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Database: PDB
Entry: 1E9H
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Original site: 1E9H 
HEADER    CELL CYCLE                              16-OCT-00   1E9H              
TITLE     THR 160 PHOSPHORYLATED CDK2 - HUMAN CYCLIN A3 COMPLEX WITH            
TITLE    2 THE INHIBITOR INDIRUBIN-5-SULPHONATE BOUND                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION PROTEIN KINASE 2;                            
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: CYCLIN-DEPENDENT KINASE 2, CDK2;                            
COMPND   5 EC: 2.7.1.37;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: PHOSPHORYLATED ON THR 160 CHAINS A AND C              
COMPND   8  ARE ASYMETRIC UNIT COPIES;                                          
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: CYCLIN A3;                                                 
COMPND  11 CHAIN: B, D;                                                         
COMPND  12 SYNONYM: A3;                                                         
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 OTHER_DETAILS: TRUNCATED FRAGMENT OF CYCLIN A. IN COMPLEX            
COMPND  15  WITH CDK2 CHAINS B AND D ARE ASYMETRIC UNIT COPIES                  
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CELL CYCLE, COMPLEX (PROTEIN KINASE/CYCLIN), KINASES,                 
KEYWDS   2 INHIBITOR, CYCLIN, COMPLEX, PHOSPHORYLATION                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.G.DAVIES,P.TUNNAH,M.E.M.NOBLE,J.A.ENDICOTT                          
REVDAT   4   24-FEB-09 1E9H    1       VERSN                                    
REVDAT   3   07-JUN-06 1E9H    1       REMARK CRYST1                            
REVDAT   2   26-NOV-01 1E9H    1       JRNL                                     
REVDAT   1   11-OCT-01 1E9H    0                                                
JRNL        AUTH   T.G.DAVIES,P.TUNNAH,L.MEIJER,D.MARKO,G.EISENBRAND,           
JRNL        AUTH 2 J.A.ENDICOTT,M.E.NOBLE                                       
JRNL        TITL   INHIBITOR BINDING TO ACTIVE AND INACTIVE CDK2: THE           
JRNL        TITL 2 CRYSTAL STRUCTURE OF CDK2-CYCLIN A/INDIRUBIN-5-              
JRNL        TITL 3 SULPHONATE                                                   
JRNL        REF    STRUCTURE                     V.   9   389 2001              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   11377199                                                     
JRNL        DOI    10.1016/S0969-2126(01)00598-6                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.5  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.5                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100                            
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90                             
REMARK   3   NUMBER OF REFLECTIONS             : 52335                          
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 SET) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8918                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 70                                      
REMARK   3   SOLVENT ATOMS            : 369                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.459                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1E9H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-OCT-00.                  
REMARK 100 THE PDBE ID CODE IS EBI-5449.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : 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                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47127                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.1                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.10900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: UNPUBLISHED STRUCTURE                                
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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       36.90050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.21800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       66.90200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       75.21800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.90050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       66.90200            
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 GENERATING THE BIOMOLECULE                                           
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 BIOMOLECULE:  2                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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  THE CDK2 SHOWS MAXIMAL ACTIVITY DURING S PHASE AND G2 AND           
REMARK 400  INTERACTS WITH CYCLINS A, D, OR E. IT IS PROBABLY                   
REMARK 400  INVOLVED IN THE CONTROL OF THE CELL CYCLE.                          
REMARK 400  CYCLIN IS ESSENTIAL FOR THE CONTROL OF THE CELL CYCLE AT THE        
REMARK 400  G1/S(START) AND THE G2/M (MITOSIS) TRANSITIONS.                     
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     SER A     0                                                      
REMARK 465     LEU B   433                                                      
REMARK 465     ASN B   434                                                      
REMARK 465     LEU B   435                                                      
REMARK 465     LEU D   433                                                      
REMARK 465     ASN D   434                                                      
REMARK 465     LEU D   435                                                      
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    TRP A   227  -  O    HOH A  2094              1.73            
REMARK 500   N    GLY A   229  -  O    HOH A  2094              2.15            
REMARK 500   N    VAL A   230  -  O    HOH A  2094              1.89            
REMARK 500   O    HOH A  2034  -  O    HOH A  2090              1.96            
REMARK 500   O    HOH A  2106  -  O    HOH A  2109              2.13            
REMARK 500   O    HOH B  2014  -  O    HOH B  2097              2.19            
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    PRO C 234   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    PRO C 241   C   -  N   -  CA  ANGL. DEV. =  23.7 DEGREES          
REMARK 500    PRO C 241   N   -  CA  -  C   ANGL. DEV. =  17.9 DEGREES          
REMARK 500    PRO C 241   N   -  CA  -  CB  ANGL. DEV. =  17.9 DEGREES          
REMARK 500    PRO C 241   N   -  CD  -  CG  ANGL. DEV. =  17.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 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   8      143.42   -176.84                                   
REMARK 500    LEU A  37      -96.69   -109.95                                   
REMARK 500    ASP A  38       20.54     88.42                                   
REMARK 500    THR A  39     -165.99     51.39                                   
REMARK 500    GLU A  40       63.45     13.52                                   
REMARK 500    THR A  41     -115.92   -156.91                                   
REMARK 500    ALA A  95      -32.60    -34.15                                   
REMARK 500    ASP A 127       38.64   -160.66                                   
REMARK 500    ASP A 145       79.15     51.68                                   
REMARK 500    GLU A 162       69.60    -67.77                                   
REMARK 500    VAL A 164      131.04     74.60                                   
REMARK 500    SER A 181     -145.16   -138.97                                   
REMARK 500    ARG A 199        7.43     86.57                                   
REMARK 500    ALA A 201      125.37    -17.94                                   
REMARK 500    THR A 231      -10.22    -47.62                                   
REMARK 500    ASP A 270      108.59    -58.72                                   
REMARK 500    ILE A 275      140.66    -39.87                                   
REMARK 500    LYS A 291       73.94   -106.40                                   
REMARK 500    PRO A 292     -111.17    -52.81                                   
REMARK 500    VAL A 293      156.54    178.64                                   
REMARK 500    ASP B 283       49.79     38.17                                   
REMARK 500    CYS B 327      -50.99    -29.98                                   
REMARK 500    TRP B 372      114.63    -25.97                                   
REMARK 500    TYR B 413       24.84    -77.90                                   
REMARK 500    GLU C   8      128.65   -173.50                                   
REMARK 500    ASP C  38       -6.61     63.01                                   
REMARK 500    THR C  39     -134.08     82.05                                   
REMARK 500    GLU C  40      111.18    -29.60                                   
REMARK 500    THR C  41      -83.59    159.60                                   
REMARK 500    LEU C  96      -71.80    -87.91                                   
REMARK 500    ASP C 127       38.08   -155.99                                   
REMARK 500    LYS C 129      146.32   -176.84                                   
REMARK 500    PRO C 130      -31.79    -38.23                                   
REMARK 500    ASP C 145       80.97     46.31                                   
REMARK 500    GLU C 162       79.61    -65.73                                   
REMARK 500    VAL C 164      130.47     71.87                                   
REMARK 500    LEU C 166      -69.86    -26.81                                   
REMARK 500    SER C 181     -149.29   -163.61                                   
REMARK 500    THR C 182      -37.81    -39.71                                   
REMARK 500    ARG C 199       -7.34     93.42                                   
REMARK 500    ASP C 223      161.11    160.73                                   
REMARK 500    GLU C 224      -34.48    -32.67                                   
REMARK 500    PRO C 234      -57.58    -11.86                                   
REMARK 500    SER C 239        9.82    -60.41                                   
REMARK 500    PRO C 241      162.19     23.35                                   
REMARK 500    ARG C 245      102.23    -57.52                                   
REMARK 500    VAL C 251      -78.04    -41.12                                   
REMARK 500    ALA C 282       40.32   -103.55                                   
REMARK 500    VAL C 289      144.69    -32.13                                   
REMARK 500    THR C 290     -140.81   -125.75                                   
REMARK 500    LYS C 291       69.18   -153.26                                   
REMARK 500    PRO D 176       35.17    -71.07                                   
REMARK 500    PRO D 195      173.62    -53.95                                   
REMARK 500    GLN D 228      153.97    -48.15                                   
REMARK 500    ASP D 284       59.18     31.76                                   
REMARK 500    HIS D 321       50.91    -90.50                                   
REMARK 500    ALA D 325      114.55    -30.46                                   
REMARK 500    TYR D 347      -17.80    -35.07                                   
REMARK 500    TRP D 372       99.14    -35.40                                   
REMARK 500    PRO D 373      151.46    -41.07                                   
REMARK 500    ALA D 401      -57.01    -25.62                                   
REMARK 500    LEU D 424      173.58    -54.29                                   
REMARK 500    ASN D 431       71.27     50.64                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    TYR B 347        24.7      L          L   OUTSIDE RANGE           
REMARK 500    PRO C 241        24.6      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INR A1298                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INR C1298                 
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               
REMARK 900  160                                                                 
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: 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: 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: 1JSU   RELATED DB: PDB                                   
REMARK 900  P27(KIP1)/CYCLIN A/CDK2 COMPLEX                                     
REMARK 900 RELATED ID: 1FIN   RELATED DB: PDB                                   
REMARK 900  CYCLIN A - CYCLIN-DEPENDENT KINASE 2 COMPLEX                        
REMARK 900 RELATED ID: 1JST   RELATED DB: PDB                                   
REMARK 900  PHOSPHORYLATED CYCLIN-DEPENDENT KINASE-2 BOUND TO CYCLIN            
REMARK 900  A                                                                   
REMARK 900 RELATED ID: 1QMZ   RELATED DB: PDB                                   
REMARK 900  PHOSPHORYLATED CDK2-CYCLYIN A-SUBSTRATE PEPTIDE COMPLEX             
DBREF  1E9H A    0     0  PDB    1E9H     1E9H             0      0             
DBREF  1E9H A    1   296  UNP    P24941   CDK2_HUMAN       1    296             
DBREF  1E9H B  175   432  UNP    P20248   CGA2_HUMAN     175    432             
DBREF  1E9H C    0     0  PDB    1E9H     1E9H             0      0             
DBREF  1E9H C    1   296  UNP    P24941   CDK2_HUMAN       1    296             
DBREF  1E9H D  175   432  UNP    P20248   CGA2_HUMAN     175    432             
SEQADV 1E9H TPO A  160  UNP  P20248    THR   160 MODIFIED RESIDUE               
SEQRES   1 A  297  SER MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU          
SEQRES   2 A  297  GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU          
SEQRES   3 A  297  THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP          
SEQRES   4 A  297  THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU          
SEQRES   5 A  297  ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL          
SEQRES   6 A  297  LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR          
SEQRES   7 A  297  LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE          
SEQRES   8 A  297  MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU          
SEQRES   9 A  297  ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA          
SEQRES  10 A  297  PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS          
SEQRES  11 A  297  PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS          
SEQRES  12 A  297  LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO          
SEQRES  13 A  297  VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP TYR          
SEQRES  14 A  297  ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER          
SEQRES  15 A  297  THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA          
SEQRES  16 A  297  GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER          
SEQRES  17 A  297  GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY          
SEQRES  18 A  297  THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET          
SEQRES  19 A  297  PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN          
SEQRES  20 A  297  ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY          
SEQRES  21 A  297  ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN          
SEQRES  22 A  297  LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE          
SEQRES  23 A  297  PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU                  
SEQRES   1 B  261  VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU ARG          
SEQRES   2 B  261  GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET          
SEQRES   3 B  261  LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE          
SEQRES   4 B  261  LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS          
SEQRES   5 B  261  LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE          
SEQRES   6 B  261  ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS          
SEQRES   7 B  261  LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER          
SEQRES   8 B  261  LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE          
SEQRES   9 B  261  VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN VAL          
SEQRES  10 B  261  LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR PHE          
SEQRES  11 B  261  ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN          
SEQRES  12 B  261  TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL GLU          
SEQRES  13 B  261  SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP          
SEQRES  14 B  261  ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE ALA          
SEQRES  15 B  261  GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY          
SEQRES  16 B  261  GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY TYR          
SEQRES  17 B  261  THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU HIS          
SEQRES  18 B  261  GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER          
SEQRES  19 B  261  ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY VAL          
SEQRES  20 B  261  SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU LEU ASN          
SEQRES  21 B  261  LEU                                                          
SEQRES   1 C  297  SER MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU          
SEQRES   2 C  297  GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU          
SEQRES   3 C  297  THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP          
SEQRES   4 C  297  THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU          
SEQRES   5 C  297  ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL          
SEQRES   6 C  297  LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR          
SEQRES   7 C  297  LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE          
SEQRES   8 C  297  MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU          
SEQRES   9 C  297  ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA          
SEQRES  10 C  297  PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS          
SEQRES  11 C  297  PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS          
SEQRES  12 C  297  LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO          
SEQRES  13 C  297  VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP TYR          
SEQRES  14 C  297  ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER          
SEQRES  15 C  297  THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA          
SEQRES  16 C  297  GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER          
SEQRES  17 C  297  GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY          
SEQRES  18 C  297  THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET          
SEQRES  19 C  297  PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN          
SEQRES  20 C  297  ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY          
SEQRES  21 C  297  ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN          
SEQRES  22 C  297  LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE          
SEQRES  23 C  297  PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU                  
SEQRES   1 D  261  VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU ARG          
SEQRES   2 D  261  GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET          
SEQRES   3 D  261  LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE          
SEQRES   4 D  261  LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS          
SEQRES   5 D  261  LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE          
SEQRES   6 D  261  ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS          
SEQRES   7 D  261  LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER          
SEQRES   8 D  261  LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE          
SEQRES   9 D  261  VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN VAL          
SEQRES  10 D  261  LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR PHE          
SEQRES  11 D  261  ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN          
SEQRES  12 D  261  TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL GLU          
SEQRES  13 D  261  SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP          
SEQRES  14 D  261  ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE ALA          
SEQRES  15 D  261  GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY          
SEQRES  16 D  261  GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY TYR          
SEQRES  17 D  261  THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU HIS          
SEQRES  18 D  261  GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER          
SEQRES  19 D  261  ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY VAL          
SEQRES  20 D  261  SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU LEU ASN          
SEQRES  21 D  261  LEU                                                          
MODRES 1E9H TPO A  160  THR  PHOSPHOTHREONINE                                   
MODRES 1E9H TPO C  160  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET    INR  A1298      24                                                       
HET    INR  C1298      24                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     INR 2',3-DIOXO-1,1',2',3-TETRAHYDRO-2,3'-                            
HETNAM   2 INR  BIINDOLE-5'-SULFONIC ACID                                       
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     INR INDIRUBIN-5-SULPHONATE                                           
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   5  INR    2(C16 H10 N2 O5 S)                                           
FORMUL   7  HOH   *369(H2 O1)                                                   
HELIX    1   1 PRO A   45  GLU A   57  1                                  13    
HELIX    2   2 LEU A   87  ALA A   93  1                                   7    
HELIX    3   3 PRO A  100  HIS A  121  1                                  22    
HELIX    4   4 LYS A  129  GLN A  131  5                                   3    
HELIX    5   5 THR A  165  ARG A  169  5                                   5    
HELIX    6   6 ALA A  170  LEU A  175  1                                   6    
HELIX    7   7 THR A  182  ARG A  199  1                                  18    
HELIX    8   8 SER A  207  GLY A  220  1                                  14    
HELIX    9   9 GLY A  229  MET A  233  5                                   5    
HELIX   10  10 ASP A  247  VAL A  251  5                                   5    
HELIX   11  11 ASP A  256  LEU A  267  1                                  12    
HELIX   12  12 SER A  276  LEU A  281  1                                   6    
HELIX   13  13 ALA A  282  GLN A  287  5                                   6    
HELIX   14  14 TYR B  178  LYS B  194  1                                  17    
HELIX   15  15 TYR B  199  GLN B  203  5                                   5    
HELIX   16  16 THR B  207  TYR B  225  1                                  19    
HELIX   17  17 GLN B  228  LEU B  243  1                                  16    
HELIX   18  18 LYS B  252  GLU B  269  1                                  18    
HELIX   19  19 GLU B  274  ILE B  281  1                                   8    
HELIX   20  20 THR B  287  LEU B  302  1                                  16    
HELIX   21  21 THR B  310  PHE B  319  1                                  10    
HELIX   22  22 LEU B  320  GLN B  322  5                                   3    
HELIX   23  23 ASN B  326  ASP B  343  1                                  18    
HELIX   24  24 ASP B  343  LEU B  348  1                                   6    
HELIX   25  25 LEU B  351  GLY B  369  1                                  19    
HELIX   26  26 PRO B  373  GLY B  381  1                                   9    
HELIX   27  27 THR B  383  ALA B  401  1                                  19    
HELIX   28  28 PRO B  402  HIS B  404  5                                   3    
HELIX   29  29 GLN B  407  TYR B  413  1                                   7    
HELIX   30  30 LYS B  414  HIS B  419  5                                   6    
HELIX   31  31 GLY B  420  LEU B  424  5                                   5    
HELIX   32  32 SER C    0  GLU C    2  5                                   3    
HELIX   33  33 PRO C   45  LYS C   56  1                                  12    
HELIX   34  34 LEU C   87  ALA C   93  1                                   7    
HELIX   35  35 PRO C  100  HIS C  121  1                                  22    
HELIX   36  36 LYS C  129  GLN C  131  5                                   3    
HELIX   37  37 THR C  165  ARG C  169  5                                   5    
HELIX   38  38 ALA C  170  LEU C  175  1                                   6    
HELIX   39  39 THR C  182  ARG C  199  1                                  18    
HELIX   40  40 SER C  207  GLY C  220  1                                  14    
HELIX   41  41 GLY C  229  MET C  233  5                                   5    
HELIX   42  42 ASP C  247  VAL C  252  1                                   6    
HELIX   43  43 ASP C  256  LEU C  267  1                                  12    
HELIX   44  44 SER C  276  LEU C  281  1                                   6    
HELIX   45  45 HIS C  283  GLN C  287  5                                   5    
HELIX   46  46 TYR D  178  VAL D  191  1                                  14    
HELIX   47  47 THR D  207  TYR D  225  1                                  19    
HELIX   48  48 GLN D  228  SER D  244  1                                  17    
HELIX   49  49 LEU D  249  GLU D  269  1                                  21    
HELIX   50  50 GLU D  274  ILE D  281  1                                   8    
HELIX   51  51 THR D  287  LEU D  302  1                                  16    
HELIX   52  52 THR D  310  LEU D  320  1                                  11    
HELIX   53  53 ASN D  326  SER D  340  1                                  15    
HELIX   54  54 PRO D  346  TYR D  350  5                                   5    
HELIX   55  55 LEU D  351  THR D  368  1                                  18    
HELIX   56  56 PRO D  373  GLY D  381  1                                   9    
HELIX   57  57 LEU D  387  ALA D  401  1                                  15    
HELIX   58  58 PRO D  402  HIS D  404  5                                   3    
HELIX   59  59 ILE D  409  LYS D  414  1                                   6    
HELIX   60  60 ASN D  415  HIS D  419  5                                   5    
SHEET    1   A 5 PHE A   4  GLY A  11  0                                        
SHEET    2   A 5 VAL A  18  ASN A  23 -1  O  VAL A  18   N  ILE A  10           
SHEET    3   A 5 VAL A  29  ARG A  36 -1  O  VAL A  30   N  ALA A  21           
SHEET    4   A 5 LYS A  75  GLU A  81 -1  O  LEU A  76   N  ILE A  35           
SHEET    5   A 5 LEU A  66  HIS A  71 -1  N  LEU A  67   O  VAL A  79           
SHEET    1   B 3 GLN A  85  ASP A  86  0                                        
SHEET    2   B 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3   B 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1   C 2 VAL A 123  LEU A 124  0                                        
SHEET    2   C 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SHEET    1   D 5 PHE C   4  LYS C   9  0                                        
SHEET    2   D 5 VAL C  18  ASN C  23 -1  O  LYS C  20   N  VAL C   7           
SHEET    3   D 5 VAL C  29  ARG C  36 -1  O  VAL C  30   N  ALA C  21           
SHEET    4   D 5 LYS C  75  GLU C  81 -1  O  LEU C  76   N  ILE C  35           
SHEET    5   D 5 LEU C  66  HIS C  71 -1  N  LEU C  67   O  VAL C  79           
SHEET    1   E 3 GLN C  85  ASP C  86  0                                        
SHEET    2   E 3 LEU C 133  ILE C 135 -1  O  ILE C 135   N  GLN C  85           
SHEET    3   E 3 ILE C 141  LEU C 143 -1  O  LYS C 142   N  LEU C 134           
SHEET    1   F 2 VAL C 123  LEU C 124  0                                        
SHEET    2   F 2 ARG C 150  ALA C 151 -1  O  ARG C 150   N  LEU C 124           
LINK         C   TYR A 159                 N   TPO A 160     1555   1555  1.32  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.33  
LINK         C   TYR C 159                 N   TPO C 160     1555   1555  1.32  
LINK         C   TPO C 160                 N   HIS C 161     1555   1555  1.33  
CISPEP   1 VAL A  154    PRO A  155          0        -0.10                     
CISPEP   2 GLN B  323    PRO B  324          0        -0.35                     
CISPEP   3 ASP B  345    PRO B  346          0         0.60                     
CISPEP   4 VAL C  154    PRO C  155          0        -0.05                     
CISPEP   5 GLN D  323    PRO D  324          0        -0.48                     
CISPEP   6 ASP D  345    PRO D  346          0         0.34                     
SITE     1 AC1 14 ILE A  10  VAL A  18  ALA A  31  LYS A  33                    
SITE     2 AC1 14 PHE A  80  GLU A  81  PHE A  82  LEU A  83                    
SITE     3 AC1 14 HIS A  84  GLN A  85  LYS A  89  LEU A 134                    
SITE     4 AC1 14 ALA A 144  ASP A 145                                          
SITE     1 AC2 11 ALA C  31  LYS C  33  PHE C  80  GLU C  81                    
SITE     2 AC2 11 PHE C  82  LEU C  83  HIS C  84  GLN C  85                    
SITE     3 AC2 11 ASP C  86  LEU C 134  ASP C 145                               
CRYST1   73.801  133.804  150.436  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      0.013550  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007474  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006647        0.00000                         
MTRIX1   1 -0.999932 -0.011239  0.003138      174.44279    1                    
MTRIX2   1  0.010826 -0.793178  0.608894       -1.51400    1                    
MTRIX3   1 -0.004354  0.608886  0.793246        0.70450    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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