CHAIN I, PRO 76 TO ARG                        
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     ARG A   297                                                      
REMARK 465     LEU A   298                                                      
REMARK 465     ARG C   297                                                      
REMARK 465     LEU C   298                                                      
REMARK 465     GLN F    74                                                      
REMARK 465     GLY F    75                                                      
REMARK 465     LYS F    76                                                      
REMARK 465     LYS F    77                                                      
REMARK 465     GLU F    78                                                      
REMARK 465     ASN F    79                                                      
REMARK 465     GLY F    80                                                      
REMARK 465     PRO F    81                                                      
REMARK 465     PRO F    82                                                      
REMARK 465     HIS F    83                                                      
REMARK 465     SER F    84                                                      
REMARK 465     HIS I    67                                                      
REMARK 465     HIS I    68                                                      
REMARK 465     GLN I    74                                                      
REMARK 465     GLY I    75                                                      
REMARK 465     LYS I    76                                                      
REMARK 465     LYS I    77                                                      
REMARK 465     GLU I    78                                                      
REMARK 465     ASN I    79                                                      
REMARK 465     GLY I    80                                                      
REMARK 465     PRO I    81                                                      
REMARK 465     PRO I    82                                                      
REMARK 465     HIS I    83                                                      
REMARK 465     SER I    84                                                      
REMARK 465     HIS I    85                                                      
REMARK 465     ASP I    95                                                      
REMARK 465     ASN I    96                                                      
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    GLU A  12      104.41     22.79                                   
REMARK 500    THR A  14      -22.55     56.48                                   
REMARK 500    ASP A  38     -159.44     78.66                                   
REMARK 500    GLU A  40        9.79     80.58                                   
REMARK 500    THR A  41     -159.91    -77.28                                   
REMARK 500    HIS A  71       61.35   -109.98                                   
REMARK 500    LEU A  96      -79.29    -83.65                                   
REMARK 500    ARG A 126       13.15     58.22                                   
REMARK 500    ASP A 127       40.60   -148.27                                   
REMARK 500    ASP A 145       81.43     48.01                                   
REMARK 500    VAL A 164      131.30     76.14                                   
REMARK 500    SER A 181     -161.43   -163.20                                   
REMARK 500    TRP A 227       83.26   -154.36                                   
REMARK 500    ASP B 177      -64.18    -11.35                                   
REMARK 500    THR B 303       17.84     46.98                                   
REMARK 500    PHE B 304       13.81     80.07                                   
REMARK 500    TRP B 372      115.48    -31.92                                   
REMARK 500    GLU C  12       75.88   -117.28                                   
REMARK 500    THR C  14      -59.82     38.34                                   
REMARK 500    ASP C  38     -127.68     46.38                                   
REMARK 500    GLU C  40      -13.37     78.88                                   
REMARK 500    SER C  94       32.62    -84.56                                   
REMARK 500    ARG C 122       51.18     39.25                                   
REMARK 500    ASP C 127       51.48   -153.85                                   
REMARK 500    PRO C 130      -59.68    -28.81                                   
REMARK 500    ASN C 136     -158.80   -103.60                                   
REMARK 500    ASP C 145       86.76     64.10                                   
REMARK 500    VAL C 164      137.90     71.13                                   
REMARK 500    LEU C 166      -60.17    -29.15                                   
REMARK 500    SER C 181     -157.22   -152.71                                   
REMARK 500    ARG C 199      -38.70     72.78                                   
REMARK 500    TRP C 227       84.54   -154.04                                   
REMARK 500    SER C 239       33.77    -93.83                                   
REMARK 500    ARG C 245      104.89    -57.77                                   
REMARK 500    LEU C 281        9.75    -66.97                                   
REMARK 500    PRO C 284       -8.71    -55.84                                   
REMARK 500    CYS D 193       35.72    -77.10                                   
REMARK 500    THR D 303       36.69     37.61                                   
REMARK 500    VAL D 367      -66.84    -98.81                                   
REMARK 500    TRP D 372      106.44    -53.73                                   
REMARK 500    ASN D 415     -161.16    -72.40                                   
REMARK 500    HIS D 419      -26.45     67.92                                   
REMARK 500    ASN D 431       82.57     53.83                                   
REMARK 500    HIS F  68      121.32     95.80                                   
REMARK 500    ARG I  72     -164.56   -126.68                                   
REMARK 500    LEU I  87       84.28     54.10                                   
REMARK 500    LEU I  92      101.85     51.06                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1298  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 132   OD1                                                    
REMARK 620 2 ASP A 145   OD1  83.6                                              
REMARK 620 3 ATP A1297   O3B 134.6  93.4                                        
REMARK 620 4 ATP A1297   O1A  76.5  69.3  60.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C1298  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP C1297   O1G                                                    
REMARK 620 2 ASP C 145   OD1  88.1                                              
REMARK 620 3 ATP C1297   O2B  58.0  53.1                                        
REMARK 620 4 ATP C1297   O3G  54.9 121.4  68.4                                  
REMARK 620 5 ASN C 132   ND2 124.0  68.2 121.4 169.0                            
REMARK 620 6 ASN C 132   OD1  75.3  72.4 105.2 125.5  49.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1298                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C1298                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A1297                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP C1297                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AQ1   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR         
REMARK 900 STAUROSPORINE                                                        
REMARK 900 RELATED ID: 1B38   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2                                      
REMARK 900 RELATED ID: 1B39   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2 PHOSPHORYLATED ON THR 160            
REMARK 900 RELATED ID: 1BUH   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CDK2 KINASE COMPLEX WITHCELL CYCLE-   
REMARK 900 REGULATORY PROTEIN CKSHS1                                            
REMARK 900 RELATED ID: 1CKP   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR         
REMARK 900 PURVALANOL B                                                         
REMARK 900 RELATED ID: 1DI8   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) IN COMPLEX WITH 4- 
REMARK 900 [3- HYDROXYANILINO]-6,7-DIMETHOXYQUINAZOLINE                         
REMARK 900 RELATED ID: 1DM2   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR         
REMARK 900 HYMENIALDISINE                                                       
REMARK 900 RELATED ID: 1E1V   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR NU2058  
REMARK 900 RELATED ID: 1E1X   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR NU6027  
REMARK 900 RELATED ID: 1E9H   RELATED DB: PDB                                   
REMARK 900 THR 160 PHOSPHORYLATED CDK2 - HUMAN CYCLIN A3 COMPLEX WITH THE       
REMARK 900 INHIBITOR INDIRUBIN-5- SULPHONATE BOUND                              
REMARK 900 RELATED ID: 1F5Q   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MURINE GAMMA HERPESVIRUS CYCLIN COMPLEXED TO    
REMARK 900 HUMAN CYCLIN DEPENDANT KINASE 2                                      
REMARK 900 RELATED ID: 1FIN   RELATED DB: PDB                                   
REMARK 900 CYCLIN A - CYCLIN-DEPENDENT KINASE 2 COMPLEX                         
REMARK 900 RELATED ID: 1FQ1   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF KINASE ASSOCIATED PHOSPHATASE (KAP) INCOMPLEX   
REMARK 900 WITH PHOSPHO-CDK2                                                    
REMARK 900 RELATED ID: 1FVT   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) INCOMPLEX WITH AN  
REMARK 900 OXINDOLE INHIBITOR                                                   
REMARK 900 RELATED ID: 1FVV   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CDK2/CYCLIN A IN COMPLEX WITH AN OXINDOLEINHIBITOR  
REMARK 900 RELATED ID: 1G5S   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLIN DEPENDENT KINASE 2 (CDK2)IN        
REMARK 900 COMPLEX WITH THE INHIBITOR H717                                      
REMARK 900 RELATED ID: 1GIH   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE CDK4INHIBITOR     
REMARK 900 RELATED ID: 1GII   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE CDK4INHIBITOR     
REMARK 900 RELATED ID: 1GIJ   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE CDK4INHIBITOR     
REMARK 900 RELATED ID: 1GY3   RELATED DB: PDB                                   
REMARK 900 PCDK2/CYCLIN A IN COMPLEX WITH MGADP, NITRATE AND PEPTIDE SUBSTRATE  
REMARK 900 RELATED ID: 1GZ8   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR 2-      
REMARK 900 AMINO-6-(3'-METHYL- 2'-OXO)BUTOXYPURINE                              
REMARK 900 RELATED ID: 1H00   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6 -BIS ANILINO PYRIMIDINE    
REMARK 900 CDK4 INHIBITOR                                                       
REMARK 900 RELATED ID: 1H01   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 2, 4 -BIS ANILINO PYRIMIDINE    
REMARK 900 CDK4 INHIBITOR                                                       
REMARK 900 RELATED ID: 1H07   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6 -BIS ANILINO PYRIMIDINE    
REMARK 900 CDK4 INHIBITOR                                                       
REMARK 900 RELATED ID: 1H08   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 2, 4 -BIS ANILINO PYRIMIDINE    
REMARK 900 CDK4 INHIBITOR                                                       
REMARK 900 RELATED ID: 1H0V   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN COMPLEX WITH THE          
REMARK 900 INHIBITOR 2-AMINO-6-[(R )-PYRROLIDINO-5'-YL]METHOXYPURINE            
REMARK 900 RELATED ID: 1H0W   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN COMPLEX WITH THE          
REMARK 900 INHIBITOR 2-AMINO-6-[ CYCLOHEX-3-ENYL]METHOXYPURINE                  
REMARK 900 RELATED ID: 1H1P   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH THE  
REMARK 900 INHIBITOR NU2058                                                     
REMARK 900 RELATED ID: 1H1Q   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH THE  
REMARK 900 INHIBITOR NU6094                                                     
REMARK 900 RELATED ID: 1H1R   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH THE  
REMARK 900 INHIBITOR NU6086                                                     
REMARK 900 RELATED ID: 1H1S   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH THE  
REMARK 900 INHIBITOR NU6102                                                     
REMARK 900 RELATED ID: 1H24   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH A 9 RESIDUE RECRUITMENT PEPTIDE FROM    
REMARK 900 E2F                                                                  
REMARK 900 RELATED ID: 1H25   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM  
REMARK 900 E2F                                                                  
REMARK 900 RELATED ID: 1H26   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM  
REMARK 900 P53                                                                  
REMARK 900 RELATED ID: 1H27   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM  
REMARK 900 P27                                                                  
REMARK 900 RELATED ID: 1H28   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM  
REMARK 900 P107                                                                 
REMARK 900 RELATED ID: 1HCK   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2                                      
REMARK 900 RELATED ID: 1HCL   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2                                      
REMARK 900 RELATED ID: 1JST   RELATED DB: PDB                                   
REMARK 900 PHOSPHORYLATED CYCLIN-DEPENDENT KINASE-2 BOUND TO CYCLIN A           
REMARK 900 RELATED ID: 1JSU   RELATED DB: PDB                                   
REMARK 900 P27(KIP1)/CYCLIN A/CDK2 COMPLEX                                      
REMARK 900 RELATED ID: 1JSV   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) INCOMPLEX WITH 4-  
REMARK 900 [(6-AMINO-4- PYRIMIDINYL)AMINO]BENZENESULFONAMIDE                    
REMARK 900 RELATED ID: 1JVP   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CDK2 ( UNPHOSPHORYLATED) INCOMPLEX WITH   
REMARK 900 PKF049-365                                                           
REMARK 900 RELATED ID: 1KE5   RELATED DB: PDB                                   
REMARK 900 CDK2 COMPLEXED WITH N-METHYL-4-{[(2-OXO- 1,2-DIHYDRO-3H-INDOL-3-     
REMARK 900 YLIDENE)METHYL] AMINO}BENZENESULFONAMIDE                             
REMARK 900 RELATED ID: 1KE6   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH N-METHYL-{4-[2-(7-   
REMARK 900 OXO-6,7-DIHYDRO -8H-[1,3]THIAZOLO[5,4-E]INDOL-8- YLIDENE)HYDRAZINO]  
REMARK 900 PHENYL}METHANESULFONAMIDE                                            
REMARK 900 RELATED ID: 1KE7   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 3-{[(2,2-DIOXIDO-1,  
REMARK 900 3-DIHYDRO-2- BENZOTHIEN-5-YL)AMINO]METHYLENE}-5-(1,3- OXAZOL-5-YL)-  
REMARK 900 1,3-DIHYDRO-2H-INDOL-2- ONE                                          
REMARK 900 RELATED ID: 1KE8   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 4-{[(2-OXO-1,2-      
REMARK 900 DIHYDRO-3H-INDOL-3 -YLIDENE)METHYL]AMINO}-N-(1,3-THIAZOL-2- YL)      
REMARK 900 BENZENESULFONAMIDE                                                   
REMARK 900 RELATED ID: 1KE9   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 3-{[4-({             
REMARK 900 [AMINO(IMINO)METHYL] AMINOSULFONYL)ANILINO]METHYLENE}-2-OXO-2,3-     
REMARK 900 DIHYDRO-1H-INDOLE                                                    
REMARK 900 RELATED ID: 1OGU   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH A 2- 
REMARK 900 ARYLAMINO-4- CYCLOHEXYLMETHYL-5-NITROSO-6-AMINOPYRIMIDINE INHIBITOR  
REMARK 900 RELATED ID: 1OI9   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH A 6- 
REMARK 900 CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR                       
REMARK 900 RELATED ID: 1OIQ   RELATED DB: PDB                                   
REMARK 900 IMIDAZOPYRIDINES: A POTENT AND SELECTIVE CLASS OF CYCLIN-DEPENDENT   
REMARK 900 KINASE INHIBITORS IDENTIFIED THROUGH STRUCTURE-BASED HYBRIDISATION   
REMARK 900 RELATED ID: 1OIR   RELATED DB: PDB                                   
REMARK 900 IMIDAZOPYRIDINES: A POTENT AND SELECTIVE CLASS OF CYCLIN-DEPENDENT   
REMARK 900 KINASE INHIBITORS IDENTIFIED THROUGH STRUCTURE-BASED HYBRIDISATION   
REMARK 900 RELATED ID: 1OIT   RELATED DB: PDB                                   
REMARK 900 IMIDAZOPYRIDINES: A POTENT AND SELECTIVE CLASS OF CYCLIN-DEPENDENT   
REMARK 900 KINASE INHIBITORS IDENTIFIED THROUGH STRUCTURE-BASED HYBRIDISATION   
REMARK 900 RELATED ID: 1OIU   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH A 6- 
REMARK 900 CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR                       
REMARK 900 RELATED ID: 1OIY   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH A 6- 
REMARK 900 CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR                       
REMARK 900 RELATED ID: 1OKU   RELATED DB: PDB                                   
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-ALA- ALA-ABU-ARG-ER-LEU-ILE-(P-  
REMARK 900 F-PHE)-NH2                                                           
REMARK 900 RELATED ID: 1OKV   RELATED DB: PDB                                   
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-ARG- ARG-LEU-ILE-PHE-NH2         
REMARK 900 RELATED ID: 1OKW   RELATED DB: PDB                                   
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR AC-ARG- ARG-LEU-ASN-(M-CL-PHE)-NH2 
REMARK 900 RELATED ID: 1OL1   RELATED DB: PDB                                   
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-CIT- CIT-LEU-ILE-(P-F-PHE)-NH2   
REMARK 900 RELATED ID: 1OL2   RELATED DB: PDB                                   
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-ARG- ARG-LEU-ASN-(P-F-PHE)-NH2   
REMARK 900 RELATED ID: 1P2A   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN DEPENDENT KINASE 2 (CKD2) WITH               
REMARK 900 ATRISUBSTITUTED NAPHTHOSTYRIL INHIBITOR                              
REMARK 900 RELATED ID: 1P5E   RELATED DB: PDB                                   
REMARK 900 THE STRUCURE OF PHOSPHO-CDK2/CYCLIN A IN COMPLEX WITH THEINHIBITOR   
REMARK 900 4,5,6,7- TETRABROMOBENZOTRIAZOLE (TBS)                               
REMARK 900 RELATED ID: 1PF8   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLIN-DEPENDENT KINASE 2COMPLEXED WITH   
REMARK 900 A NUCLEOSIDE INHIBITOR                                               
REMARK 900 RELATED ID: 1PKD   RELATED DB: PDB                                   
REMARK 900 THE CRYSTAL STRUCTURE OF UCN-01 IN COMPLEX WITH PHOSPHO-CDK2/CYCLIN  
REMARK 900 A                                                                    
REMARK 900 RELATED ID: 1PW2   RELATED DB: PDB                                   
REMARK 900 APO STRUCTURE OF HUMAN CYCLIN-DEPENDENT KINASE 2                     
REMARK 900 RELATED ID: 1PXI   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THEINHIBITOR 4-(2,5-  
REMARK 900 DICHLORO-THIOPHEN- 3-YL)-PYRIMIDIN-2-YLAMINE                         
REMARK 900 RELATED ID: 1PXJ   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THEINHIBITOR 4-(2,4-  
REMARK 900 DIMETHYL-THIAZOL- 5-YL)-PYRIMIDIN-2-YLAMINE                          
REMARK 900 RELATED ID: 1PXK   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THEINHIBITOR N-[4-(2, 
REMARK 900 4-DIMETHYL- THIAZOL-5-YL)PYRIMIDIN-2-YL]-N'- HYDROXYIMINOFORMAMIDE   
REMARK 900 RELATED ID: 1PXL   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THEINHIBITOR [4-(2,4- 
REMARK 900 DIMETHYL-THIAZOL- 5-YL)-PYRIMIDIN-2-YL]-(4-TRIFLUOROMETHYL- PHENYL)- 
REMARK 900 AMINE                                                                
REMARK 900 RELATED ID: 1PXM   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THEINHIBITOR 3-[4-(2, 
REMARK 900 4-DIMETHYL- THIAZOL-5-YL)-PYRIMIDIN-2-YLAMINO]-PHENOL                
REMARK 900 RELATED ID: 1PXN   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THEINHIBITOR 4-[4-(4- 
REMARK 900 METHYL-2- METHYLAMINO-THIAZOL-5-YL)-PYRIMIDIN-2- YLAMINO]-PHENOL     
REMARK 900 RELATED ID: 1PXO   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THEINHIBITOR [4-(2-   
REMARK 900 AMINO-4-METHYL- THIAZOL-5-YL)-PYRIMIDIN-2-YL]-(3-NITRO- PHENYL)-     
REMARK 900 AMINE                                                                
REMARK 900 RELATED ID: 1PXP   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THEINHIBITOR N-[4-(2, 
REMARK 900 4-DIMETHYL- THIAZOL-5-YL)-PYRIMIDIN-2-YL]-N',N'- DIMETHYL-BENZENE-1, 
REMARK 900 4-DIAMINE                                                            
REMARK 900 RELATED ID: 1PYE   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF CDK2 WITH INHIBITOR                             
REMARK 900 RELATED ID: 1QMZ   RELATED DB: PDB                                   
REMARK 900 PHOSPHORYLATED CDK2-CYCLYIN A-SUBSTRATE PEPTIDE COMPLEX              
REMARK 900 RELATED ID: 1R78   RELATED DB: PDB                                   
REMARK 900 CDK2 COMPLEX WITH A 4-ALKYNYL OXINDOLE INHIBITOR                     
REMARK 900 RELATED ID: 1URC   RELATED DB: PDB                                   
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-ARG- ARG-LEU-ASN-(P-F-PHE)-NH2   
REMARK 900 RELATED ID: 1URW   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH AN IMIDAZO[1,2-B] PYRIDAZINE                    
REMARK 900 RELATED ID: 1V1K   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6 -BIS ANILINO PYRIMIDINE    
REMARK 900 CDK4 INHIBITOR                                                       
REMARK 900 RELATED ID: 1VYW   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CDK2/CYCLIN A WITH PNU-292137                           
REMARK 900 RELATED ID: 1VYZ   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CDK2 COMPLEXED WITH PNU-181227                          
REMARK 900 RELATED ID: 1W0X   RELATED DB: PDB                                   
REMARK 900 CRYSTALS STRUCTURE OF HUMAN CDK2 IN COMPLEX WITH THE INHIBITOR       
REMARK 900 OLOMOUCINE.                                                          
REMARK 900 RELATED ID: 1W8C   RELATED DB: PDB                                   
REMARK 900 CO-CRYSTAL STRUCTURE OF 6-CYCLOHEXYLMETHOXY- 8-ISOPROPYL-9H-PURIN-2- 
REMARK 900 YLAMINE AND MONOMERIC CDK2                                           
REMARK 900 RELATED ID: 1W98   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURAL BASIS OF CDK2 ACTIVATION BY CYCLIN E                  
REMARK 900 RELATED ID: 1WCC   RELATED DB: PDB                                   
REMARK 900 SCREENING FOR FRAGMENT BINDING BY X-RAY CRYSTALLOGRAPHY              
REMARK 900 RELATED ID: 1Y8Y   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CDK2 COMPLEXED WITH A PYRAZOLO[1,5-A]     
REMARK 900 PYRIMIDINE INHIBITOR                                                 
REMARK 900 RELATED ID: 1Y91   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CDK2 COMPLEXED WITH A PYRAZOLO[1,5-A]     
REMARK 900 PYRIMIDINE INHIBITOR                                                 
REMARK 900 RELATED ID: 2B52   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH DPH-042562     
REMARK 900 RELATED ID: 2B53   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH DIN-234325     
REMARK 900 RELATED ID: 2B54   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 (CKD2) COMPLEXED WITH DIN-232305     
REMARK 900 RELATED ID: 2B55   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 (CDK2) COMPLEXED WITHINDENOPYRAXOLE  
REMARK 900 DIN-101312                                                           
REMARK 900 RELATED ID: 2BHE   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN COMPLEX WITH THE          
REMARK 900 INHIBITOR 5-BROMO- INDIRUBINE                                        
REMARK 900 RELATED ID: 2BHH   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN COMPLEX WITH THE          
REMARK 900 INHIBITOR 4- HYDROXYPIPERINDINESULFONYL-INDIRUBINE                   
REMARK 900 RELATED ID: 2BKZ   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CDK2-CYCLIN A WITH PHA-404611                           
REMARK 900 RELATED ID: 2BPM   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CDK2-CYCLIN A WITH PHA-630529                           
REMARK 900 RELATED ID: 2BTR   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CDK2 COMPLEXED WITH PNU-198873                          
REMARK 900 RELATED ID: 2BTS   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CDK2 COMPLEXED WITH PNU-230032                          
REMARK 900 RELATED ID: 2C4G   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CDK2-CYCLIN A WITH PHA-533514                           
REMARK 900 RELATED ID: 2C5N   RELATED DB: PDB                                   
REMARK 900 DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2       
REMARK 900 PROVIDES INSIGHTS FOR DRUG DESIGN                                    
REMARK 900 RELATED ID: 2C5O   RELATED DB: PDB                                   
REMARK 900 DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2       
REMARK 900 PROVIDES INSIGHTS FOR DRUG DESIGN                                    
REMARK 900 RELATED ID: 2C5P   RELATED DB: PDB                                   
REMARK 900 DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2       
REMARK 900 PROVIDES INSIGHTS FOR DRUG DESIGN                                    
REMARK 900 RELATED ID: 2C5T   RELATED DB: PDB                                   
REMARK 900 DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2       
REMARK 900 PROVIDES INSIGHTS FOR DRUG DESIGN                                    
REMARK 900 RELATED ID: 2C5V   RELATED DB: PDB                                   
REMARK 900 DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2       
REMARK 900 PROVIDES INSIGHTS FOR DRUG DESIGN                                    
REMARK 900 RELATED ID: 2C5X   RELATED DB: PDB                                   
REMARK 900 DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2       
REMARK 900 PROVIDES INSIGHTS FOR DRUG DESIGN                                    
REMARK 900 RELATED ID: 2C5Y   RELATED DB: PDB                                   
REMARK 900 DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2       
REMARK 900 PROVIDES INSIGHTS FOR DRUG DESIGN                                    
REMARK 900 RELATED ID: 2C68   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CDK2 COMPLEXED WITH THE               
REMARK 900 TRIAZOLOPYRIMIDINE INHIBITOR                                         
REMARK 900 RELATED ID: 2C69   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CDK2 COMPLEXED WITH THE               
REMARK 900 TRIAZOLOPYRIMIDINE INHIBITOR                                         
REMARK 900 RELATED ID: 2C6I   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CDK2 COMPLEXED WITH THE               
REMARK 900 TRIAZOLOPYRIMIDINE INHIBITOR                                         
REMARK 900 RELATED ID: 2C6K   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CDK2 COMPLEXED WITH THE               
REMARK 900 TRIAZOLOPYRIMIDINE INHIBITOR                                         
REMARK 900 RELATED ID: 2C6L   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CDK2 COMPLEXED WITH THE               
REMARK 900 TRIAZOLOPYRIMIDINE INHIBITOR                                         
REMARK 900 RELATED ID: 2C6M   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CDK2 COMPLEXED WITH THE               
REMARK 900 TRIAZOLOPYRIMIDINE INHIBITOR                                         
REMARK 900 RELATED ID: 2C6O   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CDK2 COMPLEXED WITH THE               
REMARK 900 TRIAZOLOPYRIMIDINE INHIBITOR                                         
REMARK 900 RELATED ID: 2C6T   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CDK2 COMPLEXED WITH THE               
REMARK 900 TRIAZOLOPYRIMIDINE INHIBITOR                                         
REMARK 900 RELATED ID: 2CCH   RELATED DB: PDB                                   
REMARK 900 THE CRYSTAL STRUCTURE OF CDK2 CYCLIN A IN COMPLEX WITH A SUBSTRATE   
REMARK 900 PEPTIDE DERIVED FROM CDC MODIFIED WITH A GAMMA-LINKED ATP ANALOGUE   
REMARK 900 RELATED ID: 2EXM   RELATED DB: PDB                                   
REMARK 900 HUMAN CDK2 IN COMPLEX WITH ISOPENTENYLADENINE                        
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 CHAINS B AND D ARE A TRUNCATED FRAGMENT OF CYCLIN A2                 
REMARK 999  CONSISTING OF RESIDUES 175-432                                      
REMARK 999  THE PEPTIDE CONTAINS RESIDUES 71-100 OF CDC6 WITH THE               
REMARK 999  FIRST SEVEN PEPTIDES MODIFIED TO GENERATE AN IDEAL                  
REMARK 999  SUBSTRATE                                                           
DBREF  2CCI A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  2CCI B  175   432  UNP    P20248   CCNA2_HUMAN    175    432             
DBREF  2CCI C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  2CCI D  175   432  UNP    P20248   CCNA2_HUMAN    175    432             
DBREF  2CCI F   67    96  UNP    Q99741   CDC6_HUMAN      71    100             
DBREF  2CCI I   67    96  UNP    Q99741   CDC6_HUMAN      71    100             
SEQADV 2CCI SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 2CCI SER C    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 2CCI HIS F   67  UNP  Q99741    PRO    71 ENGINEERED MUTATION            
SEQADV 2CCI HIS F   68  UNP  Q99741    PRO    72 ENGINEERED MUTATION            
SEQADV 2CCI ALA F   69  UNP  Q99741    CYS    73 ENGINEERED MUTATION            
SEQADV 2CCI ARG F   72  UNP  Q99741    PRO    76 ENGINEERED MUTATION            
SEQADV 2CCI HIS I   67  UNP  Q99741    PRO    71 ENGINEERED MUTATION            
SEQADV 2CCI HIS I   68  UNP  Q99741    PRO    72 ENGINEERED MUTATION            
SEQADV 2CCI ALA I   69  UNP  Q99741    CYS    73 ENGINEERED MUTATION            
SEQADV 2CCI ARG I   72  UNP  Q99741    PRO    76 ENGINEERED MUTATION            
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  258  VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU ARG          
SEQRES   2 B  258  GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET          
SEQRES   3 B  258  LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE          
SEQRES   4 B  258  LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS          
SEQRES   5 B  258  LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE          
SEQRES   6 B  258  ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS          
SEQRES   7 B  258  LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER          
SEQRES   8 B  258  LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE          
SEQRES   9 B  258  VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN VAL          
SEQRES  10 B  258  LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR PHE          
SEQRES  11 B  258  ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN          
SEQRES  12 B  258  TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL GLU          
SEQRES  13 B  258  SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP          
SEQRES  14 B  258  ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE ALA          
SEQRES  15 B  258  GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY          
SEQRES  16 B  258  GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY TYR          
SEQRES  17 B  258  THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU HIS          
SEQRES  18 B  258  GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER          
SEQRES  19 B  258  ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY VAL          
SEQRES  20 B  258  SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU                  
SEQRES   1 C  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  258  VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU ARG          
SEQRES   2 D  258  GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET          
SEQRES   3 D  258  LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE          
SEQRES   4 D  258  LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS          
SEQRES   5 D  258  LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE          
SEQRES   6 D  258  ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS          
SEQRES   7 D  258  LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER          
SEQRES   8 D  258  LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE          
SEQRES   9 D  258  VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN VAL          
SEQRES  10 D  258  LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR PHE          
SEQRES  11 D  258  ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN          
SEQRES  12 D  258  TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL GLU          
SEQRES  13 D  258  SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP          
SEQRES  14 D  258  ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE ALA          
SEQRES  15 D  258  GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY          
SEQRES  16 D  258  GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY TYR          
SEQRES  17 D  258  THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU HIS          
SEQRES  18 D  258  GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER          
SEQRES  19 D  258  ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY VAL          
SEQRES  20 D  258  SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU                  
SEQRES   1 F   30  HIS HIS ALA SER PRO ARG LYS GLN GLY LYS LYS GLU ASN          
SEQRES   2 F   30  GLY PRO PRO HIS SER HIS THR LEU LYS GLY ARG ARG LEU          
SEQRES   3 F   30  VAL PHE ASP ASN                                              
SEQRES   1 I   30  HIS HIS ALA SER PRO ARG LYS GLN GLY LYS LYS GLU ASN          
SEQRES   2 I   30  GLY PRO PRO HIS SER HIS THR LEU LYS GLY ARG ARG LEU          
SEQRES   3 I   30  VAL PHE ASP ASN                                              
MODRES 2CCI TPO A  160  THR  MODIFIED RESIDUE                                   
MODRES 2CCI TPO C  160  THR  MODIFIED RESIDUE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET    ATP  A1297      31                                                       
HET     MG  A1298       1                                                       
HET    ATP  C1297      31                                                       
HET     MG  C1298       1                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   7  ATP    2(C10 H16 N5 O13 P3)                                         
FORMUL   8   MG    2(MG 2+)                                                     
FORMUL  11  HOH   *111(H2 O)                                                    
HELIX    1   1 PRO A   45  LYS A   56  1                                  12    
HELIX    2   2 LEU A   87  ALA A   93  1                                   7    
HELIX    3   3 PRO A  100  HIS A  121  1                                  22    
HELIX    4   4 LYS A  129  GLN A  131  5                                   3    
HELIX    5   5 THR A  165  ARG A  169  5                                   5    
HELIX    6   6 ALA A  170  LEU A  175  1                                   6    
HELIX    7   7 THR A  182  ARG A  199  1                                  18    
HELIX    8   8 SER A  207  GLY A  220  1                                  14    
HELIX    9   9 GLY A  229  MET A  233  5                                   5    
HELIX   10  10 ASP A  247  VAL A  251  5                                   5    
HELIX   11  11 ASP A  256  LEU A  267  1                                  12    
HELIX   12  12 SER A  276  LEU A  281  1                                   6    
HELIX   13  13 ALA A  282  GLN A  287  5                                   6    
HELIX   14  14 VAL B  175  ASP B  177  5                                   3    
HELIX   15  15 TYR B  178  CYS B  193  1                                  16    
HELIX   16  16 THR B  207  LYS B  226  1                                  20    
HELIX   17  17 GLN B  228  SER B  244  1                                  17    
HELIX   18  18 LEU B  249  GLY B  251  5                                   3    
HELIX   19  19 LYS B  252  GLU B  269  1                                  18    
HELIX   20  20 GLU B  274  ILE B  281  1                                   8    
HELIX   21  21 THR B  287  LEU B  302  1                                  16    
HELIX   22  22 THR B  310  LEU B  320  1                                  11    
HELIX   23  23 ASN B  326  ASP B  343  1                                  18    
HELIX   24  24 ASP B  343  LEU B  348  1                                   6    
HELIX   25  25 LEU B  351  THR B  368  1                                  18    
HELIX   26  26 PRO B  373  GLY B  381  1                                   9    
HELIX   27  27 LEU B  387  ALA B  401  1                                  15    
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  GLU C   57  1                                  13    
HELIX   33  33 LEU C   87  SER C   94  1                                   8    
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  GLY C  220  1                                  14    
HELIX   40  40 ASP C  247  VAL C  252  1                                   6    
HELIX   41  41 ASP C  256  HIS C  268  1                                  13    
HELIX   42  42 SER C  276  LEU C  281  1                                   6    
HELIX   43  43 ALA C  282  GLN C  287  5                                   6    
HELIX   44  44 TYR D  178  CYS D  193  1                                  16    
HELIX   45  45 THR D  207  TYR D  225  1                                  19    
HELIX   46  46 GLN D  228  MET D  246  1                                  19    
HELIX   47  47 LEU D  249  GLY D  251  5                                   3    
HELIX   48  48 LYS D  252  GLU D  269  1                                  18    
HELIX   49  49 GLU D  274  ILE D  281  1                                   8    
HELIX   50  50 THR D  287  LEU D  302  1                                  16    
HELIX   51  51 THR D  310  LEU D  320  1                                  11    
HELIX   52  52 CYS D  327  SER D  340  1                                  14    
HELIX   53  53 ASP D  343  LEU D  348  1                                   6    
HELIX   54  54 LEU D  351  VAL D  367  1                                  17    
HELIX   55  55 PRO D  373  GLY D  381  1                                   9    
HELIX   56  56 LEU D  387  ALA D  401  1                                  15    
HELIX   57  57 GLN D  407  TYR D  413  1                                   7    
HELIX   58  58 GLY D  420  LEU D  424  5                                   5    
SHEET    1  AA 5 PHE A   4  LYS A   9  0                                        
SHEET    2  AA 5 VAL A  18  ASN A  23 -1  O  LYS A  20   N  VAL A   7           
SHEET    3  AA 5 VAL A  29  ARG A  36 -1  O  VAL A  30   N  ALA A  21           
SHEET    4  AA 5 LYS A  75  GLU A  81 -1  O  LEU A  76   N  ILE A  35           
SHEET    5  AA 5 LEU A  66  HIS A  71 -1  N  LEU A  67   O  VAL A  79           
SHEET    1  AB 3 GLN A  85  ASP A  86  0                                        
SHEET    2  AB 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3  AB 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1  AC 2 VAL A 123  LEU A 124  0                                        
SHEET    2  AC 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SHEET    1  CA 5 PHE C   4  GLY C  13  0                                        
SHEET    2  CA 5 GLY C  16  ASN C  23 -1  O  GLY C  16   N  GLY C  13           
SHEET    3  CA 5 VAL C  29  ARG C  36 -1  O  VAL C  30   N  ALA C  21           
SHEET    4  CA 5 LYS C  75  GLU C  81 -1  O  LEU C  76   N  ILE C  35           
SHEET    5  CA 5 LEU C  66  HIS C  71 -1  N  LEU C  67   O  VAL C  79           
SHEET    1  CB 3 GLN C  85  ASP C  86  0                                        
SHEET    2  CB 3 LEU C 133  ILE C 135 -1  O  ILE C 135   N  GLN C  85           
SHEET    3  CB 3 ILE C 141  LEU C 143 -1  O  LYS C 142   N  LEU C 134           
SHEET    1  CC 2 VAL C 123  LEU C 124  0                                        
SHEET    2  CC 2 ARG C 150  ALA C 151 -1  O  ARG C 150   N  LEU C 124           
LINK         C   TYR A 159                 N   TPO A 160     1555   1555  1.33  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.33  
LINK        MG    MG A1298                 OD1 ASN A 132     1555   1555  2.34  
LINK        MG    MG A1298                 OD1 ASP A 145     1555   1555  1.91  
LINK        MG    MG A1298                 O3B ATP A1297     1555   1555  2.62  
LINK        MG    MG A1298                 O1A ATP A1297     1555   1555  2.96  
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  
LINK         O1G ATP C1297                MG    MG C1298     1555   1555  1.86  
LINK        MG    MG C1298                 OD1 ASP C 145     1555   1555  2.49  
LINK        MG    MG C1298                 O2B ATP C1297     1555   1555  3.14  
LINK        MG    MG C1298                 O3G ATP C1297     1555   1555  3.09  
LINK        MG    MG C1298                 ND2 ASN C 132     1555   1555  2.81  
LINK        MG    MG C1298                 OD1 ASN C 132     1555   1555  2.50  
CISPEP   1 VAL A  154    PRO A  155          0        -4.00                     
CISPEP   2 GLN B  323    PRO B  324          0        -2.52                     
CISPEP   3 ASP B  345    PRO B  346          0         5.80                     
CISPEP   4 VAL C  154    PRO C  155          0        -5.81                     
CISPEP   5 GLN D  323    PRO D  324          0        -3.49                     
CISPEP   6 ASP D  345    PRO D  346          0         2.08                     
SITE     1 AC1  3 ASN A 132  ASP A 145  ATP A1297                               
SITE     1 AC2  4 LYS C 129  ASN C 132  ASP C 145  ATP C1297                    
SITE     1 AC3 18 GLY A  11  GLU A  12  GLY A  13  THR A  14                    
SITE     2 AC3 18 ALA A  31  LYS A  33  PHE A  80  GLU A  81                    
SITE     3 AC3 18 PHE A  82  LEU A  83  ASP A  86  GLN A 131                    
SITE     4 AC3 18 ASN A 132  LEU A 134  ASP A 145   MG A1298                    
SITE     5 AC3 18 HOH A2044  ARG F  72                                          
SITE     1 AC4 15 ILE C  10  GLY C  11  GLY C  13  THR C  14                    
SITE     2 AC4 15 ALA C  31  LYS C  33  GLU C  81  LEU C  83                    
SITE     3 AC4 15 ASP C  86  GLN C 131  ASN C 132  LEU C 134                    
SITE     4 AC4 15 ASP C 145   MG C1298  HOH C2022                               
CRYST1   74.420  114.389  170.709  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      0.013437  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008742  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005858        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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