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Database: PDB
Entry: 3DOG
LinkDB: 3DOG
Original site: 3DOG 
HEADER    TRANSFERASE, CELL CYCLE                 04-JUL-08   3DOG              
TITLE     STRUCTURE OF THR 160 PHOSPHORYLATED CDK2/CYCLIN A IN                  
TITLE    2 COMPLEX WITH THE INHIBITOR N-&-N1                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION PROTEIN KINASE 2;                            
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: P33 PROTEIN KINASE, CDK2;                                   
COMPND   5 EC: 2.7.11.22;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CYCLIN-A2;                                                 
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: UNP RESIDUES 169-430;                                      
COMPND  11 SYNONYM: CYCLIN-A;                                                   
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CDK2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: B834;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PLASMID;                                   
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX;                                     
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  12 ORGANISM_COMMON: BOVINE, COW;                                        
SOURCE  13 ORGANISM_TAXID: 9913;                                                
SOURCE  14 GENE: CCNA2, CCNA;                                                   
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: B834;                                      
SOURCE  17 EXPRESSION_SYSTEM_VECTOR: PLASMID;                                   
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET                                       
KEYWDS    SER/THR PROTEIN KINASE; TRANSFERASE; PHOSPHORYLATION; CELL            
KEYWDS   2 CYCLE, ATP-BINDING, CELL CYCLE, CELL DIVISION, KINASE,               
KEYWDS   3 MITOSIS, NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, POLYMORPHISM,           
KEYWDS   4 SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE, CYCLIN,                
KEYWDS   5 CYTOPLASM, NUCLEUS                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.ECHALIER,J.ENDICOTT                                                 
REVDAT   2   24-FEB-09 3DOG    1       VERSN                                    
REVDAT   1   30-SEP-08 3DOG    0                                                
JRNL        AUTH   K.BETTAYEB,H.SALLAM,Y.FERANDIN,F.POPOWYCZ,                   
JRNL        AUTH 2 G.FOURNET,M.HASSAN,A.ECHALIER,P.BERNARD,J.ENDICOTT,          
JRNL        AUTH 3 B.JOSEPH,L.MEIJER                                            
JRNL        TITL   N-&-N, A NEW CLASS OF CELL DEATH-INDUCING KINASE             
JRNL        TITL 2 INHIBITORS DERIVED FROM THE PURINE ROSCOVITINE.              
JRNL        REF    MOL.CANCER THER.              V.   7  2713 2008              
JRNL        REFN                   ISSN 1535-7163                               
JRNL        PMID   18790752                                                     
JRNL        DOI    10.1158/1535-7163.MCT-08-0080                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 38582                          
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) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2037                            
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) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2690                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.44                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2690                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 155                          
REMARK   3   BIN FREE R VALUE                    : 0.3150                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8803                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 233                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 7.31                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.95000                                             
REMARK   3    B22 (A**2) : -0.47000                                             
REMARK   3    B33 (A**2) : 1.42000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 1.096         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.331         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.243         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.968        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.922                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.874                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9086 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12335 ; 1.267 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1088 ; 5.712 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   392 ;39.258 ;23.980       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1592 ;16.894 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    45 ;15.905 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1405 ; 0.166 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6731 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4607 ; 0.203 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  6257 ; 0.308 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   388 ; 0.171 ; 0.200       
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):    44 ; 0.161 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.294 ; 0.200       
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):  5606 ; 0.449 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8898 ; 0.710 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3922 ; 0.827 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3437 ; 1.410 ; 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 : MASK                                                 
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: NULL                                      
REMARK   4                                                                      
REMARK   4 3DOG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUL-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB048290.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-MAR-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
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                  : SI 111                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40784                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.11600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
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: CDK2/CYCLIN A                                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, POTASSIUM             
REMARK 280  CHLORIDE, HEPES PH7.0, VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 277K                                                    
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       37.21000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       73.99800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       66.74450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       73.99800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.21000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       66.74450            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4060 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22490 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL                        
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4020 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A    38                                                      
REMARK 465     GLU B   433                                                      
REMARK 465     HIS B   434                                                      
REMARK 465     PRO C   222                                                      
REMARK 465     ASP C   223                                                      
REMARK 465     GLU C   224                                                      
REMARK 465     VAL C   225                                                      
REMARK 465     VAL C   226                                                      
REMARK 465     TRP C   227                                                      
REMARK 465     PRO C   228                                                      
REMARK 465     GLY C   229                                                      
REMARK 465     VAL C   230                                                      
REMARK 465     THR C   231                                                      
REMARK 465     SER C   232                                                      
REMARK 465     MET C   233                                                      
REMARK 465     PRO C   234                                                      
REMARK 465     ASP C   235                                                      
REMARK 465     TYR C   236                                                      
REMARK 465     LYS C   237                                                      
REMARK 465     PRO C   238                                                      
REMARK 465     SER C   239                                                      
REMARK 465     PHE C   240                                                      
REMARK 465     PRO C   241                                                      
REMARK 465     LYS C   242                                                      
REMARK 465     TRP C   243                                                      
REMARK 465     ALA C   244                                                      
REMARK 465     ARG C   245                                                      
REMARK 465     GLN C   246                                                      
REMARK 465     ASP C   247                                                      
REMARK 465     PHE C   248                                                      
REMARK 465     SER C   249                                                      
REMARK 465     LYS C   250                                                      
REMARK 465     VAL C   251                                                      
REMARK 465     LEU C   298                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   N    SER A     0     OE1  GLU A     2              2.11            
REMARK 500   O    TPO A   160     OH   TYR A   180              2.12            
REMARK 500   SG   CYS B   327     S1   SGM B   435              2.13            
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    THR C  41   N   -  CA  -  C   ANGL. DEV. = -18.6 DEGREES          
REMARK 500    GLU C  42   C   -  N   -  CA  ANGL. DEV. =  16.8 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  40      -54.96     47.73                                   
REMARK 500    THR A  41     -126.30    -61.63                                   
REMARK 500    ASP A 127       39.37   -152.45                                   
REMARK 500    ASP A 145       94.47     56.41                                   
REMARK 500    GLU A 162      104.30    -58.21                                   
REMARK 500    VAL A 164      135.39     67.46                                   
REMARK 500    SER A 181     -158.97   -139.61                                   
REMARK 500    TRP A 227       82.30   -155.64                                   
REMARK 500    PHE B 304        8.67     59.51                                   
REMARK 500    TRP B 372      107.89    -37.47                                   
REMARK 500    THR B 429      100.79     88.60                                   
REMARK 500    ASP C  38       25.34     98.59                                   
REMARK 500    THR C  41     -143.36   -100.75                                   
REMARK 500    GLU C  42      -16.22   -159.77                                   
REMARK 500    ASP C 127       45.09   -147.68                                   
REMARK 500    ASP C 145       89.67     44.45                                   
REMARK 500    GLU C 162       77.20    -65.98                                   
REMARK 500    SER C 181     -155.22   -144.60                                   
REMARK 500    THR C 290     -163.83   -126.08                                   
REMARK 500    LEU C 296      158.51     76.67                                   
REMARK 500    PHE D 304       10.29     57.90                                   
REMARK 500    TRP D 372      110.68    -37.06                                   
REMARK 500    ASN D 431      124.23     76.54                                   
REMARK 500    VAL D 432      -10.15   -172.97                                   
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 TPO A  160     HIS A  161                   56.87                    
REMARK 500 THR C   41     GLU C   42                  -45.85                    
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 RESIDUE NNN A 299                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NNN C 299                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGM B 1                   
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGM D 1                   
DBREF  3DOG A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  3DOG B  171   432  UNP    P30274   CCNA2_BOVIN    169    430             
DBREF  3DOG C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  3DOG D  171   432  UNP    P30274   CCNA2_BOVIN    169    430             
SEQADV 3DOG SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 3DOG GLU B  433  UNP  P30274              EXPRESSION TAG                 
SEQADV 3DOG HIS B  434  UNP  P30274              EXPRESSION TAG                 
SEQADV 3DOG SER C    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 3DOG GLU D  433  UNP  P30274              EXPRESSION TAG                 
SEQADV 3DOG HIS D  434  UNP  P30274              EXPRESSION TAG                 
SEQRES   1 A  299  SER MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU          
SEQRES   2 A  299  GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU          
SEQRES   3 A  299  THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP          
SEQRES   4 A  299  THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU          
SEQRES   5 A  299  ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL          
SEQRES   6 A  299  LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR          
SEQRES   7 A  299  LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE          
SEQRES   8 A  299  MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU          
SEQRES   9 A  299  ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA          
SEQRES  10 A  299  PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS          
SEQRES  11 A  299  PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS          
SEQRES  12 A  299  LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO          
SEQRES  13 A  299  VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP TYR          
SEQRES  14 A  299  ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER          
SEQRES  15 A  299  THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA          
SEQRES  16 A  299  GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER          
SEQRES  17 A  299  GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY          
SEQRES  18 A  299  THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET          
SEQRES  19 A  299  PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN          
SEQRES  20 A  299  ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY          
SEQRES  21 A  299  ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN          
SEQRES  22 A  299  LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE          
SEQRES  23 A  299  PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU          
SEQRES   1 B  264  SER VAL ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS          
SEQRES   2 B  264  THR TYR LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS          
SEQRES   3 B  264  VAL GLY TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER          
SEQRES   4 B  264  MET ARG ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY          
SEQRES   5 B  264  GLU GLU TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA          
SEQRES   6 B  264  VAL ASN TYR ILE ASP ARG PHE LEU SER SER MET SER VAL          
SEQRES   7 B  264  LEU ARG GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET          
SEQRES   8 B  264  LEU LEU ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU          
SEQRES   9 B  264  VAL ALA GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR          
SEQRES  10 B  264  LYS LYS GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS          
SEQRES  11 B  264  VAL LEU ALA PHE ASP LEU ALA ALA PRO THR ILE ASN GLN          
SEQRES  12 B  264  PHE LEU THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN          
SEQRES  13 B  264  CYS LYS VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU          
SEQRES  14 B  264  SER LEU ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO          
SEQRES  15 B  264  SER VAL ILE ALA ALA ALA ALA PHE HIS LEU ALA LEU TYR          
SEQRES  16 B  264  THR VAL THR GLY GLN SER TRP PRO GLU SER LEU VAL GLN          
SEQRES  17 B  264  LYS THR GLY TYR THR LEU GLU THR LEU LYS PRO CYS LEU          
SEQRES  18 B  264  LEU ASP LEU HIS GLN THR TYR LEU ARG ALA PRO GLN HIS          
SEQRES  19 B  264  ALA GLN GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS          
SEQRES  20 B  264  TYR HIS GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU          
SEQRES  21 B  264  ASN VAL GLU HIS                                              
SEQRES   1 C  299  SER MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU          
SEQRES   2 C  299  GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU          
SEQRES   3 C  299  THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP          
SEQRES   4 C  299  THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU          
SEQRES   5 C  299  ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL          
SEQRES   6 C  299  LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR          
SEQRES   7 C  299  LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE          
SEQRES   8 C  299  MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU          
SEQRES   9 C  299  ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA          
SEQRES  10 C  299  PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS          
SEQRES  11 C  299  PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS          
SEQRES  12 C  299  LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO          
SEQRES  13 C  299  VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP TYR          
SEQRES  14 C  299  ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER          
SEQRES  15 C  299  THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA          
SEQRES  16 C  299  GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER          
SEQRES  17 C  299  GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY          
SEQRES  18 C  299  THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET          
SEQRES  19 C  299  PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN          
SEQRES  20 C  299  ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY          
SEQRES  21 C  299  ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN          
SEQRES  22 C  299  LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE          
SEQRES  23 C  299  PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU          
SEQRES   1 D  264  SER VAL ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS          
SEQRES   2 D  264  THR TYR LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS          
SEQRES   3 D  264  VAL GLY TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER          
SEQRES   4 D  264  MET ARG ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY          
SEQRES   5 D  264  GLU GLU TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA          
SEQRES   6 D  264  VAL ASN TYR ILE ASP ARG PHE LEU SER SER MET SER VAL          
SEQRES   7 D  264  LEU ARG GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET          
SEQRES   8 D  264  LEU LEU ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU          
SEQRES   9 D  264  VAL ALA GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR          
SEQRES  10 D  264  LYS LYS GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS          
SEQRES  11 D  264  VAL LEU ALA PHE ASP LEU ALA ALA PRO THR ILE ASN GLN          
SEQRES  12 D  264  PHE LEU THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN          
SEQRES  13 D  264  CYS LYS VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU          
SEQRES  14 D  264  SER LEU ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO          
SEQRES  15 D  264  SER VAL ILE ALA ALA ALA ALA PHE HIS LEU ALA LEU TYR          
SEQRES  16 D  264  THR VAL THR GLY GLN SER TRP PRO GLU SER LEU VAL GLN          
SEQRES  17 D  264  LYS THR GLY TYR THR LEU GLU THR LEU LYS PRO CYS LEU          
SEQRES  18 D  264  LEU ASP LEU HIS GLN THR TYR LEU ARG ALA PRO GLN HIS          
SEQRES  19 D  264  ALA GLN GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS          
SEQRES  20 D  264  TYR HIS GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU          
SEQRES  21 D  264  ASN VAL GLU HIS                                              
MODRES 3DOG TPO A  160  THR  PHOSPHOTHREONINE                                   
MODRES 3DOG TPO C  160  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET    NNN  A 299      26                                                       
HET    NNN  C 299      26                                                       
HET    SGM  B   1       6                                                       
HET    SGM  B 435       6                                                       
HET    SGM  D   1       6                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     NNN (2R)-2-{[4-(BENZYLAMINO)-8-(1-METHYLETHYL)PYRAZOLO[1,            
HETNAM   2 NNN  5-A][1,3,5]TRIAZIN-2-YL]AMINO}BUTAN-1-OL                        
HETNAM     SGM MONOTHIOGLYCEROL                                                 
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   5  NNN    2(C19 H26 N6 O)                                              
FORMUL   7  SGM    3(C3 H8 O2 S)                                                
FORMUL  10  HOH   *215(H2 O)                                                    
HELIX    1   1 PRO A   45  LYS A   56  1                                  12    
HELIX    2   2 LEU A   87  SER A   94  1                                   8    
HELIX    3   3 PRO A  100  HIS A  121  1                                  22    
HELIX    4   4 LYS A  129  GLN A  131  5                                   3    
HELIX    5   5 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  252  1                                   6    
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 SER B  171  VAL B  175  5                                   5    
HELIX   15  15 TYR B  178  CYS B  193  1                                  16    
HELIX   16  16 TYR B  199  GLN B  203  5                                   5    
HELIX   17  17 THR B  207  LYS B  226  1                                  20    
HELIX   18  18 GLN B  228  SER B  244  1                                  17    
HELIX   19  19 LEU B  249  GLU B  269  1                                  21    
HELIX   20  20 GLU B  274  ILE B  281  1                                   8    
HELIX   21  21 THR B  287  LEU B  302  1                                  16    
HELIX   22  22 THR B  310  LEU B  320  1                                  11    
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 PRO C   45  LEU C   58  1                                  14    
HELIX   33  33 LEU C   87  SER C   94  1                                   8    
HELIX   34  34 PRO C  100  SER C  120  1                                  21    
HELIX   35  35 LYS C  129  GLN C  131  5                                   3    
HELIX   36  36 THR C  165  ARG C  169  5                                   5    
HELIX   37  37 ALA C  170  LEU C  175  1                                   6    
HELIX   38  38 THR C  182  ARG C  199  1                                  18    
HELIX   39  39 SER C  207  GLY C  220  1                                  14    
HELIX   40  40 ASP C  256  LEU C  267  1                                  12    
HELIX   41  41 SER C  276  LEU C  281  1                                   6    
HELIX   42  42 ALA C  282  GLN C  287  5                                   6    
HELIX   43  43 SER D  171  VAL D  175  5                                   5    
HELIX   44  44 TYR D  178  GLU D  190  1                                  13    
HELIX   45  45 TYR D  199  GLN D  203  5                                   5    
HELIX   46  46 THR D  207  TYR D  225  1                                  19    
HELIX   47  47 GLN D  228  SER D  244  1                                  17    
HELIX   48  48 LEU D  249  GLY D  251  5                                   3    
HELIX   49  49 LYS D  252  GLU D  269  1                                  18    
HELIX   50  50 GLU D  274  THR D  282  1                                   9    
HELIX   51  51 THR D  287  LEU D  302  1                                  16    
HELIX   52  52 THR D  310  PHE D  319  1                                  10    
HELIX   53  53 LEU D  320  GLN D  322  5                                   3    
HELIX   54  54 ASN D  326  LEU D  341  1                                  16    
HELIX   55  55 ASP D  343  LEU D  348  1                                   6    
HELIX   56  56 LEU D  351  THR D  368  1                                  18    
HELIX   57  57 GLU D  374  GLY D  381  1                                   8    
HELIX   58  58 THR D  383  ALA D  401  1                                  19    
HELIX   59  59 PRO D  402  HIS D  404  5                                   3    
HELIX   60  60 GLN D  407  TYR D  413  1                                   7    
HELIX   61  61 LYS D  414  HIS D  419  5                                   6    
HELIX   62  62 GLY D  420  LEU D  424  5                                   5    
SHEET    1   A 5 PHE A   4  GLY A  11  0                                        
SHEET    2   A 5 VAL A  17  ASN A  23 -1  O  LYS A  20   N  VAL A   7           
SHEET    3   A 5 VAL A  29  ARG A  36 -1  O  LEU A  32   N  TYR A  19           
SHEET    4   A 5 LYS A  75  GLU A  81 -1  O  PHE A  80   N  ALA A  31           
SHEET    5   A 5 LEU A  66  HIS A  71 -1  N  ILE A  70   O  TYR A  77           
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  GLY C  11  0                                        
SHEET    2   D 5 VAL C  17  ASN C  23 -1  O  LYS C  20   N  VAL C   7           
SHEET    3   D 5 VAL C  29  ARG C  36 -1  O  LYS C  34   N  VAL C  17           
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  ASP C  68   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  1.34  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.34  
LINK         C   TYR C 159                 N   TPO C 160     1555   1555  1.33  
LINK         C   TPO C 160                 N   HIS C 161     1555   1555  1.33  
CISPEP   1 VAL A  154    PRO A  155          0        -8.32                     
CISPEP   2 GLN B  323    PRO B  324          0        -7.48                     
CISPEP   3 ASP B  345    PRO B  346          0         2.39                     
CISPEP   4 GLU B  428    THR B  429          0        -6.48                     
CISPEP   5 LEU C   37    ASP C   38          0        16.94                     
CISPEP   6 VAL C  154    PRO C  155          0         1.74                     
CISPEP   7 GLN D  323    PRO D  324          0        -3.25                     
CISPEP   8 ASP D  345    PRO D  346          0         5.38                     
SITE     1 AC1 11 ILE A  10  GLU A  12  ALA A  31  PHE A  80                    
SITE     2 AC1 11 GLU A  81  LEU A  83  HIS A  84  GLN A  85                    
SITE     3 AC1 11 GLN A 131  ASN A 132  LEU A 134                               
SITE     1 AC2 11 ILE C  10  GLY C  11  GLU C  12  GLY C  13                    
SITE     2 AC2 11 ALA C  31  PHE C  80  GLU C  81  LEU C  83                    
SITE     3 AC2 11 HIS C  84  GLN C  85  LEU C 134                               
SITE     1 AC3  4 LYS B 192  CYS B 193  ARG B 241  ASP B 305                    
SITE     1 AC4  5 MET D 189  LYS D 192  CYS D 193  ARG D 241                    
SITE     2 AC4  5 ASP D 305                                                     
CRYST1   74.420  133.489  147.996  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      0.013437  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007491  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006757        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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