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Database: PDB
Entry: 1QMZ
LinkDB: 1QMZ
Original site: 1QMZ 
HEADER    CELL CYCLE                              11-OCT-99   1QMZ              
TITLE     PHOSPHORYLATED CDK2-CYCLYIN A-SUBSTRATE PEPTIDE COMPLEX               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION PROTEIN KINASE 2;                            
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: CYCLIN-DEPENDENT KINASE-2, CDK2, P33 PROTEIN                
COMPND   5  KINASE;                                                             
COMPND   6 EC: 2.7.1.-;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: PHOSPHORYLATED;                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: G2/MITOTIC-SPECIFIC CYCLIN A;                              
COMPND  11 CHAIN: B, D;                                                         
COMPND  12 FRAGMENT: RESIDUES 174-432;                                          
COMPND  13 SYNONYM: CCNA, CCN1;                                                 
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: SUBSTRATE PEPTIDE;                                         
COMPND  17 CHAIN: E, F;                                                         
COMPND  18 FRAGMENT: 1-7                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PGEX;                                     
SOURCE   8 OTHER_DETAILS: CYCLIN A-BOUND FORM PHOSPHORYLATED SOURCE             
SOURCE   9  COEXPRESSION WITH CAK1P;                                            
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PET21D;                                   
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 SYNTHETIC: YES;                                                      
SOURCE  19 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  20 ORGANISM_COMMON: HUMAN;                                              
SOURCE  21 ORGANISM_TAXID: 9606                                                 
KEYWDS    CELL CYCLE, COMPLEX (PROTEIN KINASE/CYCLIN), CYCLIN, CDK,             
KEYWDS   2 PHOSPHORYLATION, SUBSTRATE COMPLEX                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.R.BROWN,M.E.M.NOBLE,J.A.ENDICOTT,L.N.JOHNSON                        
REVDAT   4   24-FEB-09 1QMZ    1       VERSN                                    
REVDAT   3   03-MAR-06 1QMZ    1       COMPND                                   
REVDAT   2   24-JUL-03 1QMZ    1       COMPND JRNL                              
REVDAT   1   14-DEC-99 1QMZ    0                                                
JRNL        AUTH   N.R.BROWN,M.E.NOBLE,J.A.ENDICOTT,L.N.JOHNSON                 
JRNL        TITL   THE STRUCTURAL BASIS FOR SPECIFICITY OF SUBSTRATE            
JRNL        TITL 2 AND RECRUITMENT PEPTIDES FOR CYCLIN-DEPENDENT                
JRNL        TITL 3 KINASES                                                      
JRNL        REF    NAT.CELL BIOL.                V.   1   438 1999              
JRNL        REFN                   ISSN 1465-7392                               
JRNL        PMID   10559988                                                     
JRNL        DOI    10.1038/15674                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.0                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.6                            
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 39189                          
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) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.22                            
REMARK   3   FREE R VALUE                     : 0.28                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9036                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 86                                      
REMARK   3   SOLVENT ATOMS            : 767                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.3                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.019 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.048 ; 0.040               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.086 ; 0.050               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1QMZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-OCT-99.                  
REMARK 100 THE PDBE ID CODE IS EBI-4209.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-DEC-95                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ELETTRA                            
REMARK 200  BEAMLINE                       : 5.2R                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51615                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.600                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : 0.10100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: CDK2-CYCLIN A-RECRUITMENT PEPTIDE STRUCTURE          
REMARK 200  SUBMITTED ALONG WITH THIS STRUCTURE                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       76.30000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       81.85000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       76.30000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       81.85000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 300                                                                      
REMARK 300 DETAILS:BIOLOGICAL_UNIT: HETERODIMER OF DIMERS                       
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 11910 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 54860 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.4 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, 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 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     GLU B   174                                                      
REMARK 465     ARG C   297                                                      
REMARK 465     LEU C   298                                                      
REMARK 465     GLU D   174                                                      
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   O    SER A     0  -  O    HOH A  2001              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500                                                                      
REMARK 500   O    LYS B   379     NH2  ARG D   378     2665      1.70           
REMARK 500   NH2  ARG D   378     O    LYS B   379     2665      1.70           
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    SER B 340   CB    SER B 340   OG      0.081                       
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  22   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ARG A  22   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    THR A  39   N   -  CA  -  CB  ANGL. DEV. =  11.8 DEGREES          
REMARK 500    THR A  47   OG1 -  CB  -  CG2 ANGL. DEV. = -28.6 DEGREES          
REMARK 500    GLU A  51   OE1 -  CD  -  OE2 ANGL. DEV. = -12.2 DEGREES          
REMARK 500    VAL A  64   CA  -  CB  -  CG2 ANGL. DEV. = -11.5 DEGREES          
REMARK 500    TYR A  77   CB  -  CG  -  CD1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    LEU A  78   CA  -  CB  -  CG  ANGL. DEV. =  15.4 DEGREES          
REMARK 500    ARG A 122   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    GLN A 131   CG  -  CD  -  OE1 ANGL. DEV. =  19.1 DEGREES          
REMARK 500    GLN A 131   OE1 -  CD  -  NE2 ANGL. DEV. = -18.4 DEGREES          
REMARK 500    ARG A 150   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ARG A 150   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    VAL A 154   CA  -  C   -  O   ANGL. DEV. = -12.7 DEGREES          
REMARK 500    PRO A 155   C   -  N   -  CA  ANGL. DEV. =  12.5 DEGREES          
REMARK 500    ARG A 157   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    ARG A 157   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    VAL A 163   CA  -  CB  -  CG1 ANGL. DEV. =   9.4 DEGREES          
REMARK 500    VAL A 163   N   -  CA  -  CB  ANGL. DEV. = -16.4 DEGREES          
REMARK 500    ASP A 185   CB  -  CG  -  OD1 ANGL. DEV. =   9.3 DEGREES          
REMARK 500    GLU A 195   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.9 DEGREES          
REMARK 500    GLU A 208   OE1 -  CD  -  OE2 ANGL. DEV. = -13.3 DEGREES          
REMARK 500    ARG A 214   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A 214   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ARG A 217   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ASP A 223   CB  -  CG  -  OD1 ANGL. DEV. =   7.8 DEGREES          
REMARK 500    VAL A 230   CA  -  CB  -  CG2 ANGL. DEV. =  10.1 DEGREES          
REMARK 500    VAL A 230   CB  -  CA  -  C   ANGL. DEV. = -18.1 DEGREES          
REMARK 500    ARG A 245   NE  -  CZ  -  NH1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG A 245   NE  -  CZ  -  NH2 ANGL. DEV. = -14.2 DEGREES          
REMARK 500    ARG A 245   NH1 -  CZ  -  NH2 ANGL. DEV. =   8.4 DEGREES          
REMARK 500    VAL A 252   CG1 -  CB  -  CG2 ANGL. DEV. =  -9.9 DEGREES          
REMARK 500    ASP A 256   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP A 258   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG A 274   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ASP B 177   CB  -  CG  -  OD1 ANGL. DEV. =   7.6 DEGREES          
REMARK 500    TYR B 178   CA  -  CB  -  CG  ANGL. DEV. = -15.5 DEGREES          
REMARK 500    TYR B 178   CB  -  CG  -  CD2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    TYR B 178   CG  -  CD2 -  CE2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    GLU B 180   CG  -  CD  -  OE1 ANGL. DEV. =  12.4 DEGREES          
REMARK 500    ARG B 187   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    VAL B 197   CG1 -  CB  -  CG2 ANGL. DEV. =  -9.9 DEGREES          
REMARK 500    LEU B 232   CB  -  CG  -  CD2 ANGL. DEV. =  11.9 DEGREES          
REMARK 500    ARG B 241   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ALA B 259   N   -  CA  -  CB  ANGL. DEV. =   9.0 DEGREES          
REMARK 500    GLU B 277   OE1 -  CD  -  OE2 ANGL. DEV. =  11.9 DEGREES          
REMARK 500    PHE B 278   CB  -  CG  -  CD2 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ASP B 283   CB  -  CG  -  OD1 ANGL. DEV. =   9.3 DEGREES          
REMARK 500    ASP B 284   CB  -  CG  -  OD2 ANGL. DEV. =   8.1 DEGREES          
REMARK 500    ARG B 293   CG  -  CD  -  NE  ANGL. DEV. = -15.4 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     151 ANGLE DEVIATIONS                              
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 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    MET A   1       23.39    -75.72                                   
REMARK 500    LEU A  37     -107.50   -104.73                                   
REMARK 500    ASP A  38     -128.38    124.70                                   
REMARK 500    THR A  39      157.27    174.76                                   
REMARK 500    THR A  41     -151.80   -166.23                                   
REMARK 500    ASP A 127       40.78   -154.10                                   
REMARK 500    ASP A 145       78.45     47.53                                   
REMARK 500    PRO A 155      153.33    -42.03                                   
REMARK 500    VAL A 164      130.75     72.53                                   
REMARK 500    SER A 181     -144.69   -150.37                                   
REMARK 500    PHE B 304        6.38     59.13                                   
REMARK 500    PRO B 324      175.81    -49.46                                   
REMARK 500    TRP B 372      111.57    -33.02                                   
REMARK 500    THR C  14      -75.18    -26.03                                   
REMARK 500    LEU C  37     -108.42   -107.14                                   
REMARK 500    ASP C  38     -124.66    125.19                                   
REMARK 500    THR C  39      158.93    172.96                                   
REMARK 500    THR C  41     -152.09   -162.69                                   
REMARK 500    ASP C 127       37.15   -150.07                                   
REMARK 500    ASP C 145       80.53     41.15                                   
REMARK 500    PRO C 155      157.59    -44.07                                   
REMARK 500    VAL C 164      130.58     73.46                                   
REMARK 500    SER C 181     -144.09   -150.72                                   
REMARK 500    PHE D 304       13.18     55.80                                   
REMARK 500    PRO D 324      179.76    -50.18                                   
REMARK 500    TRP D 372      118.88    -36.59                                   
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 VAL A  154     PRO A  155                  -51.31                    
REMARK 500 GLN B  323     PRO B  324                  -63.05                    
REMARK 500 ASP B  345     PRO B  346                   48.28                    
REMARK 500 VAL C  154     PRO C  155                  -48.20                    
REMARK 500 GLN D  323     PRO D  324                  -65.22                    
REMARK 500 ASP D  345     PRO D  346                   45.97                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    SER A   0         18.58                                           
REMARK 500    PHE A 152         10.62                                           
REMARK 500    VAL A 154        -20.88                                           
REMARK 500    PRO B 309         10.40                                           
REMARK 500    GLN B 323        -24.13                                           
REMARK 500    ASP B 345         22.73                                           
REMARK 500    SER C   0        -20.43                                           
REMARK 500    VAL C 154        -20.48                                           
REMARK 500    GLN D 323        -26.23                                           
REMARK 500    ASP D 345         23.46                                           
REMARK 500    TYR D 347        -12.23                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL A 163        46.9      L          L   OUTSIDE RANGE           
REMARK 500    VAL B 197        23.8      L          L   OUTSIDE RANGE           
REMARK 500    ILE C  10        45.8      L          L   OUTSIDE RANGE           
REMARK 500    ARG C 150        25.0      L          L   OUTSIDE RANGE           
REMARK 500    VAL C 163        47.0      L          L   OUTSIDE RANGE           
REMARK 500    VAL D 197        24.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 383  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP A 381   O2G                                                    
REMARK 620 2 ASN A 132   OD1 105.7                                              
REMARK 620 3 ATP A 381   O3B  73.4 166.4                                        
REMARK 620 4 ATP A 381   O2A 149.0  98.7  78.4                                  
REMARK 620 5 HOH A2205   O    76.6  87.6  78.9  85.7                            
REMARK 620 6 ASP A 145   OD2  93.1  99.1  94.4 101.8 168.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 383  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 145   OD2                                                    
REMARK 620 2 ATP C 381   O2G  89.1                                              
REMARK 620 3 ATP C 381   O3B  91.6  78.8                                        
REMARK 620 4 ATP C 381   O2A  97.2 163.0  85.3                                  
REMARK 620 5 ASN C 132   OD1  94.4  98.1 173.2  97.1                            
REMARK 620 6 HOH C2195   O   171.2  82.6  84.2  90.1  89.4                      
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 A 383                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG C 383                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 381                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP C 381                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FIN   RELATED DB: PDB                                   
REMARK 900  CYCLIN A - CYCLIN-DEPENDENT KINASE 2 COMPLEX                        
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 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THREONINE 160 IN CHAINS A AND C HAS BEEN PHOSPHORYLATED              
REMARK 999 IN VIVO BY COEXPRESSION WITH CAK1P.                                  
DBREF  1QMZ A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  1QMZ C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  1QMZ B  174   432  UNP    P20248   CG2A_HUMAN     174    432             
DBREF  1QMZ D  174   432  UNP    P20248   CG2A_HUMAN     174    432             
DBREF  1QMZ E    2     8  PDB    1QMZ     1QMZ             2      8             
DBREF  1QMZ F    2     8  PDB    1QMZ     1QMZ             2      8             
SEQADV 1QMZ SER A    0  UNP  P24941              CLONING ARTIFACT               
SEQADV 1QMZ SER C    0  UNP  P24941              CLONING ARTIFACT               
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  259  GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU          
SEQRES   2 B  259  ARG GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR          
SEQRES   3 B  259  MET LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA          
SEQRES   4 B  259  ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR          
SEQRES   5 B  259  LYS LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR          
SEQRES   6 B  259  ILE ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY          
SEQRES   7 B  259  LYS LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA          
SEQRES   8 B  259  SER LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU          
SEQRES   9 B  259  PHE VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN          
SEQRES  10 B  259  VAL LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR          
SEQRES  11 B  259  PHE ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR          
SEQRES  12 B  259  GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL          
SEQRES  13 B  259  GLU SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE          
SEQRES  14 B  259  ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE          
SEQRES  15 B  259  ALA GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR          
SEQRES  16 B  259  GLY GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY          
SEQRES  17 B  259  TYR THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU          
SEQRES  18 B  259  HIS GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN          
SEQRES  19 B  259  SER ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY          
SEQRES  20 B  259  VAL 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  259  GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU          
SEQRES   2 D  259  ARG GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR          
SEQRES   3 D  259  MET LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA          
SEQRES   4 D  259  ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR          
SEQRES   5 D  259  LYS LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR          
SEQRES   6 D  259  ILE ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY          
SEQRES   7 D  259  LYS LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA          
SEQRES   8 D  259  SER LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU          
SEQRES   9 D  259  PHE VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN          
SEQRES  10 D  259  VAL LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR          
SEQRES  11 D  259  PHE ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR          
SEQRES  12 D  259  GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL          
SEQRES  13 D  259  GLU SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE          
SEQRES  14 D  259  ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE          
SEQRES  15 D  259  ALA GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR          
SEQRES  16 D  259  GLY GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY          
SEQRES  17 D  259  TYR THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU          
SEQRES  18 D  259  HIS GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN          
SEQRES  19 D  259  SER ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY          
SEQRES  20 D  259  VAL SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU              
SEQRES   1 E    7  HIS HIS ALA SER PRO ARG LYS                                  
SEQRES   1 F    7  HIS HIS ALA SER PRO ARG LYS                                  
MODRES 1QMZ TPO A  160  THR  PHOSPHORYLATION SITE                               
MODRES 1QMZ TPO C  160  THR  PHOSPHORYLATION SITE                               
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET     MG  A 383       1                                                       
HET     MG  C 383       1                                                       
HET    ATP  A 381      31                                                       
HET    ATP  C 381      31                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETSYN     ATP ATP                                                              
HETSYN     TPO TPO                                                              
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   7   MG    2(MG 2+)                                                     
FORMUL   9  ATP    2(C10 H16 N5 O13 P3)                                         
FORMUL  11  HOH   *767(H2 O1)                                                   
HELIX    1   1 PRO A   45  GLU A   57  1                                  13    
HELIX    2   2 LEU A   87  SER A   94  1                                   8    
HELIX    3   3 PRO A  100  HIS A  121  1                                  22    
HELIX    4   4 LYS A  129  GLN A  131  5                                   3    
HELIX    5   5 ASP A  145  ALA A  149  5                                   5    
HELIX    6   6 THR A  165  ARG A  169  5                                   5    
HELIX    7   7 ALA A  170  LEU A  175  1                                   6    
HELIX    8   8 THR A  182  ARG A  199  1                                  18    
HELIX    9   9 SER A  207  GLY A  220  1                                  14    
HELIX   10  10 GLY A  229  MET A  233  5                                   5    
HELIX   11  11 ASP A  247  VAL A  252  1                                   6    
HELIX   12  12 ASP A  256  LEU A  267  1                                  12    
HELIX   13  13 SER A  276  ALA A  282  1                                   7    
HELIX   14  14 HIS A  283  GLN A  287  5                                   5    
HELIX   15  15 VAL B  175  ASP B  177  5                                   3    
HELIX   16  16 TYR B  178  CYS B  193  1                                  16    
HELIX   17  17 GLY B  198  GLN B  203  5                                   6    
HELIX   18  18 THR B  207  TYR B  225  1                                  19    
HELIX   19  19 GLN B  228  MET B  246  1                                  19    
HELIX   20  20 LEU B  249  GLU B  269  1                                  21    
HELIX   21  21 GLU B  274  THR B  282  1                                   9    
HELIX   22  22 THR B  287  LEU B  302  1                                  16    
HELIX   23  23 THR B  310  LEU B  320  1                                  11    
HELIX   24  24 ASN B  326  ASP B  343  1                                  18    
HELIX   25  25 ASP B  343  LEU B  348  1                                   6    
HELIX   26  26 LEU B  351  GLY B  369  1                                  19    
HELIX   27  27 PRO B  373  GLY B  381  1                                   9    
HELIX   28  28 THR B  383  ALA B  401  1                                  19    
HELIX   29  29 PRO B  402  HIS B  404  5                                   3    
HELIX   30  30 GLN B  407  TYR B  413  1                                   7    
HELIX   31  31 LYS B  414  HIS B  419  5                                   6    
HELIX   32  32 GLY B  420  LEU B  424  5                                   5    
HELIX   33  33 PRO C   45  GLU C   57  1                                  13    
HELIX   34  34 LEU C   87  SER C   94  1                                   8    
HELIX   35  35 PRO C  100  HIS C  121  1                                  22    
HELIX   36  36 LYS C  129  GLN C  131  5                                   3    
HELIX   37  37 THR C  165  ARG C  169  5                                   5    
HELIX   38  38 ALA C  170  LEU C  175  1                                   6    
HELIX   39  39 THR C  182  ARG C  199  1                                  18    
HELIX   40  40 SER C  207  GLY C  220  1                                  14    
HELIX   41  41 GLY C  229  MET C  233  5                                   5    
HELIX   42  42 ASP C  247  VAL C  252  1                                   6    
HELIX   43  43 ASP C  256  LEU C  267  1                                  12    
HELIX   44  44 SER C  276  ALA C  282  1                                   7    
HELIX   45  45 HIS C  283  GLN C  287  5                                   5    
HELIX   46  46 VAL D  175  ASP D  177  5                                   3    
HELIX   47  47 TYR D  178  CYS D  193  1                                  16    
HELIX   48  48 GLY D  198  GLN D  203  5                                   6    
HELIX   49  49 THR D  207  TYR D  225  1                                  19    
HELIX   50  50 GLN D  228  MET D  246  1                                  19    
HELIX   51  51 LEU D  249  GLY D  251  5                                   3    
HELIX   52  52 LYS D  252  GLU D  269  1                                  18    
HELIX   53  53 GLU D  274  THR D  282  1                                   9    
HELIX   54  54 THR D  287  LEU D  302  1                                  16    
HELIX   55  55 THR D  310  LEU D  320  1                                  11    
HELIX   56  56 ASN D  326  LEU D  341  1                                  16    
HELIX   57  57 ASP D  343  LEU D  348  1                                   6    
HELIX   58  58 LEU D  351  GLY D  369  1                                  19    
HELIX   59  59 PRO D  373  GLY D  381  1                                   9    
HELIX   60  60 THR D  383  ALA D  401  1                                  19    
HELIX   61  61 PRO D  402  HIS D  404  5                                   3    
HELIX   62  62 GLN D  407  TYR D  413  1                                   7    
HELIX   63  63 LYS D  414  HIS D  419  5                                   6    
HELIX   64  64 GLY D  420  LEU D  424  5                                   5    
SHEET    1   A 5 LEU A  66  HIS A  71  0                                        
SHEET    2   A 5 LYS A  75  GLU A  81 -1  N  VAL A  79   O  LEU A  67           
SHEET    3   A 5 VAL A  29  ARG A  36 -1  N  ILE A  35   O  LEU A  76           
SHEET    4   A 5 VAL A  18  ASN A  23 -1  N  ALA A  21   O  VAL A  30           
SHEET    5   A 5 PHE A   4  LYS A   9 -1  N  GLU A   8   O  LYS A  20           
SHEET    1   B 2 LEU A 133  ILE A 135  0                                        
SHEET    2   B 2 ILE A 141  LEU A 143 -1  N  LYS A 142   O  LEU A 134           
SHEET    1   C 5 GLY C  11  GLY C  13  0                                        
SHEET    2   C 5 GLY C  16  ARG C  22 -1  N  VAL C  18   O  GLY C  11           
SHEET    3   C 5 VAL C  29  ARG C  36 -1  N  LYS C  34   O  VAL C  17           
SHEET    4   C 5 LYS C  75  GLU C  81 -1  N  PHE C  80   O  ALA C  31           
SHEET    5   C 5 LEU C  66  HIS C  71 -1  N  ILE C  70   O  TYR C  77           
SHEET    1   D 2 LEU C 133  ILE C 135  0                                        
SHEET    2   D 2 ILE C 141  LEU C 143 -1  N  LYS C 142   O  LEU C 134           
SHEET    1   E 2 PHE C   4  LYS C   9  0                                        
SHEET    2   E 2 TYR C  19  ASN C  23 -1  N  ARG C  22   O  GLN C   5           
LINK         C   TYR A 159                 N   TPO A 160     1555   1555  1.30  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.33  
LINK        MG    MG A 383                 O2G ATP A 381     1555   1555  2.25  
LINK        MG    MG A 383                 OD1 ASN A 132     1555   1555  2.00  
LINK        MG    MG A 383                 O3B ATP A 381     1555   1555  2.12  
LINK        MG    MG A 383                 O2A ATP A 381     1555   1555  2.07  
LINK        MG    MG A 383                 O   HOH A2205     1555   1555  2.14  
LINK        MG    MG A 383                 OD2 ASP A 145     1555   1555  1.91  
LINK         C   TYR C 159                 N   TPO C 160     1555   1555  1.31  
LINK         C   TPO C 160                 N   HIS C 161     1555   1555  1.33  
LINK         O3B ATP C 381                MG    MG C 383     1555   1555  1.91  
LINK         O2A ATP C 381                MG    MG C 383     1555   1555  2.02  
LINK        MG    MG C 383                 OD1 ASN C 132     1555   1555  2.12  
LINK        MG    MG C 383                 O   HOH C2195     1555   1555  2.37  
LINK        MG    MG C 383                 O2G ATP C 381     1555   1555  2.22  
LINK        MG    MG C 383                 OD2 ASP C 145     1555   1555  2.05  
SITE     1 AC1  4 ASN A 132  ASP A 145  ATP A 381  HOH A2205                    
SITE     1 AC2  4 ASN C 132  ASP C 145  ATP C 381  HOH C2195                    
SITE     1 AC3 26 ILE A  10  GLU A  12  GLY A  13  THR A  14                    
SITE     2 AC3 26 ALA A  31  LYS A  33  GLU A  81  PHE A  82                    
SITE     3 AC3 26 LEU A  83  ASP A  86  LYS A  89  LYS A 129                    
SITE     4 AC3 26 GLN A 131  ASN A 132  LEU A 134  ASP A 145                    
SITE     5 AC3 26  MG A 383  HOH A2008  HOH A2073  HOH A2094                    
SITE     6 AC3 26 HOH A2201  HOH A2202  HOH A2203  HOH A2205                    
SITE     7 AC3 26 HOH A2206  SER E   5                                          
SITE     1 AC4 24 ILE C  10  GLU C  12  GLY C  13  THR C  14                    
SITE     2 AC4 24 VAL C  18  ALA C  31  LYS C  33  GLU C  81                    
SITE     3 AC4 24 LEU C  83  ASP C  86  LYS C  89  LYS C 129                    
SITE     4 AC4 24 GLN C 131  ASN C 132  LEU C 134  ASP C 145                    
SITE     5 AC4 24  MG C 383  HOH C2091  HOH C2192  HOH C2193                    
SITE     6 AC4 24 HOH C2195  HOH C2196  HOH C2197  SER F   5                    
CRYST1  152.600  163.700   73.300  90.00  90.00  90.00 P 21 21 2     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      0.006553  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006109  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013642        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system