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Database: PDB
Entry: 1OL1
LinkDB: 1OL1
Original site: 1OL1 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       04-AUG-03   1OL1              
TITLE     CYCLIN A BINDING GROOVE INHIBITOR H-CIT-CIT-LEU-ILE-(P-F-PHE)-NH2     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION PROTEIN KINASE 2;                            
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: CYCLIN-DEPENDENT KINASE 2, P33 PROTEIN KINASE;              
COMPND   5 EC: 2.7.1.37;                                                        
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;                                                   
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: CIR-CIR-LEU-ILE-PFF-NH2;                                   
COMPND  15 CHAIN: F, H;                                                         
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 OTHER_DETAILS: CYCLIN GROOVE-BOUND PEPTIDE CIT-CIT-LEU-ILE-PFF-NH2   
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_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
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 MOL_ID: 3;                                                           
SOURCE  16 SYNTHETIC: YES;                                                      
SOURCE  17 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  18 ORGANISM_TAXID: 32630                                                
KEYWDS    TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX, CELL CYCLE, KINASE-CYCLIN  
KEYWDS   2 COMPLEX, CYCLIN A, INHIBITOR, LIGAND EXCHANGE, DRUG DESIGN,          
KEYWDS   3 SERINE/THREONINE-PROTEIN KINASE, ATP-BINDING, CELL DIVISION,         
KEYWDS   4 MITOSIS, PHOSPHORYLATION, 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   15-FEB-17 1OL1    1       SOURCE JRNL                              
REVDAT   4   13-JUL-11 1OL1    1       VERSN                                    
REVDAT   3   16-JUN-09 1OL1    1       KEYWDS JRNL   REMARK SITE                
REVDAT   3 2                   1       MASTER                                   
REVDAT   2   24-FEB-09 1OL1    1       VERSN                                    
REVDAT   1   11-DEC-03 1OL1    0                                                
JRNL        AUTH   G.KONTOPIDIS,M.ANDREWS,C.MCINNES,A.COWAN,H.POWERS,L.INNES,   
JRNL        AUTH 2 A.PLATER,G.GRIFFITHS,D.PATERSON,D.ZHELEVA,D.LANE,S.GREEN,    
JRNL        AUTH 3 M.WALKINSHAW,P.FISCHER                                       
JRNL        TITL   INSIGHTS INTO CYCLIN GROOVE RECOGNITION. COMPLEX CRYSTAL     
JRNL        TITL 2 STRUCTURES AND INHIBITOR DESIGN THROUGH LIGAND EXCHANGE      
JRNL        REF    STRUCTURE                     V.  11  1537 2003              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   14656438                                                     
JRNL        DOI    10.1016/J.STR.2003.11.006                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 12.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 27895                          
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) : 0.209                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.284                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1198                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.97                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1950                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2910                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 81                           
REMARK   3   BIN FREE R VALUE                    : 0.4180                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9025                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 73                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.14                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.91000                                             
REMARK   3    B22 (A**2) : 1.73000                                              
REMARK   3    B33 (A**2) : 2.15000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.490         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.399         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.707        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.930                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.863                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9249 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  8494 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12555 ; 1.419 ; 1.980       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 19820 ; 1.160 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1104 ;11.417 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1424 ; 0.101 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9990 ; 0.013 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1806 ; 0.007 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3024 ; 0.331 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A): 11318 ; 0.331 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  5588 ; 0.100 ; 0.500       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   557 ; 0.305 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    40 ; 0.283 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    70 ; 0.337 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.507 ; 0.500       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5553 ; 4.393 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9031 ; 6.910 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3696 ; 9.552 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3524 ;14.098 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BULK SOLVENT                                         
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1OL1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-AUG-03.                  
REMARK 100 THE PDBE ID CODE IS EBI-13238.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-NOV-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               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
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   : 29357                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 22.500                             
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 2.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
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       37.24900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       77.24100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.73550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       77.24100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.24900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.73550            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, F                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4780 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23490 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, H                               
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  FUNCTION: INVOLVED IN THE CONTROL OF THE CELL CYCLE.                
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     ARG C   297                                                      
REMARK 465     LEU C   298                                                      
REMARK 465     ASN D   173                                                      
REMARK 465     GLU D   174                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    TYR B   318     N    LEU B   320              1.76            
REMARK 500   OD2  ASP D   216     OG   SER D   408              2.05            
REMARK 500   O    THR B   282     OG1  THR B   285              2.11            
REMARK 500   O    ILE C    49     OG   SER C    53              2.15            
REMARK 500   NZ   LYS C   278     OD2  ASP D   181              2.15            
REMARK 500   O    SER D   416     N    HIS D   419              2.17            
REMARK 500   OH   TYR D   225     OE1  GLU D   277              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NZ   LYS A    89     OH   TYR B   280     4455     2.06            
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    ASP A  92   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP A 235   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP A 256   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP A 288   CB  -  CG  -  OD2 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ASP B 177   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP B 284   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP B 345   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP C 223   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP C 256   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP C 258   CB  -  CG  -  OD2 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    ASP D 205   CB  -  CG  -  OD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP D 216   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP D 284   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP D 345   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP D 393   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 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  12     -172.26    166.10                                   
REMARK 500    THR A  14      172.25    -50.21                                   
REMARK 500    TYR A  15      -81.68     50.94                                   
REMARK 500    VAL A  17      129.20     11.68                                   
REMARK 500    LEU A  37      124.27     96.64                                   
REMARK 500    THR A  41       43.86   -146.72                                   
REMARK 500    GLU A  42      -56.92    179.19                                   
REMARK 500    HIS A  60      142.99   -172.64                                   
REMARK 500    GLN A  85     -177.54   -175.99                                   
REMARK 500    LEU A  96      -56.40    111.31                                   
REMARK 500    ARG A 122       58.16     36.01                                   
REMARK 500    ARG A 126       -0.63     68.37                                   
REMARK 500    ASP A 127       46.71   -150.41                                   
REMARK 500    LYS A 129      146.36   -178.58                                   
REMARK 500    ASP A 145       80.76     59.17                                   
REMARK 500    PHE A 152       54.84   -118.12                                   
REMARK 500    THR A 160      -79.03     -0.14                                   
REMARK 500    THR A 165      160.77    139.88                                   
REMARK 500    ARG A 199       -6.67     75.11                                   
REMARK 500    SER A 207      153.70    172.30                                   
REMARK 500    TRP A 227       78.42   -166.22                                   
REMARK 500    PRO A 284      -35.73    -35.41                                   
REMARK 500    THR A 290     -165.55   -112.17                                   
REMARK 500    PRO B 176       51.17    -53.93                                   
REMARK 500    HIS B 179     -101.15    -57.49                                   
REMARK 500    GLU B 180      -65.66     -0.75                                   
REMARK 500    ASP B 283       65.43     69.95                                   
REMARK 500    ASP B 284       49.41     33.54                                   
REMARK 500    TYR B 318     -115.64    -59.28                                   
REMARK 500    PHE B 319      -39.05     39.55                                   
REMARK 500    ALA B 325      155.95    -43.50                                   
REMARK 500    ASN B 326      124.57   -178.06                                   
REMARK 500    TRP B 372      104.00    -16.69                                   
REMARK 500    GLN B 407       -2.48   -142.47                                   
REMARK 500    LEU B 424      147.44    -37.06                                   
REMARK 500    VAL C   7      -66.13    -96.37                                   
REMARK 500    TYR C  15      -78.75   -120.05                                   
REMARK 500    THR C  39       27.44    -64.21                                   
REMARK 500    THR C  41     -108.88    -81.90                                   
REMARK 500    GLU C  42       15.70   -150.01                                   
REMARK 500    LEU C  96      -22.98     67.56                                   
REMARK 500    ARG C 126        0.27     81.19                                   
REMARK 500    ASP C 127       47.29   -155.07                                   
REMARK 500    ASP C 145       68.99     66.17                                   
REMARK 500    HIS C 161     -134.70     69.80                                   
REMARK 500    GLU C 162      121.29     62.20                                   
REMARK 500    VAL C 163     -103.73     61.11                                   
REMARK 500    VAL C 164     -112.15     48.89                                   
REMARK 500    THR C 165      -69.82   -157.24                                   
REMARK 500    LEU C 166      -73.48     96.74                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      74 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 VAL A  163     VAL A  164                 -144.99                    
REMARK 500 PRO B  346     TYR B  347                 -149.28                    
REMARK 500 LYS D  202     GLN D  203                  146.04                    
REMARK 500 LEU D  227     GLN D  228                  144.97                    
REMARK 500 ALA D  344     ASP D  345                 -146.42                    
REMARK 500 ASP D  345     PRO D  346                  149.23                    
REMARK 500 PRO D  346     TYR D  347                 -145.09                    
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 F OF CIR-CIR-LEU-ILE-PFF-   
REMARK 800  NH2                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN H OF CIR-CIR-LEU-ILE-PFF-   
REMARK 800  NH2                                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AQ1   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE                   
REMARK 900 INHIBITOR 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          
REMARK 900 CYCLE-REGULATORY PROTEIN CKSHS1                                      
REMARK 900 RELATED ID: 1CKP   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE                   
REMARK 900 INHIBITOR PURVALANOL B                                               
REMARK 900 RELATED ID: 1DI8   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) IN                 
REMARK 900 COMPLEX WITH 4-[3- HYDROXYANILINO]-6,7-DIMETHOXYQUINAZOLINE          
REMARK 900 RELATED ID: 1DM2   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2 COMPLEXED WITH THE                   
REMARK 900 INHIBITOR HYMENIALDISINE                                             
REMARK 900 RELATED ID: 1E1V   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE                   
REMARK 900 INHIBITOR NU2058                                                     
REMARK 900 RELATED ID: 1E1X   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE                   
REMARK 900 INHIBITOR NU6027                                                     
REMARK 900 RELATED ID: 1E9H   RELATED DB: PDB                                   
REMARK 900 THR 160 PHOSPHORYLATED CDK2 - HUMAN CYCLIN A3 COMPLEX WITH           
REMARK 900 THE INHIBITOR INDIRUBIN-5- SULPHONATE BOUND                          
REMARK 900 RELATED ID: 1F5Q   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MURINE GAMMA HERPESVIRUS CYCLIN                 
REMARK 900 COMPLEXED TO 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)             
REMARK 900 INCOMPLEX WITH PHOSPHO-CDK2                                          
REMARK 900 RELATED ID: 1FVT   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) INCOMPLEX          
REMARK 900 WITH AN OXINDOLE INHIBITOR                                           
REMARK 900 RELATED ID: 1FVV   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CDK2/CYCLIN A IN COMPLEX WITH AN                    
REMARK 900 OXINDOLEINHIBITOR                                                    
REMARK 900 RELATED ID: 1G5S   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLIN DEPENDENT KINASE 2 (CDK2)          
REMARK 900 IN COMPLEX WITH THE INHIBITOR H717                                   
REMARK 900 RELATED ID: 1GIH   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE                   
REMARK 900 CDK4INHIBITOR                                                        
REMARK 900 RELATED ID: 1GII   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE                   
REMARK 900 CDK4INHIBITOR                                                        
REMARK 900 RELATED ID: 1GIJ   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE                   
REMARK 900 CDK4INHIBITOR                                                        
REMARK 900 RELATED ID: 1GY3   RELATED DB: PDB                                   
REMARK 900 PCDK2/CYCLIN A IN COMPLEX WITH MGADP, NITRATE AND PEPTIDE            
REMARK 900 SUBSTRATE                                                            
REMARK 900 RELATED ID: 1GZ8   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE                   
REMARK 900 INHIBITOR 2-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               
REMARK 900 PYRIMIDINE CDK4 INHIBITOR                                            
REMARK 900 RELATED ID: 1H01   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 2, 4 -BIS ANILINO               
REMARK 900 PYRIMIDINE CDK4 INHIBITOR                                            
REMARK 900 RELATED ID: 1H06   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6 -BIS ANILINO               
REMARK 900 PYRIMIDINE CDK4 INHIBITOR                                            
REMARK 900 RELATED ID: 1H07   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6 -BIS ANILINO               
REMARK 900 PYRIMIDINE CDK4 INHIBITOR                                            
REMARK 900 RELATED ID: 1H08   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 2, 4 -BIS ANILINO               
REMARK 900 PYRIMIDINE 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           
REMARK 900 WITH THE INHIBITOR NU2058                                            
REMARK 900 RELATED ID: 1H1Q   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED           
REMARK 900 WITH THE INHIBITOR NU6094                                            
REMARK 900 RELATED ID: 1H1R   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED           
REMARK 900 WITH THE INHIBITOR NU6086                                            
REMARK 900 RELATED ID: 1H1S   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED           
REMARK 900 WITH THE INHIBITOR NU6102                                            
REMARK 900 RELATED ID: 1H24   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH A 9 RESIDUE RECRUITMENT                 
REMARK 900 PEPTIDE FROM E2F                                                     
REMARK 900 RELATED ID: 1H25   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT               
REMARK 900 PEPTIDE FROM E2F                                                     
REMARK 900 RELATED ID: 1H26   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT               
REMARK 900 PEPTIDE FROM P53                                                     
REMARK 900 RELATED ID: 1H27   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT               
REMARK 900 PEPTIDE FROM P27                                                     
REMARK 900 RELATED ID: 1H28   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT               
REMARK 900 PEPTIDE FROM 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          
REMARK 900 WITH 4-[(6-AMINO-4- PYRIMIDINYL)AMINO]BENZENESULFONAMIDE             
REMARK 900 RELATED ID: 1JVP   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CDK2 (UNPHOSPHORYLATED)                   
REMARK 900 INCOMPLEX WITH PKF049-365                                            
REMARK 900 RELATED ID: 1KE5   RELATED DB: PDB                                   
REMARK 900 CDK2 COMPLEXED WITH N-METHYL-4-{[(2-OXO- 1,2-DIHYDRO-3H-             
REMARK 900 INDOL-3-YLIDENE)METHYL] AMINO}BENZENESULFONAMIDE                     
REMARK 900 RELATED ID: 1KE6   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH N-METHYL-{           
REMARK 900 4-[2-(7-OXO-6,7-DIHYDRO -8H-[1,3]THIAZOLO[5,4-E]INDOL-8-             
REMARK 900 YLIDENE)HYDRAZINO]PHENYL}METHANESULFONAMIDE                          
REMARK 900 RELATED ID: 1KE7   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 3-{[(2,2-            
REMARK 900 DIOXIDO-1,3-DIHYDRO-2- BENZOTHIEN-5-YL)AMINO]METHYLENE}-5-           
REMARK 900 (1,3- OXAZOL-5-YL)-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-          
REMARK 900 1,2-DIHYDRO-3H-INDOL-3 -YLIDENE)METHYL]AMINO}-N-(1,3-                
REMARK 900 THIAZOL-2- YL)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          
REMARK 900 -2,3- DIHYDRO-1H-INDOLE                                              
REMARK 900 RELATED ID: 1OGU   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED           
REMARK 900 WITH A 2-ARYLAMINO-4- CYCLOHEXYLMETHYL-5-NITROSO-6-                  
REMARK 900 AMINOPYRIMIDINE INHIBITOR                                            
REMARK 900 RELATED ID: 1OI9   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED           
REMARK 900 WITH A 6- CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR             
REMARK 900 RELATED ID: 1OIQ   RELATED DB: PDB                                   
REMARK 900 IMIDAZOPYRIDINES: A POTENT AND SELECTIVE CLASS OF CYCLIN-            
REMARK 900 DEPENDENT KINASE INHIBITORS IDENTIFIED THROUGH STRUCTURE-            
REMARK 900 BASED HYBRIDISATION                                                  
REMARK 900 RELATED ID: 1OIR   RELATED DB: PDB                                   
REMARK 900 IMIDAZOPYRIDINES: A POTENT AND SELECTIVE CLASS OF CYCLIN-            
REMARK 900 DEPENDENT KINASE INHIBITORS IDENTIFIED THROUGH STRUCTURE-            
REMARK 900 BASED HYBRIDISATION                                                  
REMARK 900 RELATED ID: 1OIT   RELATED DB: PDB                                   
REMARK 900 IMIDAZOPYRIDINES: A POTENT AND SELECTIVE CLASS OF CYCLIN-            
REMARK 900 DEPENDENT KINASE INHIBITORS IDENTIFIED THROUGH STRUCTURE-            
REMARK 900 BASED HYBRIDISATION                                                  
REMARK 900 RELATED ID: 1OIU   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED           
REMARK 900 WITH A 6- CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR             
REMARK 900 RELATED ID: 1OIY   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED           
REMARK 900 WITH A 6- 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          
REMARK 900 -ILE-(P-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          
REMARK 900 -PHE)-NH2                                                            
REMARK 900 RELATED ID: 1OL2   RELATED DB: PDB                                   
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-ARG- ARG-LEU-ASN-(P-F-           
REMARK 900 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                
REMARK 900 THEINHIBITOR 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-             
REMARK 900 CDK2/CYCLIN A                                                        
REMARK 900 RELATED ID: 1QMZ   RELATED DB: PDB                                   
REMARK 900 PHOSPHORYLATED CDK2-CYCLYIN A-SUBSTRATE PEPTIDE COMPLEX              
DBREF  1OL1 A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  1OL1 B  173   432  UNP    P20248   CG2A_HUMAN     173    432             
DBREF  1OL1 C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  1OL1 D  173   432  UNP    P20248   CG2A_HUMAN     173    432             
DBREF  1OL1 F  500   505  PDB    1OL1     1OL1           500    505             
DBREF  1OL1 H  500   505  PDB    1OL1     1OL1           500    505             
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 F    6  CIR CIR LEU ILE PFF NH2                                      
SEQRES   1 H    6  CIR CIR LEU ILE PFF NH2                                      
MODRES 1OL1 PFF F  504  PHE  4-FLUORO-L-PHENYLANANINE                           
MODRES 1OL1 PFF H  504  PHE  4-FLUORO-L-PHENYLANANINE                           
MODRES 1OL1 CIR F  500  ARG  CITRULLINE                                         
MODRES 1OL1 CIR F  501  ARG  CITRULLINE                                         
MODRES 1OL1 CIR H  500  ARG  CITRULLINE                                         
MODRES 1OL1 CIR H  501  ARG  CITRULLINE                                         
HET    CIR  F 500      11                                                       
HET    CIR  F 501      11                                                       
HET    PFF  F 504      12                                                       
HET    NH2  F 505       1                                                       
HET    CIR  H 500      11                                                       
HET    CIR  H 501      11                                                       
HET    PFF  H 504      12                                                       
HET    NH2  H 505       1                                                       
HETNAM     CIR CITRULLINE                                                       
HETNAM     PFF 4-FLUORO-L-PHENYLALANINE                                         
HETNAM     NH2 AMINO GROUP                                                      
FORMUL   5  CIR    4(C6 H13 N3 O3)                                              
FORMUL   5  PFF    2(C9 H10 F N O2)                                             
FORMUL   5  NH2    2(H2 N)                                                      
FORMUL   7  HOH   *73(H2 O)                                                     
HELIX    1   1 PRO A   45  LYS A   56  1                                  12    
HELIX    2   2 LEU A   87  ALA A   95  1                                   9    
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 SER A  181  ARG A  199  1                                  19    
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 ASP A  270  ARG A  274  5                                   5    
HELIX   12  12 SER A  276  HIS A  283  1                                   8    
HELIX   13  13 PRO A  284  GLN A  287  5                                   4    
HELIX   14  14 TYR B  178  CYS B  193  1                                  16    
HELIX   15  15 THR B  207  TYR B  225  1                                  19    
HELIX   16  16 GLN B  228  LEU B  243  1                                  16    
HELIX   17  17 LYS B  252  GLU B  269  1                                  18    
HELIX   18  18 GLU B  274  ILE B  281  1                                   8    
HELIX   19  19 THR B  287  LEU B  302  1                                  16    
HELIX   20  20 THR B  310  TYR B  318  1                                   9    
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  THR B  368  1                                  18    
HELIX   24  24 GLU B  374  THR B  380  1                                   7    
HELIX   25  25 THR B  383  LYS B  400  1                                  18    
HELIX   26  26 ALA B  401  HIS B  404  5                                   4    
HELIX   27  27 GLN B  407  TYR B  413  1                                   7    
HELIX   28  28 ASN B  415  HIS B  419  5                                   5    
HELIX   29  29 GLY B  420  LEU B  424  5                                   5    
HELIX   30  30 PRO C   45  LYS C   56  1                                  12    
HELIX   31  31 LEU C   87  ALA C   93  1                                   7    
HELIX   32  32 PRO C  100  SER C  120  1                                  21    
HELIX   33  33 ALA C  170  LEU C  175  1                                   6    
HELIX   34  34 THR C  182  ARG C  199  1                                  18    
HELIX   35  35 SER C  207  GLY C  220  1                                  14    
HELIX   36  36 GLY C  229  MET C  233  5                                   5    
HELIX   37  37 ASP C  247  VAL C  252  1                                   6    
HELIX   38  38 ASP C  256  LEU C  267  1                                  12    
HELIX   39  39 SER C  276  ALA C  282  1                                   7    
HELIX   40  40 HIS C  283  GLN C  287  5                                   5    
HELIX   41  41 TYR D  178  GLU D  190  1                                  13    
HELIX   42  42 THR D  207  TYR D  225  1                                  19    
HELIX   43  43 GLN D  228  SER D  244  1                                  17    
HELIX   44  44 LEU D  249  GLU D  269  1                                  21    
HELIX   45  45 GLU D  274  ILE D  281  1                                   8    
HELIX   46  46 THR D  287  LEU D  302  1                                  16    
HELIX   47  47 THR D  310  PHE D  319  1                                  10    
HELIX   48  48 LEU D  320  GLN D  322  5                                   3    
HELIX   49  49 ASN D  326  ASP D  343  1                                  18    
HELIX   50  50 ASP D  343  LEU D  348  1                                   6    
HELIX   51  51 LEU D  351  THR D  368  1                                  18    
HELIX   52  52 PRO D  373  GLY D  381  1                                   9    
HELIX   53  53 LEU D  387  LYS D  400  1                                  14    
HELIX   54  54 GLN D  407  TYR D  413  1                                   7    
SHEET    1  AA 5 PHE A   4  LYS A   9  0                                        
SHEET    2  AA 5 VAL A  18  ASN A  23 -1  O  LYS A  20   N  VAL A   7           
SHEET    3  AA 5 VAL A  29  ILE A  35 -1  O  VAL A  30   N  ALA A  21           
SHEET    4  AA 5 LEU A  76  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         C1  CIR F 500                 N2  CIR F 501     1555   1555  1.35  
LINK         C1  CIR F 501                 N   LEU F 502     1555   1555  1.32  
LINK         C   ILE F 503                 N   PFF F 504     1555   1555  1.33  
LINK         C   PFF F 504                 N   NH2 F 505     1555   1555  1.34  
LINK         C1  CIR H 500                 N2  CIR H 501     1555   1555  1.33  
LINK         C1  CIR H 501                 N   LEU H 502     1555   1555  1.34  
LINK         C   ILE H 503                 N   PFF H 504     1555   1555  1.34  
LINK         C   PFF H 504                 N   NH2 H 505     1555   1555  1.33  
CISPEP   1 GLN B  323    PRO B  324          0        -8.08                     
CISPEP   2 GLN D  323    PRO D  324          0        -6.43                     
SITE     1 AC1 13 GLU A  12  GLY A  13  VAL A 163  THR A 165                    
SITE     2 AC1 13 MET B 210  LEU B 214  TRP B 217  ARG B 250                    
SITE     3 AC1 13 GLN B 254  TYR B 271  ILE B 281  ASP B 283                    
SITE     4 AC1 13 THR B 285                                                     
SITE     1 AC2 10 ASP C 247  MET D 210  LEU D 214  TRP D 217                    
SITE     2 AC2 10 ARG D 250  GLN D 254  ILE D 281  THR D 282                    
SITE     3 AC2 10 ASP D 283  THR D 285                                          
CRYST1   74.498  113.471  154.482  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      0.013423  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008813  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006473        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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