GenomeNet

Database: PDB
Entry: 1FQ1
LinkDB: 1FQ1
Original site: 1FQ1 
HEADER    HYDROLASE/TRANSFERASE                   01-SEP-00   1FQ1              
TITLE     CRYSTAL STRUCTURE OF KINASE ASSOCIATED PHOSPHATASE (KAP) IN COMPLEX   
TITLE    2 WITH PHOSPHO-CDK2                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE INHIBITOR 3;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.1.3.48;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CELL DIVISION PROTEIN KINASE 2;                            
COMPND   9 CHAIN: B;                                                            
COMPND  10 EC: 2.7.11.22;                                                       
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR: PGEX-6P;                                   
SOURCE   8 OTHER_DETAILS: HOMO SAPIENS;                                         
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 EXPRESSION_SYSTEM_VECTOR: PGEX-6P;                                   
SOURCE  16 OTHER_DETAILS: HOMO SAPIENS                                          
KEYWDS    PHOSPHO-PROTEIN-PROTEIN COMPLEX, HYDROLASE-TRANSFERASE COMPLEX        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.SONG,N.HANLON,N.R.BROWN,M.E.M.NOBLE,L.N.JOHNSON,D.BARFORD           
REVDAT   5   14-MAR-18 1FQ1    1       SEQADV                                   
REVDAT   4   24-FEB-09 1FQ1    1       VERSN                                    
REVDAT   3   26-AUG-08 1FQ1    1       COMPND                                   
REVDAT   2   01-APR-03 1FQ1    1       JRNL                                     
REVDAT   1   09-MAY-01 1FQ1    0                                                
JRNL        AUTH   H.SONG,N.HANLON,N.R.BROWN,M.E.NOBLE,L.N.JOHNSON,D.BARFORD    
JRNL        TITL   PHOSPHOPROTEIN-PROTEIN INTERACTIONS REVEALED BY THE CRYSTAL  
JRNL        TITL 2 STRUCTURE OF KINASE-ASSOCIATED PHOSPHATASE IN COMPLEX WITH   
JRNL        TITL 3 PHOSPHOCDK2.                                                 
JRNL        REF    MOL.CELL                      V.   7   615 2001              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   11463386                                                     
JRNL        DOI    10.1016/S1097-2765(01)00208-8                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   R.Y.C.POON,T.HUNTER                                          
REMARK   1  TITL   DEPHOSPHORYLATION OF CDK2 THR160 BY THE CYCLIN DEPENDENT     
REMARK   1  TITL 2 KINASE-INTERACTING PHOSPHATASE KAP IN THE ABSENCE OF CYCLIN  
REMARK   1  REF    SCIENCE                       V. 270    90 1995              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   J.GYRURIS,E.GOLEMIS,H.CHERTKOV,R.BRENT                       
REMARK   1  TITL   CDI1, A HUMAN G1 AND S PHASE PROTEIN PHOSPHATASE THAT        
REMARK   1  TITL 2 ASSOCIATES WITH CDK2                                         
REMARK   1  REF    CELL(CAMBRIDGE,MASS.)         V.  75   791 1993              
REMARK   1  REFN                   ISSN 0092-8674                               
REMARK   1  DOI    10.1016/0092-8674(93)90498-F                                 
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   J.W.HARPER,G.R.ADAMI,N.WEI,K.KEYOMARSI,S.J.ELLEDGE           
REMARK   1  TITL   THE P21CDK-INTERACTING PROTEIN CIP1 IS A POTENT INHIBITOR OF 
REMARK   1  TITL 2 G1 CYCLIN-DEPENDENT KINASES                                  
REMARK   1  REF    CELL(CAMBRIDGE,MASS.)         V.  75   805 1993              
REMARK   1  REFN                   ISSN 0092-8674                               
REMARK   1  DOI    10.1016/0092-8674(93)90499-G                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 13940                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.235                           
REMARK   3   FREE R VALUE                     : 0.313                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 702                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3821                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 32                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 95.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.800                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : 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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1FQ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-SEP-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000011804.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17091                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.13                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000,KCL, MGACETATE,NA CACODYLATE    
REMARK 280  , PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       43.86667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       21.93333            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       21.93333            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       43.86667            
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 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3050 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     ILE A     7                                                      
REMARK 465     GLN A     8                                                      
REMARK 465     THR A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     PHE A    12                                                      
REMARK 465     ASP A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 465     SER A    15                                                      
REMARK 465     ASP A    16                                                      
REMARK 465     GLU A    17                                                      
REMARK 465     GLU A    18                                                      
REMARK 465     PRO A    19                                                      
REMARK 465     ILE A    20                                                      
REMARK 465     ASP A   204                                                      
REMARK 465     SER A   205                                                      
REMARK 465     GLN A   206                                                      
REMARK 465     SER A   207                                                      
REMARK 465     ARG A   208                                                      
REMARK 465     SER A   209                                                      
REMARK 465     VAL A   210                                                      
REMARK 465     SER A   211                                                      
REMARK 465     ARG A   212                                                      
REMARK 465     ARG B   297                                                      
REMARK 465     LEU B   298                                                      
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 B    46     N    ALA B    48              1.94            
REMARK 500   OD1  ASP B   206     OD2  ASP B   210              2.09            
REMARK 500   O    VAL B   230     N    SER B   232              2.19            
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    ILE B  35   C     ARG B  36   N      -0.149                       
REMARK 500    THR B  47   C     ALA B  48   N      -0.193                       
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    ILE B  35   CA  -  C   -  N   ANGL. DEV. =  21.3 DEGREES          
REMARK 500    ILE B  35   O   -  C   -  N   ANGL. DEV. = -24.6 DEGREES          
REMARK 500    ALA B  48   C   -  N   -  CA  ANGL. DEV. = -27.7 DEGREES          
REMARK 500    PRO B 234   C   -  N   -  CD  ANGL. DEV. = -12.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  22     -169.16     33.07                                   
REMARK 500    GLU A  23      -38.83      9.70                                   
REMARK 500    ARG A  36        7.55    -67.36                                   
REMARK 500    LYS A  54       92.81     17.44                                   
REMARK 500    VAL A  60      -79.49    -45.71                                   
REMARK 500    GLN A  73      -72.23    -91.71                                   
REMARK 500    CYS A  79     -150.08    -87.39                                   
REMARK 500    VAL A  89       47.35   -144.65                                   
REMARK 500    GLN A  98       45.10    -85.70                                   
REMARK 500    GLU A 124      -76.05    -57.81                                   
REMARK 500    ASN A 132       40.98    -98.20                                   
REMARK 500    TYR A 133       38.16     33.05                                   
REMARK 500    SER A 140     -131.86   -134.43                                   
REMARK 500    TYR A 141      -72.19    -90.67                                   
REMARK 500    LEU A 144       -6.51   -172.09                                   
REMARK 500    SER A 177        3.86    -69.56                                   
REMARK 500    ALA A 179     -113.67    -27.98                                   
REMARK 500    THR A 182      172.19    -58.93                                   
REMARK 500    ALA A 198      -13.23    -47.66                                   
REMARK 500    HIS A 199       41.38    -89.99                                   
REMARK 500    SER A 201       70.48    -58.03                                   
REMARK 500    GLU B   2      116.80     54.23                                   
REMARK 500    ASN B   3       87.32    -49.10                                   
REMARK 500    GLU B  12       79.58   -176.67                                   
REMARK 500    THR B  14       98.91     23.03                                   
REMARK 500    TYR B  15       77.14     34.70                                   
REMARK 500    LYS B  24       18.91    -60.55                                   
REMARK 500    LEU B  25      -78.41   -127.42                                   
REMARK 500    GLU B  28       89.81     36.07                                   
REMARK 500    VAL B  29     -154.62     33.31                                   
REMARK 500    VAL B  30      137.63    133.43                                   
REMARK 500    LEU B  32      121.04    -30.92                                   
REMARK 500    LYS B  33     -158.81    -89.44                                   
REMARK 500    LYS B  34      146.67   -179.29                                   
REMARK 500    LEU B  37      -66.94   -120.62                                   
REMARK 500    ASP B  38       10.65     87.32                                   
REMARK 500    THR B  39      172.55     58.62                                   
REMARK 500    VAL B  44      161.88     68.27                                   
REMARK 500    THR B  47       -1.67    -38.59                                   
REMARK 500    ALA B  48      -57.06   -138.64                                   
REMARK 500    SER B  53      -71.96    -60.78                                   
REMARK 500    GLU B  57      -39.14    -38.01                                   
REMARK 500    ASN B  62       47.83    -73.32                                   
REMARK 500    VAL B  64      135.15    -27.07                                   
REMARK 500    THR B  72      130.85    -27.04                                   
REMARK 500    LEU B  83       52.88   -154.45                                   
REMARK 500    HIS B  84      -87.33     56.63                                   
REMARK 500    ASP B  92      -74.80    -53.64                                   
REMARK 500    ALA B  93       55.80    -57.56                                   
REMARK 500    SER B  94      -11.53   -179.28                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      86 RAMACHANDRAN OUTLIERS.                        
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 ANGLE, 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    ILE B  35         14.99                                           
REMARK 500    THR B  47        -21.96                                           
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 B 383  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B 132   OD1                                                    
REMARK 620 2 ATP B 381   O3B 108.8                                              
REMARK 620 3 ATP B 381   O2A 162.5  75.6                                        
REMARK 620 4 ATP B 381   O2G  59.1  49.7 122.4                                  
REMARK 620 5 ASN B 132   ND2  49.8 101.0 113.1  68.8                            
REMARK 620 6 ATP B 381   O1G  91.8  52.0 103.6  58.8 126.5                      
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 B 383                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 381                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FPZ   RELATED DB: PDB                                   
DBREF  1FQ1 A    1   212  UNP    Q16667   CDKN3_HUMAN      1    212             
DBREF  1FQ1 B    1   298  UNP    P24941   CDK2_HUMAN       1    298             
SEQADV 1FQ1 SER A  140  UNP  Q16667    CYS   140 ENGINEERED MUTATION            
SEQRES   1 A  212  MET LYS PRO PRO SER SER ILE GLN THR SER GLU PHE ASP          
SEQRES   2 A  212  SER SER ASP GLU GLU PRO ILE GLU ASP GLU GLN THR PRO          
SEQRES   3 A  212  ILE HIS ILE SER TRP LEU SER LEU SER ARG VAL ASN CYS          
SEQRES   4 A  212  SER GLN PHE LEU GLY LEU CYS ALA LEU PRO GLY CYS LYS          
SEQRES   5 A  212  PHE LYS ASP VAL ARG ARG ASN VAL GLN LYS ASP THR GLU          
SEQRES   6 A  212  GLU LEU LYS SER CYS GLY ILE GLN ASP ILE PHE VAL PHE          
SEQRES   7 A  212  CYS THR ARG GLY GLU LEU SER LYS TYR ARG VAL PRO ASN          
SEQRES   8 A  212  LEU LEU ASP LEU TYR GLN GLN CYS GLY ILE ILE THR HIS          
SEQRES   9 A  212  HIS HIS PRO ILE ALA ASP GLY GLY THR PRO ASP ILE ALA          
SEQRES  10 A  212  SER CYS CYS GLU ILE MET GLU GLU LEU THR THR CYS LEU          
SEQRES  11 A  212  LYS ASN TYR ARG LYS THR LEU ILE HIS SER TYR GLY GLY          
SEQRES  12 A  212  LEU GLY ARG SER CYS LEU VAL ALA ALA CYS LEU LEU LEU          
SEQRES  13 A  212  TYR LEU SER ASP THR ILE SER PRO GLU GLN ALA ILE ASP          
SEQRES  14 A  212  SER LEU ARG ASP LEU ARG GLY SER GLY ALA ILE GLN THR          
SEQRES  15 A  212  ILE LYS GLN TYR ASN TYR LEU HIS GLU PHE ARG ASP LYS          
SEQRES  16 A  212  LEU ALA ALA HIS LEU SER SER ARG ASP SER GLN SER ARG          
SEQRES  17 A  212  SER VAL SER ARG                                              
SEQRES   1 B  298  MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY          
SEQRES   2 B  298  THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR          
SEQRES   3 B  298  GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR          
SEQRES   4 B  298  GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 B  298  SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS          
SEQRES   6 B  298  LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU          
SEQRES   7 B  298  VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET          
SEQRES   8 B  298  ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE          
SEQRES   9 B  298  LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE          
SEQRES  10 B  298  CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  11 B  298  GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU          
SEQRES  12 B  298  ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL          
SEQRES  13 B  298  ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP TYR ARG          
SEQRES  14 B  298  ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR          
SEQRES  15 B  298  ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU          
SEQRES  16 B  298  MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU          
SEQRES  17 B  298  ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR          
SEQRES  18 B  298  PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO          
SEQRES  19 B  298  ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP          
SEQRES  20 B  298  PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG          
SEQRES  21 B  298  SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS          
SEQRES  22 B  298  ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE          
SEQRES  23 B  298  GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU              
MODRES 1FQ1 TPO B  160  THR  PHOSPHOTHREONINE                                   
HET    TPO  B 160      11                                                       
HET     MG  B 383       1                                                       
HET    ATP  B 381      31                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   2  TPO    C4 H10 N O6 P                                                
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  ATP    C10 H16 N5 O13 P3                                            
HELIX    1   1 SER A   35  ASN A   38  5                                   4    
HELIX    2   2 ASN A   59  GLY A   71  1                                  13    
HELIX    3   3 THR A   80  TYR A   87  1                                   8    
HELIX    4   4 ASN A   91  GLN A   98  1                                   8    
HELIX    5   5 ASP A  115  ASN A  132  1                                  18    
HELIX    6   6 GLY A  145  SER A  159  1                                  15    
HELIX    7   7 SER A  163  GLY A  176  1                                  14    
HELIX    8   8 THR A  182  ALA A  198  1                                  17    
HELIX    9   9 PRO B   45  LEU B   58  1                                  14    
HELIX   10  10 LEU B   87  ALA B   93  1                                   7    
HELIX   11  11 PRO B  100  SER B  120  1                                  21    
HELIX   12  12 LYS B  129  GLN B  131  5                                   3    
HELIX   13  13 ASP B  145  ALA B  149  5                                   5    
HELIX   14  14 ALA B  170  LEU B  175  1                                   6    
HELIX   15  15 VAL B  184  ARG B  199  1                                  16    
HELIX   16  16 SER B  207  GLY B  220  1                                  14    
HELIX   17  17 ASP B  247  VAL B  252  1                                   6    
HELIX   18  18 ASP B  258  LEU B  267  1                                  10    
HELIX   19  19 SER B  276  HIS B  283  1                                   8    
HELIX   20  20 PRO B  284  GLN B  287  5                                   4    
SHEET    1   A 5 SER A  30  SER A  33  0                                        
SHEET    2   A 5 PHE A  42  LEU A  45 -1  O  LEU A  43   N  LEU A  32           
SHEET    3   A 5 THR A 136  HIS A 139  1  O  THR A 136   N  GLY A  44           
SHEET    4   A 5 ASP A  74  VAL A  77  1  O  ASP A  74   N  LEU A 137           
SHEET    5   A 5 ILE A 102  HIS A 105  1  O  ILE A 102   N  ILE A  75           
SHEET    1   B 2 LYS B   9  GLY B  11  0                                        
SHEET    2   B 2 VAL B  18  TYR B  19 -1  N  VAL B  18   O  GLY B  11           
SHEET    1   C 3 GLN B  85  ASP B  86  0                                        
SHEET    2   C 3 LEU B 133  ILE B 135 -1  N  ILE B 135   O  GLN B  85           
SHEET    3   C 3 ILE B 141  LEU B 143 -1  N  LYS B 142   O  LEU B 134           
SHEET    1   D 2 VAL B 123  LEU B 124  0                                        
SHEET    2   D 2 ARG B 150  ALA B 151 -1  O  ARG B 150   N  LEU B 124           
LINK         C   TYR B 159                 N   TPO B 160     1555   1555  1.33  
LINK         C   TPO B 160                 N   HIS B 161     1555   1555  1.33  
LINK        MG    MG B 383                 OD1 ASN B 132     1555   1555  2.71  
LINK        MG    MG B 383                 O3B ATP B 381     1555   1555  2.99  
LINK        MG    MG B 383                 O2A ATP B 381     1555   1555  2.58  
LINK        MG    MG B 383                 O2G ATP B 381     1555   1555  2.61  
LINK        MG    MG B 383                 ND2 ASN B 132     1555   1555  2.58  
LINK        MG    MG B 383                 O1G ATP B 381     1555   1555  2.48  
SITE     1 AC1  3 ASN B 132  ASP B 145  ATP B 381                               
SITE     1 AC2 17 ILE B  10  GLY B  13  THR B  14  VAL B  18                    
SITE     2 AC2 17 ALA B  31  LYS B  33  GLU B  81  PHE B  82                    
SITE     3 AC2 17 LEU B  83  ASP B  86  LYS B  89  ASP B 127                    
SITE     4 AC2 17 LYS B 129  GLN B 131  ASN B 132  ASP B 145                    
SITE     5 AC2 17  MG B 383                                                     
CRYST1  134.450  134.450   65.800  90.00  90.00 120.00 P 32 2 1      6          
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      0.007438  0.004294  0.000000        0.00000                         
SCALE2      0.000000  0.008588  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015198        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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