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Entry: 3BHT
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HEADER    TRANSFERASE                             29-NOV-07   3BHT              
TITLE     STRUCTURE OF PHOSPHORYLATED THR160 CDK2/CYCLIN A IN COMPLEX WITH THE  
TITLE    2 INHIBITOR MERIOLIN 3                                                 
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_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: B834;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX;                                     
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  13 ORGANISM_COMMON: CATTLE;                                             
SOURCE  14 ORGANISM_TAXID: 9913;                                                
SOURCE  15 GENE: CCNA2, CCNA;                                                   
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: B834;                                      
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET                                       
KEYWDS    SER/THR PROTEIN KINASE, TRANSFERASE, PHOSPHORYLATION, CELL CYCLE,     
KEYWDS   2 ATP-BINDING, CELL DIVISION, MITOSIS, NUCLEOTIDE-BINDING,             
KEYWDS   3 PHOSPHOPROTEIN, SERINE/THREONINE-PROTEIN KINASE, CYCLIN              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.ECHALIER,K.BETTAYEB,Y.FERANDIN,O.LOZACH,M.CLEMENT,A.VALETTE,        
AUTHOR   2 F.LIGER,B.MARQUET,J.C.MORRIS,J.A.ENDICOTT,B.JOSEPH,L.MEIJER          
REVDAT   3   13-JUL-11 3BHT    1       VERSN                                    
REVDAT   2   24-FEB-09 3BHT    1       VERSN                                    
REVDAT   1   12-FEB-08 3BHT    0                                                
JRNL        AUTH   K.BETTAYEB,O.M.TIRADO,S.MARIONNEAU-LAMBOT,Y.FERANDIN,        
JRNL        AUTH 2 O.LOZACH,J.C.MORRIS,S.MATEO-LOZANO,P.DRUECKES,M.H.KUBBUTAT,  
JRNL        AUTH 3 F.LIGER,B.MARQUET,B.JOSEPH,A.ECHALIER,J.A.ENDICOTT,          
JRNL        AUTH 4 V.NOTARIO,L.MEIJER                                           
JRNL        TITL   MERIOLINS, A NEW CLASS OF CELL DEATH INDUCING KINASE         
JRNL        TITL 2 INHIBITORS WITH ENHANCED SELECTIVITY FOR CYCLIN-DEPENDENT    
JRNL        TITL 3 KINASES                                                      
JRNL        REF    CANCER RES.                   V.  67  8325 2007              
JRNL        REFN                   ISSN 0008-5472                               
JRNL        PMID   17804748                                                     
JRNL        DOI    10.1158/0008-5472.CAN-07-1826                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 95266                          
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) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4777                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4838                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 70.78                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2070                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 262                          
REMARK   3   BIN FREE R VALUE                    : 0.2480                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8793                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 1078                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 9.60                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.32000                                              
REMARK   3    B22 (A**2) : -1.17000                                             
REMARK   3    B33 (A**2) : 0.85000                                              
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): 0.167         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.151         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.097         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.802         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9154 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12441 ; 1.365 ; 1.984       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1111 ; 5.953 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   400 ;40.559 ;24.025       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1605 ;15.165 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    46 ;16.982 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1412 ; 0.117 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6817 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4595 ; 0.199 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  6245 ; 0.304 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   899 ; 0.173 ; 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):    65 ; 0.207 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    41 ; 0.160 ; 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):  5715 ; 0.645 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8976 ; 1.093 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3938 ; 1.654 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3455 ; 2.528 ; 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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    10        A   200                          
REMARK   3    RESIDUE RANGE :   A   260        A   280                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.8760  23.4740 -12.2240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2364 T22:  -0.0631                                     
REMARK   3      T33:  -0.1653 T12:   0.0165                                     
REMARK   3      T13:   0.0273 T23:  -0.0072                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0713 L22:   0.9633                                     
REMARK   3      L33:   1.2424 L12:   0.0601                                     
REMARK   3      L13:   0.3157 L23:  -0.0585                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0081 S12:   0.0226 S13:  -0.0179                       
REMARK   3      S21:  -0.1472 S22:   0.0049 S23:  -0.1210                       
REMARK   3      S31:   0.1201 S32:   0.0982 S33:  -0.0130                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   180        B   420                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.1510  -0.9140   2.4490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1418 T22:  -0.0408                                     
REMARK   3      T33:  -0.1577 T12:  -0.0112                                     
REMARK   3      T13:  -0.0386 T23:   0.0530                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0178 L22:   1.5093                                     
REMARK   3      L33:   1.3632 L12:  -0.1631                                     
REMARK   3      L13:  -0.2555 L23:   0.0673                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0081 S12:  -0.1319 S13:  -0.1149                       
REMARK   3      S21:  -0.0080 S22:   0.0640 S23:   0.0153                       
REMARK   3      S31:   0.2989 S32:   0.0035 S33:  -0.0560                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    10        C   200                          
REMARK   3    RESIDUE RANGE :   C   260        C   280                          
REMARK   3    ORIGIN FOR THE GROUP (A): -42.8860 -12.7710 -31.2320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0005 T22:  -0.0503                                     
REMARK   3      T33:  -0.1479 T12:   0.0044                                     
REMARK   3      T13:   0.0540 T23:  -0.0262                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8892 L22:   1.9144                                     
REMARK   3      L33:   0.8347 L12:   0.4091                                     
REMARK   3      L13:   0.3382 L23:   0.1903                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0556 S12:   0.0122 S13:  -0.0094                       
REMARK   3      S21:   0.1852 S22:  -0.0519 S23:   0.1074                       
REMARK   3      S31:   0.0839 S32:  -0.0915 S33:  -0.0036                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   180        D   420                          
REMARK   3    ORIGIN FOR THE GROUP (A): -44.5200  18.0110 -33.9240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0001 T22:  -0.0796                                     
REMARK   3      T33:  -0.0485 T12:   0.0973                                     
REMARK   3      T13:   0.0444 T23:  -0.0234                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5757 L22:   2.5196                                     
REMARK   3      L33:   1.4570 L12:   0.4338                                     
REMARK   3      L13:  -0.2500 L23:   0.1895                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0183 S12:   0.0483 S13:   0.2600                       
REMARK   3      S21:   0.1951 S22:  -0.0310 S23:   0.5297                       
REMARK   3      S31:  -0.2088 S32:  -0.1906 S33:   0.0492                       
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 3BHT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-DEC-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB045538.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-NOV-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   : 95411                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
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     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.05100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 77.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.22500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, POTASSIUM CHLORIDE,   
REMARK 280  HEPES PH7.0, VAPOR DIFFUSION, HANGING DROP, 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       37.06400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       73.91550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       66.88500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       73.91550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.06400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       66.88500            
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: 4130 ANGSTROM**2                          
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                                                                      
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: 4010 ANGSTROM**2                          
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 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     THR A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 465     GLY C    -1                                                      
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     ARG C   297                                                      
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   OG   SER B   171     O    HOH B   644              1.62            
REMARK 500   OG   SER B   171     O    HOH B   595              1.68            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH2  ARG A   297     CG2  VAL C   251     3454     2.18            
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    VAL A 163   N   -  CA  -  C   ANGL. DEV. = -17.2 DEGREES          
REMARK 500    ARG A 217   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    GLU D 174   N   -  CA  -  C   ANGL. DEV. =  27.5 DEGREES          
REMARK 500    VAL D 175   N   -  CA  -  C   ANGL. DEV. = -18.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A   0     -144.67   -147.60                                   
REMARK 500    MET A   1      -47.49    115.54                                   
REMARK 500    TYR A  15     -125.62      5.69                                   
REMARK 500    LEU A  96      -28.64     94.31                                   
REMARK 500    ASP A 127       51.08   -156.82                                   
REMARK 500    ASP A 145       90.09     58.94                                   
REMARK 500    GLU A 162      -89.73    -20.73                                   
REMARK 500    VAL A 164      133.04     78.42                                   
REMARK 500    SER A 181     -154.76   -142.00                                   
REMARK 500    THR A 290     -167.60   -129.82                                   
REMARK 500    VAL B 175       67.49     28.96                                   
REMARK 500    TRP B 372      110.91    -31.53                                   
REMARK 500    GLU C  12     -151.79   -143.79                                   
REMARK 500    THR C  14       10.39    -63.21                                   
REMARK 500    TYR C  15      -82.88   -100.98                                   
REMARK 500    THR C  41      -88.97   -133.67                                   
REMARK 500    ASP C 127       45.39   -152.40                                   
REMARK 500    ASP C 145       83.05     54.19                                   
REMARK 500    GLU C 162      -96.68    -33.94                                   
REMARK 500    VAL C 163      126.65     49.00                                   
REMARK 500    VAL C 164      124.33     70.83                                   
REMARK 500    SER C 181     -155.56   -141.45                                   
REMARK 500    THR C 290     -165.36   -119.09                                   
REMARK 500    ASP D 283     -134.78     60.58                                   
REMARK 500    PHE D 304       19.89     56.21                                   
REMARK 500    TRP D 372      113.29    -32.79                                   
REMARK 500    ASN D 431       73.11     64.06                                   
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 THR A   14     TYR A   15                   56.81                    
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 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
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    MET A   1        21.4      L          L   OUTSIDE RANGE           
REMARK 500    TYR A  15         9.6      L          L   EXPECTING SP3           
REMARK 500    HIS A 161        23.8      L          L   OUTSIDE RANGE           
REMARK 500    GLU A 162        22.8      L          L   OUTSIDE RANGE           
REMARK 500    VAL C 163        19.7      L          L   OUTSIDE RANGE           
REMARK 500    GLU D 174        11.3      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 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 509        DISTANCE =  5.31 ANGSTROMS                       
REMARK 525    HOH B 434        DISTANCE =  5.76 ANGSTROMS                       
REMARK 525    HOH B 573        DISTANCE =  6.52 ANGSTROMS                       
REMARK 525    HOH C 344        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH C 402        DISTANCE =  7.07 ANGSTROMS                       
REMARK 525    HOH C 426        DISTANCE =  5.30 ANGSTROMS                       
REMARK 525    HOH C 477        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH D 665        DISTANCE =  5.36 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B   1  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN B 203   O                                                      
REMARK 620 2 ILE B 206   O    99.2                                              
REMARK 620 3 HOH B 640   O   163.2  96.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D   2  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN D 203   O                                                      
REMARK 620 2 HOH D 615   O   177.6                                              
REMARK 620 3 HOH D 623   O    88.2  89.7                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MFR A 299                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MFR C 299                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGM B 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGM B 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGM D 3                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3BHU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3BHV   RELATED DB: PDB                                   
DBREF  3BHT A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  3BHT B  171   432  UNP    P30274   CCNA2_BOVIN    169    430             
DBREF  3BHT C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  3BHT D  171   432  UNP    P30274   CCNA2_BOVIN    169    430             
SEQADV 3BHT GLY A   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 3BHT SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 3BHT GLY C   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 3BHT SER C    0  UNP  P24941              EXPRESSION TAG                 
SEQRES   1 A  300  GLY SER MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY          
SEQRES   2 A  300  GLU GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS          
SEQRES   3 A  300  LEU THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU          
SEQRES   4 A  300  ASP THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG          
SEQRES   5 A  300  GLU ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE          
SEQRES   6 A  300  VAL LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU          
SEQRES   7 A  300  TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS          
SEQRES   8 A  300  PHE MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO          
SEQRES   9 A  300  LEU ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU          
SEQRES  10 A  300  ALA PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU          
SEQRES  11 A  300  LYS PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE          
SEQRES  12 A  300  LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL          
SEQRES  13 A  300  PRO VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP          
SEQRES  14 A  300  TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR          
SEQRES  15 A  300  SER THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE          
SEQRES  16 A  300  ALA GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP          
SEQRES  17 A  300  SER GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU          
SEQRES  18 A  300  GLY THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER          
SEQRES  19 A  300  MET PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG          
SEQRES  20 A  300  GLN ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP          
SEQRES  21 A  300  GLY ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO          
SEQRES  22 A  300  ASN LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO          
SEQRES  23 A  300  PHE PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG          
SEQRES  24 A  300  LEU                                                          
SEQRES   1 B  262  SER VAL ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS          
SEQRES   2 B  262  THR TYR LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS          
SEQRES   3 B  262  VAL GLY TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER          
SEQRES   4 B  262  MET ARG ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY          
SEQRES   5 B  262  GLU GLU TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA          
SEQRES   6 B  262  VAL ASN TYR ILE ASP ARG PHE LEU SER SER MET SER VAL          
SEQRES   7 B  262  LEU ARG GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET          
SEQRES   8 B  262  LEU LEU ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU          
SEQRES   9 B  262  VAL ALA GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR          
SEQRES  10 B  262  LYS LYS GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS          
SEQRES  11 B  262  VAL LEU ALA PHE ASP LEU ALA ALA PRO THR ILE ASN GLN          
SEQRES  12 B  262  PHE LEU THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN          
SEQRES  13 B  262  CYS LYS VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU          
SEQRES  14 B  262  SER LEU ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO          
SEQRES  15 B  262  SER VAL ILE ALA ALA ALA ALA PHE HIS LEU ALA LEU TYR          
SEQRES  16 B  262  THR VAL THR GLY GLN SER TRP PRO GLU SER LEU VAL GLN          
SEQRES  17 B  262  LYS THR GLY TYR THR LEU GLU THR LEU LYS PRO CYS LEU          
SEQRES  18 B  262  LEU ASP LEU HIS GLN THR TYR LEU ARG ALA PRO GLN HIS          
SEQRES  19 B  262  ALA GLN GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS          
SEQRES  20 B  262  TYR HIS GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU          
SEQRES  21 B  262  ASN VAL                                                      
SEQRES   1 C  300  GLY SER MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY          
SEQRES   2 C  300  GLU GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS          
SEQRES   3 C  300  LEU THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU          
SEQRES   4 C  300  ASP THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG          
SEQRES   5 C  300  GLU ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE          
SEQRES   6 C  300  VAL LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU          
SEQRES   7 C  300  TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS          
SEQRES   8 C  300  PHE MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO          
SEQRES   9 C  300  LEU ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU          
SEQRES  10 C  300  ALA PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU          
SEQRES  11 C  300  LYS PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE          
SEQRES  12 C  300  LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL          
SEQRES  13 C  300  PRO VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP          
SEQRES  14 C  300  TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR          
SEQRES  15 C  300  SER THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE          
SEQRES  16 C  300  ALA GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP          
SEQRES  17 C  300  SER GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU          
SEQRES  18 C  300  GLY THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER          
SEQRES  19 C  300  MET PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG          
SEQRES  20 C  300  GLN ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP          
SEQRES  21 C  300  GLY ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO          
SEQRES  22 C  300  ASN LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO          
SEQRES  23 C  300  PHE PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG          
SEQRES  24 C  300  LEU                                                          
SEQRES   1 D  262  SER VAL ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS          
SEQRES   2 D  262  THR TYR LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS          
SEQRES   3 D  262  VAL GLY TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER          
SEQRES   4 D  262  MET ARG ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY          
SEQRES   5 D  262  GLU GLU TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA          
SEQRES   6 D  262  VAL ASN TYR ILE ASP ARG PHE LEU SER SER MET SER VAL          
SEQRES   7 D  262  LEU ARG GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET          
SEQRES   8 D  262  LEU LEU ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU          
SEQRES   9 D  262  VAL ALA GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR          
SEQRES  10 D  262  LYS LYS GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS          
SEQRES  11 D  262  VAL LEU ALA PHE ASP LEU ALA ALA PRO THR ILE ASN GLN          
SEQRES  12 D  262  PHE LEU THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN          
SEQRES  13 D  262  CYS LYS VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU          
SEQRES  14 D  262  SER LEU ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO          
SEQRES  15 D  262  SER VAL ILE ALA ALA ALA ALA PHE HIS LEU ALA LEU TYR          
SEQRES  16 D  262  THR VAL THR GLY GLN SER TRP PRO GLU SER LEU VAL GLN          
SEQRES  17 D  262  LYS THR GLY TYR THR LEU GLU THR LEU LYS PRO CYS LEU          
SEQRES  18 D  262  LEU ASP LEU HIS GLN THR TYR LEU ARG ALA PRO GLN HIS          
SEQRES  19 D  262  ALA GLN GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS          
SEQRES  20 D  262  TYR HIS GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU          
SEQRES  21 D  262  ASN VAL                                                      
MODRES 3BHT TPO A  160  THR  PHOSPHOTHREONINE                                   
MODRES 3BHT TPO C  160  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET     MG  B   1       1                                                       
HET     MG  D   2       1                                                       
HET    MFR  A 299      18                                                       
HET    MFR  C 299      18                                                       
HET    SGM  B   4       6                                                       
HET    SGM  B   5       6                                                       
HET    SGM  D   3       6                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     MFR 4-(4-METHOXY-1H-PYRROLO[2,3-B]PYRIDIN-3-YL)PYRIMIDIN-2-          
HETNAM   2 MFR  AMINE                                                           
HETNAM     SGM MONOTHIOGLYCEROL                                                 
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   5   MG    2(MG 2+)                                                     
FORMUL   7  MFR    2(C12 H11 N5 O)                                              
FORMUL   9  SGM    3(C3 H8 O2 S)                                                
FORMUL  12  HOH   *1078(H2 O)                                                   
HELIX    1   1 PRO A   45  LEU A   58  1                                  14    
HELIX    2   2 LEU A   87  SER A   94  1                                   8    
HELIX    3   3 PRO A  100  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 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  TYR B  225  1                                  19    
HELIX   18  18 GLN B  228  MET B  246  1                                  19    
HELIX   19  19 LEU B  249  GLY B  251  5                                   3    
HELIX   20  20 LYS B  252  GLU B  269  1                                  18    
HELIX   21  21 GLU B  274  ILE B  281  1                                   8    
HELIX   22  22 THR B  287  LEU B  302  1                                  16    
HELIX   23  23 THR B  310  LEU B  320  1                                  11    
HELIX   24  24 ASN B  326  ASP B  343  1                                  18    
HELIX   25  25 ASP B  343  LEU B  348  1                                   6    
HELIX   26  26 LEU B  351  GLY B  369  1                                  19    
HELIX   27  27 PRO B  373  GLY B  381  1                                   9    
HELIX   28  28 THR B  383  ALA B  401  1                                  19    
HELIX   29  29 PRO B  402  HIS B  404  5                                   3    
HELIX   30  30 GLN B  407  TYR B  413  1                                   7    
HELIX   31  31 LYS B  414  HIS B  419  5                                   6    
HELIX   32  32 GLY B  420  LEU B  424  5                                   5    
HELIX   33  33 PRO C   45  LEU C   58  1                                  14    
HELIX   34  34 LEU C   87  SER C   94  1                                   8    
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 ASP C  256  LEU C  267  1                                  12    
HELIX   42  42 SER C  276  ALA C  282  1                                   7    
HELIX   43  43 HIS C  283  GLN C  287  5                                   5    
HELIX   44  44 TYR D  178  CYS D  193  1                                  16    
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  GLU D  269  1                                  21    
HELIX   49  49 GLU D  274  THR D  282  1                                   9    
HELIX   50  50 THR D  287  LEU D  302  1                                  16    
HELIX   51  51 THR D  310  PHE D  319  1                                  10    
HELIX   52  52 LEU D  320  GLN D  322  5                                   3    
HELIX   53  53 ASN D  326  ASP D  343  1                                  18    
HELIX   54  54 ASP D  343  LEU D  348  1                                   6    
HELIX   55  55 LEU D  351  GLY D  369  1                                  19    
HELIX   56  56 PRO D  373  GLY D  381  1                                   9    
HELIX   57  57 THR D  383  ALA D  401  1                                  19    
HELIX   58  58 PRO D  402  HIS D  404  5                                   3    
HELIX   59  59 GLN D  407  TYR D  413  1                                   7    
HELIX   60  60 LYS D  414  HIS D  419  5                                   6    
HELIX   61  61 GLY D  420  LEU D  424  5                                   5    
SHEET    1   A 5 PHE A   4  GLU A  12  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  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  GLY C  11  0                                        
SHEET    2   D 5 GLY C  16  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  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         O   GLN B 203                MG    MG B   1     1555   1555  2.31  
LINK         O   ILE B 206                MG    MG B   1     1555   1555  2.49  
LINK         O   GLN D 203                MG    MG D   2     1555   1555  2.14  
LINK        MG    MG B   1                 O   HOH B 640     1555   1555  2.40  
LINK        MG    MG D   2                 O   HOH D 615     1555   1555  2.48  
LINK        MG    MG D   2                 O   HOH D 623     1555   1555  2.29  
LINK         C   TYR A 159                 N   TPO A 160     1555   1555  1.31  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.31  
LINK         C   TYR C 159                 N   TPO C 160     1555   1555  1.31  
LINK         C   TPO C 160                 N   HIS C 161     1555   1555  1.30  
CISPEP   1 GLY A   -1    SER A    0          0        -0.21                     
CISPEP   2 TYR A   15    GLY A   16          0        -8.00                     
CISPEP   3 VAL A  154    PRO A  155          0        -2.82                     
CISPEP   4 GLU A  162    VAL A  163          0       -23.09                     
CISPEP   5 GLN B  323    PRO B  324          0        -4.59                     
CISPEP   6 ASP B  345    PRO B  346          0         6.54                     
CISPEP   7 TYR C   15    GLY C   16          0        -5.98                     
CISPEP   8 VAL C  154    PRO C  155          0        -3.65                     
CISPEP   9 GLU D  174    VAL D  175          0       -13.99                     
CISPEP  10 GLN D  323    PRO D  324          0        -4.31                     
CISPEP  11 ASP D  345    PRO D  346          0         9.88                     
SITE     1 AC1  5 MET B 200  GLN B 203  ILE B 206  HOH B 640                    
SITE     2 AC1  5 HOH B 669                                                     
SITE     1 AC2  6 MET D 200  GLN D 203  ILE D 206  HOH D 615                    
SITE     2 AC2  6 HOH D 623  HOH D 647                                          
SITE     1 AC3 10 ILE A  10  ALA A  31  LYS A  33  GLU A  51                    
SITE     2 AC3 10 VAL A  64  PHE A  80  GLU A  81  LEU A  83                    
SITE     3 AC3 10 LEU A 134  ASP A 145                                          
SITE     1 AC4  8 ALA C  31  LYS C  33  GLU C  51  PHE C  80                    
SITE     2 AC4  8 GLU C  81  LEU C  83  LEU C 134  ASP C 145                    
SITE     1 AC5  7 HOH A 368  MET B 189  CYS B 193  ARG B 241                    
SITE     2 AC5  7 ASP B 305  HOH B 642  HOH B 650                               
SITE     1 AC6  4 CYS B 327  GLU B 330  HOH B 656  HOH B 707                    
SITE     1 AC7  4 LYS D 192  CYS D 193  ARG D 241  ASP D 305                    
CRYST1   74.128  133.770  147.831  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      0.013490  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007475  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006764        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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