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Database: PDB
Entry: 1URC
LinkDB: 1URC
Original site: 1URC 
HEADER    TRANSFERASE/INHIBITOR                   28-OCT-03   1URC              
TITLE     CYCLIN A BINDING GROOVE INHIBITOR ACE-ARG-LYS-LEU-PHE-GLY             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION PROTEIN KINASE 2;                            
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: P33 PROTEIN KINASE, CDK2, CYCLIN-DEPENDENT KINASE-2;        
COMPND   5 EC: 2.7.1.37, 2.7.11.22;                                             
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CYCLIN A2;                                                 
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: RESIDUES 173 - 432;                                        
COMPND  11 SYNONYM: CYCLIN A, CCNA2, CCNA, CCN1;                                
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: PEPTIDE INHIBITOR;                                         
COMPND  15 CHAIN: E, F;                                                         
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 OTHER_DETAILS: CYCLIN GROOVE-BOUND CYCLIC(2-5) PENTAPEPTIDE ACE-ARG- 
COMPND  18 LYS-LEU-PHE-GLY                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 MOL_ID: 3;                                                           
SOURCE  15 SYNTHETIC: YES;                                                      
SOURCE  16 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  17 ORGANISM_TAXID: 32630;                                               
SOURCE  18 OTHER_DETAILS: CYCLIN GROOVE-BOUND CYCLIC(2-5) PENTAPEPTIDE AC-ARG-  
SOURCE  19 LYS-LEU-PHE-GLY                                                      
KEYWDS    TRANSFERASE-INHIBITOR COMPLEX, INHIBITOR, LIGAND EXCHANGE, DRUG       
KEYWDS   2 DESIGN, PEPTIDOMIMETICS                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.KONTOPIDIS,M.ANDREWS,C.MCINNES,A.COWAN,H.POWERS,L.INNES,A.PLATER,   
AUTHOR   2 G.GRIFFITHS,D.PATERSON,D.ZHELEVA,D.LANE,S.GREEN,M.WALKINSHAW,        
AUTHOR   3 P.FISCHER                                                            
REVDAT   5   09-OCT-19 1URC    1       REMARK LINK                              
REVDAT   4   07-MAR-18 1URC    1       SOURCE JRNL   ATOM                       
REVDAT   3   04-SEP-13 1URC    1       HEADER TITLE  COMPND SOURCE              
REVDAT   3 2                   1       KEYWDS AUTHOR JRNL   REMARK              
REVDAT   3 3                   1       VERSN  FORMUL LINK   SITE                
REVDAT   3 4                   1       CRYST1 SCALE3 CONECT MASTER              
REVDAT   2   24-FEB-09 1URC    1       VERSN                                    
REVDAT   1   31-OCT-03 1URC    0                                                
JRNL        AUTH   M.J.ANDREWS,C.MCINNES,G.KONTOPIDIS,L.INNES,A.COWAN,A.PLATER, 
JRNL        AUTH 2 P.M.FISCHER                                                  
JRNL        TITL   DESIGN, SYNTHESIS, BIOLOGICAL ACTIVITY AND STRUCTURAL        
JRNL        TITL 2 ANALYSIS OF CYCLIC PEPTIDE INHIBITORS TARGETING THE          
JRNL        TITL 3 SUBSTRATE RECRUITMENT SITE OF CYCLIN-DEPENDENT KINASE        
JRNL        TITL 4 COMPLEXES.                                                   
JRNL        REF    ORG. BIOMOL. CHEM.            V.   2  2735 2004              
JRNL        REFN                   ISSN 1477-0520                               
JRNL        PMID   15455144                                                     
JRNL        DOI    10.1039/B409157D                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 14.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 39372                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1272                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9016                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 338                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.90000                                             
REMARK   3    B22 (A**2) : -0.69000                                             
REMARK   3    B33 (A**2) : 3.58000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 1.013         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.327         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.250         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.153        
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1URC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-OCT-03.                  
REMARK 100 THE DEPOSITION ID IS D_1290013838.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-OCT-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.80                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX14.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.488                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39765                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 17.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 14.20                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.62000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1FIN                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG 3350, 0.1M NA3-CIT, PH 7.80      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       36.81500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       77.73000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.75500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       77.73000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.81500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.75500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4230 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.1 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.5 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 CYCLIN CONTROLS THE CELL CYCLE AT THE G1/S                           
REMARK 400   (START) AND THE G2/M (MITOSIS) TRANSITIONS.                        
REMARK 400  KINASE INTERACTS WITH CYCLINS A, D, OR E.                           
REMARK 400   ACTIVITY OF CDK2 IS MAXIMAL DURING S PHASE AND G2.                 
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     ASN B   173                                                      
REMARK 465     GLU B   174                                                      
REMARK 465     LEU C   298                                                      
REMARK 465     ASN D   173                                                      
REMARK 465     GLU D   174                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LEU B 432    O                                                   
REMARK 470     ARG C 297    CA   C    O    CB   CG   CD   NE                    
REMARK 470     ARG C 297    CZ   NH1  NH2                                       
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   NZ   LYS E   502     C    GLY E   505              1.33            
REMARK 500   NZ   LYS F   503     C    GLY F   506              1.33            
REMARK 500   O    HOH D  2050     O    HOH D  2051              1.74            
REMARK 500   CG2  VAL B   175     CD   PRO B   176              1.79            
REMARK 500   ND2  ASN B   415     O    HOH B  2069              1.91            
REMARK 500   OD1  ASP A    38     CG   GLU A    40              1.96            
REMARK 500   O    HOH B  2068     O    HOH B  2069              1.97            
REMARK 500   CB   TYR C    15     O    HOH C  2009              1.99            
REMARK 500   O    THR C    41     N    GLY C    43              2.06            
REMARK 500   NZ   LYS C   278     O    ASP D   177              2.10            
REMARK 500   O    HOH D  2001     O    HOH D  2011              2.11            
REMARK 500   CE1  HIS D   361     O    HOH D  2069              2.14            
REMARK 500   OG1  THR C   182     OH   TYR D   178              2.16            
REMARK 500   ND1  HIS D   361     O    HOH D  2069              2.18            
REMARK 500   NZ   LYS C     6     NZ   LYS C    34              2.19            
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   CG   ASN B   431     OD1  ASP C   210     2664     1.25            
REMARK 500   ND2  ASN B   431     OD1  ASP C   210     2664     1.46            
REMARK 500   OE2  GLU B   428     NZ   LYS C   237     2664     1.65            
REMARK 500   O    GLY B   369     NE   ARG C   217     2664     1.75            
REMARK 500   CB   ASN B   431     OD1  ASP C   210     2664     1.93            
REMARK 500   ND2  ASN B   431     CA   ASP C   210     2664     1.97            
REMARK 500   ND2  ASN B   431     CG   ASP C   210     2664     2.06            
REMARK 500   OD1  ASN B   431     OD1  ASP C   210     2664     2.07            
REMARK 500   ND1  HIS A    84     O    GLN C   287     1455     2.15            
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    TYR A  15   CB  -  CA  -  C   ANGL. DEV. = -14.1 DEGREES          
REMARK 500    ASP A  38   CB  -  CG  -  OD2 ANGL. DEV. =   8.6 DEGREES          
REMARK 500    THR A  39   N   -  CA  -  C   ANGL. DEV. = -21.3 DEGREES          
REMARK 500    ARG A 122   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ASP A 235   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP A 247   CB  -  CG  -  OD2 ANGL. DEV. =   8.1 DEGREES          
REMARK 500    ASP A 256   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    PRO B 176   C   -  N   -  CA  ANGL. DEV. =  12.3 DEGREES          
REMARK 500    ASP B 205   CB  -  CG  -  OD2 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ASP B 240   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP B 284   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASP B 345   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP C  38   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    VAL C 164   CB  -  CA  -  C   ANGL. DEV. = -13.3 DEGREES          
REMARK 500    LEU C 166   CA  -  CB  -  CG  ANGL. DEV. =  16.8 DEGREES          
REMARK 500    ASP C 210   CB  -  CG  -  OD2 ANGL. DEV. =   8.1 DEGREES          
REMARK 500    ASP C 247   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP C 256   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP C 258   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    VAL D 175   CB  -  CA  -  C   ANGL. DEV. = -12.6 DEGREES          
REMARK 500    ASP D 205   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP D 216   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP D 343   CB  -  CG  -  OD2 ANGL. DEV. =   8.6 DEGREES          
REMARK 500    ASP D 393   CB  -  CG  -  OD2 ANGL. DEV. =   7.8 DEGREES          
REMARK 500    ARG E 501   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 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    GLU A   2      -55.65    -16.19                                   
REMARK 500    GLU A  12     -119.85   -135.39                                   
REMARK 500    THR A  14      172.01     56.62                                   
REMARK 500    GLU A  40      -28.49    178.77                                   
REMARK 500    THR A  41      -34.09   -149.89                                   
REMARK 500    LEU A  96      -44.15     99.00                                   
REMARK 500    ARG A 126      -13.05     87.01                                   
REMARK 500    ASP A 127       44.90   -142.52                                   
REMARK 500    ASP A 145       83.89     55.15                                   
REMARK 500    PHE A 146       32.32    -97.60                                   
REMARK 500    THR A 160      -64.70     -1.82                                   
REMARK 500    HIS A 161       39.03   -141.10                                   
REMARK 500    GLU A 162     -126.17    -18.96                                   
REMARK 500    VAL A 164     -160.23    -65.24                                   
REMARK 500    LEU A 166     -148.21    -81.24                                   
REMARK 500    TRP A 167      -57.20     76.94                                   
REMARK 500    ARG A 199       -5.35     82.23                                   
REMARK 500    TRP A 227       74.03   -159.92                                   
REMARK 500    ASP A 256     -169.94    -79.23                                   
REMARK 500    THR A 290     -164.10   -122.97                                   
REMARK 500    PRO B 176       -8.18    -22.98                                   
REMARK 500    ASP B 283       41.33     76.20                                   
REMARK 500    ALA B 307       59.36    -99.48                                   
REMARK 500    GLN B 370     -178.45    -67.99                                   
REMARK 500    LEU B 424      166.05    -28.38                                   
REMARK 500    GLU C   2      -39.92    -28.30                                   
REMARK 500    TYR C  15      -65.72   -130.11                                   
REMARK 500    ASP C  38      -51.37    -11.76                                   
REMARK 500    GLU C  40      129.39     73.59                                   
REMARK 500    THR C  41     -155.43     23.30                                   
REMARK 500    GLU C  42      -17.72     15.07                                   
REMARK 500    LEU C  96      -51.17     96.78                                   
REMARK 500    ARG C 126       -8.55     79.16                                   
REMARK 500    ASP C 145       71.56     67.82                                   
REMARK 500    PHE C 146       30.22    -90.12                                   
REMARK 500    THR C 160      -75.06    -29.41                                   
REMARK 500    GLU C 162     -168.69    -52.20                                   
REMARK 500    VAL C 164      173.83    -47.68                                   
REMARK 500    LYS C 242       76.91   -113.56                                   
REMARK 500    THR C 290     -155.46   -125.57                                   
REMARK 500    PRO D 176      155.57    -11.02                                   
REMARK 500    ASP D 177       21.07    -73.76                                   
REMARK 500    PRO D 195      152.84    -41.64                                   
REMARK 500    THR D 303       52.59     36.93                                   
REMARK 500    GLN D 323       97.91   -164.92                                   
REMARK 500    TRP D 372      106.39    -22.44                                   
REMARK 500    LEU D 424      178.35    -50.58                                   
REMARK 500    PRO D 426      155.98    -47.29                                   
REMARK 500    ASN D 431       31.54     82.92                                   
REMARK 500    PHE E 504      -70.87     72.86                                   
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 MET A    1     GLU A    2                  141.41                    
REMARK 500 ASP A   38     THR A   39                  -93.10                    
REMARK 500 THR A   39     GLU A   40                 -118.93                    
REMARK 500 THR A  160     HIS A  161                 -141.64                    
REMARK 500 HIS A  161     GLU A  162                 -113.06                    
REMARK 500 GLU A  162     VAL A  163                  126.66                    
REMARK 500 VAL A  163     VAL A  164                 -141.92                    
REMARK 500 GLN B  323     PRO B  324                  123.89                    
REMARK 500 ASP C   38     THR C   39                 -130.43                    
REMARK 500 GLU C   40     THR C   41                  104.34                    
REMARK 500 ILE C   70     HIS C   71                 -142.82                    
REMARK 500 HIS C  161     GLU C  162                 -130.43                    
REMARK 500 GLU C  162     VAL C  163                  138.66                    
REMARK 500 VAL C  164     THR C  165                   44.79                    
REMARK 500 LYS D  194     PRO D  195                  147.79                    
REMARK 500 ASP D  345     PRO D  346                  134.36                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN E OF PEPTIDE INHIBITOR      
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN F OF PEPTIDE INHIBITOR      
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AQ1   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR         
REMARK 900 STAUROSPORINE                                                        
REMARK 900 RELATED ID: 1B38   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2                                      
REMARK 900 RELATED ID: 1B39   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2 PHOSPHORYLATED ON THR 160            
REMARK 900 RELATED ID: 1BUH   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CDK2 KINASE COMPLEX WITHCELL CYCLE-   
REMARK 900 REGULATORY PROTEIN CKSHS1                                            
REMARK 900 RELATED ID: 1CKP   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR         
REMARK 900 PURVALANOL B                                                         
REMARK 900 RELATED ID: 1DI8   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) IN COMPLEX WITH 4- 
REMARK 900 [3- HYDROXYANILINO]-6,7-DIMETHOXYQUINAZOLINE                         
REMARK 900 RELATED ID: 1DM2   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR         
REMARK 900 HYMENIALDISINE                                                       
REMARK 900 RELATED ID: 1E1V   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR NU2058  
REMARK 900 RELATED ID: 1E1X   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR NU6027  
REMARK 900 RELATED ID: 1E9H   RELATED DB: PDB                                   
REMARK 900 THR 160 PHOSPHORYLATED CDK2 - HUMAN CYCLIN A3 COMPLEX WITH THE       
REMARK 900 INHIBITOR INDIRUBIN-5- SULPHONATE BOUND                              
REMARK 900 RELATED ID: 1F5Q   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MURINE GAMMA HERPESVIRUS CYCLIN COMPLEXED TO    
REMARK 900 HUMAN CYCLIN DEPENDANT KINASE 2                                      
REMARK 900 RELATED ID: 1FIN   RELATED DB: PDB                                   
REMARK 900 CYCLIN A - CYCLIN-DEPENDENT KINASE 2 COMPLEX                         
REMARK 900 RELATED ID: 1FQ1   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF KINASE ASSOCIATED PHOSPHATASE (KAP) INCOMPLEX   
REMARK 900 WITH PHOSPHO-CDK2                                                    
REMARK 900 RELATED ID: 1FVT   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) INCOMPLEX WITH AN  
REMARK 900 OXINDOLE INHIBITOR                                                   
REMARK 900 RELATED ID: 1FVV   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CDK2/CYCLIN A IN COMPLEX WITH AN OXINDOLEINHIBITOR  
REMARK 900 RELATED ID: 1G5S   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLIN DEPENDENT KINASE 2 (CDK2)IN        
REMARK 900 COMPLEX WITH THE INHIBITOR H717                                      
REMARK 900 RELATED ID: 1GIH   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE CDK4INHIBITOR     
REMARK 900 RELATED ID: 1GII   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE CDK4INHIBITOR     
REMARK 900 RELATED ID: 1GIJ   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE CDK4INHIBITOR     
REMARK 900 RELATED ID: 1GY3   RELATED DB: PDB                                   
REMARK 900 PCDK2/CYCLIN A IN COMPLEX WITH MGADP, NITRATE AND PEPTIDE SUBSTRATE  
REMARK 900 RELATED ID: 1GZ8   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR 2-      
REMARK 900 AMINO-6-(3'-METHYL- 2'-OXO)BUTOXYPURINE                              
REMARK 900 RELATED ID: 1H00   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6 -BIS ANILINO PYRIMIDINE    
REMARK 900 CDK4 INHIBITOR                                                       
REMARK 900 RELATED ID: 1H01   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 2, 4 -BIS ANILINO PYRIMIDINE    
REMARK 900 CDK4 INHIBITOR                                                       
REMARK 900 RELATED ID: 1H06   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6 -BIS ANILINO PYRIMIDINE    
REMARK 900 CDK4 INHIBITOR                                                       
REMARK 900 RELATED ID: 1H07   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6 -BIS ANILINO PYRIMIDINE    
REMARK 900 CDK4 INHIBITOR                                                       
REMARK 900 RELATED ID: 1H08   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 2, 4 -BIS ANILINO PYRIMIDINE    
REMARK 900 CDK4 INHIBITOR                                                       
REMARK 900 RELATED ID: 1H0U   RELATED DB: PDB                                   
REMARK 900 M. SMEGMATIS ARYLAMINE N-ACETYL TRANSFERASE                          
REMARK 900 RELATED ID: 1H0V   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN COMPLEX WITH THE          
REMARK 900 INHIBITOR 2-AMINO-6-[(R )-PYRROLIDINO-5'-YL]METHOXYPURINE            
REMARK 900 RELATED ID: 1H0W   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN COMPLEX WITH THE          
REMARK 900 INHIBITOR 2-AMINO-6-[ CYCLOHEX-3-ENYL]METHOXYPURINE                  
REMARK 900 RELATED ID: 1H1P   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH THE  
REMARK 900 INHIBITOR NU2058                                                     
REMARK 900 RELATED ID: 1H1Q   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH THE  
REMARK 900 INHIBITOR NU6094                                                     
REMARK 900 RELATED ID: 1H1R   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH THE  
REMARK 900 INHIBITOR NU6086                                                     
REMARK 900 RELATED ID: 1H1S   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH THE  
REMARK 900 INHIBITOR NU6102                                                     
REMARK 900 RELATED ID: 1H24   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH A 9 RESIDUE RECRUITMENT PEPTIDE FROM    
REMARK 900 E2F                                                                  
REMARK 900 RELATED ID: 1H25   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM  
REMARK 900 E2F                                                                  
REMARK 900 RELATED ID: 1H26   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM  
REMARK 900 P53                                                                  
REMARK 900 RELATED ID: 1H27   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM  
REMARK 900 P27                                                                  
REMARK 900 RELATED ID: 1H28   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM  
REMARK 900 P107                                                                 
REMARK 900 RELATED ID: 1HCK   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2                                      
REMARK 900 RELATED ID: 1HCL   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2                                      
REMARK 900 RELATED ID: 1JST   RELATED DB: PDB                                   
REMARK 900 PHOSPHORYLATED CYCLIN-DEPENDENT KINASE-2 BOUND TO CYCLIN A           
REMARK 900 RELATED ID: 1JSU   RELATED DB: PDB                                   
REMARK 900 P27(KIP1)/CYCLIN A/CDK2 COMPLEX                                      
REMARK 900 RELATED ID: 1JSV   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) INCOMPLEX WITH 4-  
REMARK 900 [(6-AMINO-4- PYRIMIDINYL)AMINO]BENZENESULFONAMIDE                    
REMARK 900 RELATED ID: 1JVP   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CDK2 ( UNPHOSPHORYLATED) INCOMPLEX WITH   
REMARK 900 PKF049-365                                                           
REMARK 900 RELATED ID: 1KE5   RELATED DB: PDB                                   
REMARK 900 CDK2 COMPLEXED WITH N-METHYL-4-{[(2-OXO- 1,2-DIHYDRO-3H-INDOL-3-     
REMARK 900 YLIDENE)METHYL] AMINO}BENZENESULFONAMIDE                             
REMARK 900 RELATED ID: 1KE6   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH N-METHYL-{4-[2-(7-   
REMARK 900 OXO-6,7-DIHYDRO -8H-[1,3]THIAZOLO[5,4-E]INDOL-8- YLIDENE)HYDRAZINO]  
REMARK 900 PHENYL}METHANESULFONAMIDE                                            
REMARK 900 RELATED ID: 1KE7   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 3-{[(2,2-DIOXIDO-1,  
REMARK 900 3-DIHYDRO-2- BENZOTHIEN-5-YL)AMINO]METHYLENE}-5-(1,3- OXAZOL-5-YL)-  
REMARK 900 1,3-DIHYDRO-2H-INDOL-2- ONE                                          
REMARK 900 RELATED ID: 1KE8   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 4-{[(2-OXO-1,2-      
REMARK 900 DIHYDRO-3H-INDOL-3 -YLIDENE)METHYL]AMINO}-N-(1,3-THIAZOL-2- YL)      
REMARK 900 BENZENESULFONAMIDE                                                   
REMARK 900 RELATED ID: 1KE9   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 3-{[4-({             
REMARK 900 [AMINO(IMINO)METHYL] AMINOSULFONYL)ANILINO]METHYLENE}-2-OXO-2,3-     
REMARK 900 DIHYDRO-1H-INDOLE                                                    
REMARK 900 RELATED ID: 1OGU   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH A 2- 
REMARK 900 ARYLAMINO-4- CYCLOHEXYLMETHYL-5-NITROSO-6-AMINOPYRIMIDINE INHIBITOR  
REMARK 900 RELATED ID: 1OI9   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH A 6- 
REMARK 900 CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR                       
REMARK 900 RELATED ID: 1OIQ   RELATED DB: PDB                                   
REMARK 900 IMIDAZOPYRIDINES: A POTENT AND SELECTIVE CLASS OF CYCLIN-DEPENDENT   
REMARK 900 KINASE INHIBITORS IDENTIFIED THROUGH STRUCTURE-BASED HYBRIDISATION   
REMARK 900 RELATED ID: 1OIR   RELATED DB: PDB                                   
REMARK 900 IMIDAZOPYRIDINES: A POTENT AND SELECTIVE CLASS OF CYCLIN-DEPENDENT   
REMARK 900 KINASE INHIBITORS IDENTIFIED THROUGH STRUCTURE-BASED HYBRIDISATION   
REMARK 900 RELATED ID: 1OIT   RELATED DB: PDB                                   
REMARK 900 IMIDAZOPYRIDINES: A POTENT AND SELECTIVE CLASS OF CYCLIN-DEPENDENT   
REMARK 900 KINASE INHIBITORS IDENTIFIED THROUGH STRUCTURE-BASED HYBRIDISATION   
REMARK 900 RELATED ID: 1OIU   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH A 6- 
REMARK 900 CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR                       
REMARK 900 RELATED ID: 1OIY   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH A 6- 
REMARK 900 CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR                       
REMARK 900 RELATED ID: 1OKU   RELATED DB: PDB                                   
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-ALA- ALA-ABU-ARG-ER-LEU-ILE-(P-  
REMARK 900 F-PHE)-NH2                                                           
REMARK 900 RELATED ID: 1OKV   RELATED DB: PDB                                   
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-ARG- ARG-LEU-ILE-PHE-NH2         
REMARK 900 RELATED ID: 1OKW   RELATED DB: PDB                                   
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR AC-ARG- ARG-LEU-ASN-(M-CL-PHE)-NH2 
REMARK 900 RELATED ID: 1OL1   RELATED DB: PDB                                   
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-CIT- CIT-LEU-ILE-(P-F-PHE)-NH2   
REMARK 900 RELATED ID: 1OL2   RELATED DB: PDB                                   
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-ARG- ARG-LEU-ASN-(P-F-PHE)-NH2   
REMARK 900 RELATED ID: 1P2A   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN DEPENDENT KINASE 2 (CKD2) WITH               
REMARK 900 ATRISUBSTITUTED NAPHTHOSTYRIL INHIBITOR                              
REMARK 900 RELATED ID: 1P5E   RELATED DB: PDB                                   
REMARK 900 THE STRUCURE OF PHOSPHO-CDK2/CYCLIN A IN COMPLEX WITH THEINHIBITOR   
REMARK 900 4,5,6,7- TETRABROMOBENZOTRIAZOLE (TBS)                               
REMARK 900 RELATED ID: 1PKD   RELATED DB: PDB                                   
REMARK 900 THE CRYSTAL STRUCTURE OF UCN-01 IN COMPLEX WITH PHOSPHO-CDK2/CYCLIN  
REMARK 900 A                                                                    
REMARK 900 RELATED ID: 1QMZ   RELATED DB: PDB                                   
REMARK 900 PHOSPHORYLATED CDK2-CYCLYIN A-SUBSTRATE PEPTIDE COMPLEX              
DBREF  1URC A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  1URC B  173   432  UNP    P20248   CGA2_HUMAN     173    432             
DBREF  1URC C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  1URC D  173   432  UNP    P20248   CGA2_HUMAN     173    432             
DBREF  1URC E  500   505  PDB    1URC     1URC           500    505             
DBREF  1URC F  501   506  PDB    1URC     1URC           501    506             
SEQRES   1 A  298  MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY          
SEQRES   2 A  298  THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR          
SEQRES   3 A  298  GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR          
SEQRES   4 A  298  GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 A  298  SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS          
SEQRES   6 A  298  LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU          
SEQRES   7 A  298  VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET          
SEQRES   8 A  298  ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE          
SEQRES   9 A  298  LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE          
SEQRES  10 A  298  CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  11 A  298  GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU          
SEQRES  12 A  298  ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL          
SEQRES  13 A  298  ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP TYR ARG          
SEQRES  14 A  298  ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR          
SEQRES  15 A  298  ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU          
SEQRES  16 A  298  MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU          
SEQRES  17 A  298  ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR          
SEQRES  18 A  298  PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO          
SEQRES  19 A  298  ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP          
SEQRES  20 A  298  PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG          
SEQRES  21 A  298  SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS          
SEQRES  22 A  298  ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE          
SEQRES  23 A  298  GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU              
SEQRES   1 B  260  ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR          
SEQRES   2 B  260  LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY          
SEQRES   3 B  260  TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG          
SEQRES   4 B  260  ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU          
SEQRES   5 B  260  TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN          
SEQRES   6 B  260  TYR ILE ASP ARG PHE LEU SER SER MET SER VAL LEU ARG          
SEQRES   7 B  260  GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU          
SEQRES   8 B  260  ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA          
SEQRES   9 B  260  GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS          
SEQRES  10 B  260  GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU          
SEQRES  11 B  260  THR PHE ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU          
SEQRES  12 B  260  THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS          
SEQRES  13 B  260  VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU          
SEQRES  14 B  260  ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL          
SEQRES  15 B  260  ILE ALA GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL          
SEQRES  16 B  260  THR GLY GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR          
SEQRES  17 B  260  GLY TYR THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP          
SEQRES  18 B  260  LEU HIS GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN          
SEQRES  19 B  260  GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS          
SEQRES  20 B  260  GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU          
SEQRES   1 C  298  MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY          
SEQRES   2 C  298  THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR          
SEQRES   3 C  298  GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR          
SEQRES   4 C  298  GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 C  298  SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS          
SEQRES   6 C  298  LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU          
SEQRES   7 C  298  VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET          
SEQRES   8 C  298  ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE          
SEQRES   9 C  298  LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE          
SEQRES  10 C  298  CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  11 C  298  GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU          
SEQRES  12 C  298  ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL          
SEQRES  13 C  298  ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP TYR ARG          
SEQRES  14 C  298  ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR          
SEQRES  15 C  298  ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU          
SEQRES  16 C  298  MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU          
SEQRES  17 C  298  ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR          
SEQRES  18 C  298  PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO          
SEQRES  19 C  298  ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP          
SEQRES  20 C  298  PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG          
SEQRES  21 C  298  SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS          
SEQRES  22 C  298  ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE          
SEQRES  23 C  298  GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU              
SEQRES   1 D  260  ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR          
SEQRES   2 D  260  LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY          
SEQRES   3 D  260  TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG          
SEQRES   4 D  260  ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU          
SEQRES   5 D  260  TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN          
SEQRES   6 D  260  TYR ILE ASP ARG PHE LEU SER SER MET SER VAL LEU ARG          
SEQRES   7 D  260  GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU          
SEQRES   8 D  260  ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA          
SEQRES   9 D  260  GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS          
SEQRES  10 D  260  GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU          
SEQRES  11 D  260  THR PHE ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU          
SEQRES  12 D  260  THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS          
SEQRES  13 D  260  VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU          
SEQRES  14 D  260  ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL          
SEQRES  15 D  260  ILE ALA GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL          
SEQRES  16 D  260  THR GLY GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR          
SEQRES  17 D  260  GLY TYR THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP          
SEQRES  18 D  260  LEU HIS GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN          
SEQRES  19 D  260  GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS          
SEQRES  20 D  260  GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU          
SEQRES   1 E    6  ACE ARG LYS LEU PHE GLY                                      
SEQRES   1 F    6  ACE ARG LYS LEU PHE GLY                                      
HET    ACE  E 500       3                                                       
HET    ACE  F 501       3                                                       
HETNAM     ACE ACETYL GROUP                                                     
FORMUL   5  ACE    2(C2 H4 O)                                                   
FORMUL   7  HOH   *338(H2 O)                                                    
HELIX    1   1 PRO A   45  LEU A   58  1                                  14    
HELIX    2   2 LEU A   87  SER A   94  1                                   8    
HELIX    3   3 PRO A  100  SER A  120  1                                  21    
HELIX    4   4 LYS A  129  GLN A  131  5                                   3    
HELIX    5   5 ALA A  170  LEU A  175  1                                   6    
HELIX    6   6 THR A  182  ARG A  199  1                                  18    
HELIX    7   7 SER A  207  GLY A  220  1                                  14    
HELIX    8   8 GLY A  229  MET A  233  5                                   5    
HELIX    9   9 ASP A  247  VAL A  252  1                                   6    
HELIX   10  10 ASP A  256  LEU A  267  1                                  12    
HELIX   11  11 SER A  276  LEU A  281  1                                   6    
HELIX   12  12 ALA A  282  GLN A  287  5                                   6    
HELIX   13  13 TYR B  178  CYS B  193  1                                  16    
HELIX   14  14 GLY B  198  GLN B  203  1                                   6    
HELIX   15  15 THR B  207  TYR B  225  1                                  19    
HELIX   16  16 GLN B  228  MET B  246  1                                  19    
HELIX   17  17 LEU B  249  GLU B  269  1                                  21    
HELIX   18  18 GLU B  274  ILE B  281  1                                   8    
HELIX   19  19 THR B  287  THR B  303  1                                  17    
HELIX   20  20 THR B  310  LEU B  320  1                                  11    
HELIX   21  21 ASN B  326  ASP B  343  1                                  18    
HELIX   22  22 ASP B  343  LEU B  348  1                                   6    
HELIX   23  23 LEU B  351  GLY B  369  1                                  19    
HELIX   24  24 PRO B  373  GLY B  381  1                                   9    
HELIX   25  25 LEU B  384  SER B  386  5                                   3    
HELIX   26  26 LEU B  387  ALA B  401  1                                  15    
HELIX   27  27 PRO B  402  HIS B  404  5                                   3    
HELIX   28  28 GLN B  407  TYR B  413  1                                   7    
HELIX   29  29 ASN B  415  HIS B  419  5                                   5    
HELIX   30  30 PRO C   45  LEU C   58  1                                  14    
HELIX   31  31 LEU C   87  ALA C   93  1                                   7    
HELIX   32  32 PRO C  100  HIS C  121  1                                  22    
HELIX   33  33 LYS C  129  GLN C  131  5                                   3    
HELIX   34  34 ALA C  170  LEU C  175  1                                   6    
HELIX   35  35 THR C  182  ARG C  199  1                                  18    
HELIX   36  36 SER C  207  GLY C  220  1                                  14    
HELIX   37  37 GLY C  229  MET C  233  5                                   5    
HELIX   38  38 ASP C  247  VAL C  252  1                                   6    
HELIX   39  39 ASP C  256  LEU C  267  1                                  12    
HELIX   40  40 SER C  276  ALA C  282  1                                   7    
HELIX   41  41 HIS C  283  VAL C  289  5                                   7    
HELIX   42  42 TYR D  178  CYS D  193  1                                  16    
HELIX   43  43 LYS D  196  GLN D  203  5                                   8    
HELIX   44  44 THR D  207  TYR D  225  1                                  19    
HELIX   45  45 GLN D  228  MET D  246  1                                  19    
HELIX   46  46 LEU D  249  GLU D  269  1                                  21    
HELIX   47  47 GLU D  274  ILE D  281  1                                   8    
HELIX   48  48 THR D  287  LEU D  302  1                                  16    
HELIX   49  49 THR D  310  PHE D  319  1                                  10    
HELIX   50  50 LEU D  320  GLN D  322  5                                   3    
HELIX   51  51 ASN D  326  ILE D  342  1                                  17    
HELIX   52  52 ASP D  343  LEU D  348  1                                   6    
HELIX   53  53 LEU D  351  THR D  368  1                                  18    
HELIX   54  54 PRO D  373  GLY D  381  1                                   9    
HELIX   55  55 LEU D  387  ALA D  401  1                                  15    
HELIX   56  56 GLN D  407  LYS D  414  1                                   8    
HELIX   57  57 ASN D  415  HIS D  419  5                                   5    
SHEET    1  AA 5 PHE A   4  GLY A  11  0                                        
SHEET    2  AA 5 VAL A  17  ASN A  23 -1  O  VAL A  18   N  ILE A  10           
SHEET    3  AA 5 VAL A  29  ARG A  36 -1  O  VAL A  30   N  ALA A  21           
SHEET    4  AA 5 LYS A  75  GLU A  81 -1  O  LEU A  76   N  ILE A  35           
SHEET    5  AA 5 LEU A  66  HIS A  71 -1  N  LEU A  67   O  VAL A  79           
SHEET    1  AB 3 GLN A  85  ASP A  86  0                                        
SHEET    2  AB 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3  AB 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1  AC 2 VAL A 123  LEU A 124  0                                        
SHEET    2  AC 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SHEET    1  CA 5 PHE C   4  GLU C  12  0                                        
SHEET    2  CA 5 VAL C  17  ASN C  23 -1  O  VAL C  18   N  ILE C  10           
SHEET    3  CA 5 VAL C  29  ARG C  36 -1  O  VAL C  30   N  ALA C  21           
SHEET    4  CA 5 LYS C  75  GLU C  81 -1  O  LEU C  76   N  ILE C  35           
SHEET    5  CA 5 LEU C  66  HIS C  71 -1  N  LEU C  67   O  VAL C  79           
SHEET    1  CB 3 GLN C  85  ASP C  86  0                                        
SHEET    2  CB 3 LEU C 133  ILE C 135 -1  O  ILE C 135   N  GLN C  85           
SHEET    3  CB 3 ILE C 141  LEU C 143 -1  O  LYS C 142   N  LEU C 134           
SHEET    1  CC 2 VAL C 123  LEU C 124  0                                        
SHEET    2  CC 2 ARG C 150  ALA C 151 -1  O  ARG C 150   N  LEU C 124           
LINK         C   ACE E 500                 N   ARG E 501     1555   1555  1.32  
LINK         C   ACE F 501                 N   ARG F 502     1555   1555  1.33  
CISPEP   1 ASP B  345    PRO B  346          0         9.83                     
CISPEP   2 GLN D  323    PRO D  324          0       -14.28                     
SITE     1 AC1 13 GLU A  12  GLY A  13  ARG A  36  VAL A 163                    
SITE     2 AC1 13 MET B 210  ILE B 213  TRP B 217  GLU B 220                    
SITE     3 AC1 13 GLN B 254  ILE B 281  THR B 282  ASP B 283                    
SITE     4 AC1 13 HOH B2034                                                     
SITE     1 AC2 11 ASP C 247  MET D 210  GLU D 220  ARG D 250                    
SITE     2 AC2 11 GLN D 254  ILE D 281  THR D 282  ASP D 283                    
SITE     3 AC2 11 THR D 285  HOH F2002  HOH F2004                               
CRYST1   73.630  113.510  155.460  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013581  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008810  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006433        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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