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Database: PDB
Entry: 4EOI
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Original site: 4EOI 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       14-APR-12   4EOI              
TITLE     THR 160 PHOSPHORYLATED CDK2 K89D, Q131E - HUMAN CYCLIN A3 COMPLEX WITH
TITLE    2 THE INHIBITOR RO3306                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 2;                                 
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: CELL DIVISION PROTEIN KINASE 2, P33 PROTEIN KINASE;         
COMPND   5 EC: 2.7.11.22;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CYCLIN-A2;                                                 
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 FRAGMENT: C-TERMINAL FRAGMENT;                                       
COMPND  12 SYNONYM: CYCLIN-A;                                                   
COMPND  13 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, CDKN2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: CCNA2, CCN1, CCNA;                                             
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROTEIN KINASE, CELL CYCLE, PHOSPHORYLATION, TRANSFERASE-TRANSFERASE  
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.ECHALIER,E.COT,A.CAMASSES,E.HODIMONT,F.HOH,F.SHEINERMAN,            
AUTHOR   2 L.KRASINSKA,D.FISHER                                                 
REVDAT   1   06-FEB-13 4EOI    0                                                
JRNL        AUTH   A.ECHALIER,E.COT,A.CAMASSES,E.HODIMONT,F.HOH,P.JAY,          
JRNL        AUTH 2 F.SHEINERMAN,L.KRASINSKA,D.FISHER                            
JRNL        TITL   AN INTEGRATED CHEMICAL BIOLOGY APPROACH PROVIDES INSIGHT     
JRNL        TITL 2 INTO CDK2 FUNCTIONAL REDUNDANCY AND INHIBITOR SENSITIVITY.   
JRNL        REF    CHEM.BIOL.                    V.  19  1028 2012              
JRNL        REFN                   ISSN 1074-5521                               
JRNL        PMID   22921070                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2012.06.015                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 30.39                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 93306                          
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) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4896                            
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) : 6770                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.21                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3020                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 347                          
REMARK   3   BIN FREE R VALUE                    : 0.2980                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8906                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 64                                      
REMARK   3   SOLVENT ATOMS            : 423                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.28                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.06000                                             
REMARK   3    B22 (A**2) : -0.44000                                             
REMARK   3    B33 (A**2) : 1.49000                                              
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): 0.180         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.152         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.124         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.047        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
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):  9283 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12620 ; 1.194 ; 1.985       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1118 ; 4.870 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   399 ;38.887 ;23.935       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1616 ;14.162 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    45 ;13.178 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1423 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6933 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  5590 ; 0.304 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9102 ; 0.584 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3693 ; 0.820 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3518 ; 1.360 ; 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 : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     0        A   298                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.7250  26.1040  -9.5890              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0280 T22:   0.1163                                     
REMARK   3      T33:   0.1005 T12:   0.0117                                     
REMARK   3      T13:   0.0192 T23:   0.0088                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3388 L22:   1.2057                                     
REMARK   3      L33:   1.0432 L12:   0.3613                                     
REMARK   3      L13:   0.3519 L23:   0.0875                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0337 S12:  -0.0011 S13:   0.0682                       
REMARK   3      S21:  -0.1515 S22:  -0.0171 S23:  -0.0396                       
REMARK   3      S31:   0.0545 S32:   0.0109 S33:  -0.0167                       
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   175        B   432                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.6280  -0.8390   2.8300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0821 T22:   0.1755                                     
REMARK   3      T33:   0.0570 T12:  -0.0675                                     
REMARK   3      T13:  -0.0252 T23:   0.0539                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7431 L22:   1.7816                                     
REMARK   3      L33:   1.5679 L12:   0.1360                                     
REMARK   3      L13:  -0.0247 L23:   0.2411                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0877 S12:  -0.3052 S13:  -0.1381                       
REMARK   3      S21:   0.1009 S22:  -0.0559 S23:   0.0497                       
REMARK   3      S31:   0.2940 S32:  -0.1070 S33:  -0.0318                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     0        C   296                          
REMARK   3    ORIGIN FOR THE GROUP (A): -47.4260 -13.1400 -32.8000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1997 T22:   0.1778                                     
REMARK   3      T33:   0.0704 T12:  -0.0392                                     
REMARK   3      T13:   0.0211 T23:  -0.0556                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0045 L22:   1.3782                                     
REMARK   3      L33:   0.8541 L12:   0.5350                                     
REMARK   3      L13:   0.5018 L23:   0.1150                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0268 S12:   0.1239 S13:  -0.0895                       
REMARK   3      S21:   0.0404 S22:   0.0401 S23:   0.0287                       
REMARK   3      S31:   0.1004 S32:  -0.1364 S33:  -0.0133                       
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   178        D   432                          
REMARK   3    ORIGIN FOR THE GROUP (A): -44.9340  19.9590 -34.4960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1973 T22:   0.1471                                     
REMARK   3      T33:   0.2781 T12:   0.0628                                     
REMARK   3      T13:   0.0125 T23:   0.0293                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6167 L22:   2.3470                                     
REMARK   3      L33:   1.4296 L12:   0.6102                                     
REMARK   3      L13:  -0.2212 L23:  -0.3515                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0205 S12:   0.2097 S13:   0.5378                       
REMARK   3      S21:   0.1121 S22:   0.1204 S23:   0.5869                       
REMARK   3      S31:  -0.2231 S32:  -0.2423 S33:  -0.0999                       
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 4EOI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAY-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB071874.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JUL-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : SI CHANNEL CUT                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 93306                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.390                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
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) : 2.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, POTASSIUM CHLORIDE,    
REMARK 280  HEPES, PH 7.5, 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       37.06500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.04000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       66.46500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       74.04000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.06500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       66.46500            
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: 3560 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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 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: 3380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 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     THR A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 465     THR A    41                                                      
REMARK 465     ARG C   297                                                      
REMARK 465     LEU C   298                                                      
REMARK 465     VAL D   175                                                      
REMARK 465     PRO D   176                                                      
REMARK 465     ASP D   177                                                      
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    HIS A  84   N   -  CA  -  CB  ANGL. DEV. = -11.4 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    LEU A  83     -155.02   -112.30                                   
REMARK 500    ASP A 127       45.82   -150.62                                   
REMARK 500    ASP A 145       76.26     51.98                                   
REMARK 500    VAL A 164      131.19     77.52                                   
REMARK 500    SER A 181     -153.34   -152.50                                   
REMARK 500    THR A 290     -164.30   -122.79                                   
REMARK 500    PRO B 176      179.38    -40.58                                   
REMARK 500    PHE B 304       16.37     57.46                                   
REMARK 500    TRP B 372      119.92    -32.78                                   
REMARK 500    THR C  41      -75.76   -116.86                                   
REMARK 500    LEU C  83     -122.55   -101.85                                   
REMARK 500    ASP C 127       44.01   -151.47                                   
REMARK 500    ASP C 145       74.44     55.92                                   
REMARK 500    VAL C 164      127.83     73.94                                   
REMARK 500    SER C 181     -156.66   -153.28                                   
REMARK 500    ARG C 199       -0.58     77.73                                   
REMARK 500    LEU D 430     -141.06   -120.42                                   
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 GLU C  162     VAL C  163                 -149.55                    
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 B 706        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH C 424        DISTANCE =  6.56 ANGSTROMS                       
REMARK 525    HOH D 607        DISTANCE =  6.93 ANGSTROMS                       
REMARK 525    HOH D 614        DISTANCE =  8.90 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1RO A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGM B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1RO C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGM D 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4EOJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EOK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EOL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EOM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EON   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EOO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EOP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EOQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EOR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EOS   RELATED DB: PDB                                   
DBREF  4EOI A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4EOI B  175   432  UNP    P20248   CCNA2_HUMAN    175    432             
DBREF  4EOI C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4EOI D  175   432  UNP    P20248   CCNA2_HUMAN    175    432             
SEQADV 4EOI SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 4EOI ASP A   89  UNP  P24941    LYS    89 ENGINEERED MUTATION            
SEQADV 4EOI GLU A  131  UNP  P24941    GLN   131 ENGINEERED MUTATION            
SEQADV 4EOI SER C    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 4EOI ASP C   89  UNP  P24941    LYS    89 ENGINEERED MUTATION            
SEQADV 4EOI GLU C  131  UNP  P24941    GLN   131 ENGINEERED MUTATION            
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 ASP 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 GLU 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  258  VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU ARG          
SEQRES   2 B  258  GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET          
SEQRES   3 B  258  LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE          
SEQRES   4 B  258  LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS          
SEQRES   5 B  258  LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE          
SEQRES   6 B  258  ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS          
SEQRES   7 B  258  LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER          
SEQRES   8 B  258  LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE          
SEQRES   9 B  258  VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN VAL          
SEQRES  10 B  258  LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR PHE          
SEQRES  11 B  258  ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN          
SEQRES  12 B  258  TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL GLU          
SEQRES  13 B  258  SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP          
SEQRES  14 B  258  ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE ALA          
SEQRES  15 B  258  GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY          
SEQRES  16 B  258  GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY TYR          
SEQRES  17 B  258  THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU HIS          
SEQRES  18 B  258  GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER          
SEQRES  19 B  258  ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY VAL          
SEQRES  20 B  258  SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU                  
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 ASP 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 GLU 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  258  VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR LEU ARG          
SEQRES   2 D  258  GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET          
SEQRES   3 D  258  LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE          
SEQRES   4 D  258  LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS          
SEQRES   5 D  258  LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE          
SEQRES   6 D  258  ASP ARG PHE LEU SER SER MET SER VAL LEU ARG GLY LYS          
SEQRES   7 D  258  LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER          
SEQRES   8 D  258  LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE          
SEQRES   9 D  258  VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS GLN VAL          
SEQRES  10 D  258  LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU THR PHE          
SEQRES  11 D  258  ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN          
SEQRES  12 D  258  TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL GLU          
SEQRES  13 D  258  SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP          
SEQRES  14 D  258  ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL ILE ALA          
SEQRES  15 D  258  GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY          
SEQRES  16 D  258  GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR GLY TYR          
SEQRES  17 D  258  THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP LEU HIS          
SEQRES  18 D  258  GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER          
SEQRES  19 D  258  ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS GLY VAL          
SEQRES  20 D  258  SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU                  
MODRES 4EOI TPO A  160  THR  PHOSPHOTHREONINE                                   
MODRES 4EOI TPO C  160  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET    1RO  A 301      24                                                       
HET    DMS  A 302       4                                                       
HET    SGM  B 501       6                                                       
HET    1RO  C 301      24                                                       
HET    SGM  D 501       6                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     1RO (5E)-5-(QUINOLIN-6-YLMETHYLIDENE)-2-[(THIOPHEN-2-                
HETNAM   2 1RO  YLMETHYL)AMINO]-1,3-THIAZOL-4(5H)-ONE                           
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     SGM MONOTHIOGLYCEROL                                                 
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   5  1RO    2(C18 H13 N3 O S2)                                           
FORMUL   6  DMS    C2 H6 O S                                                    
FORMUL   7  SGM    2(C3 H8 O2 S)                                                
FORMUL  10  HOH   *423(H2 O)                                                    
HELIX    1   1 SER A    0  GLU A    2  5                                   3    
HELIX    2   2 PRO A   45  LEU A   58  1                                  14    
HELIX    3   3 LEU A   87  SER A   94  1                                   8    
HELIX    4   4 PRO A  100  HIS A  121  1                                  22    
HELIX    5   5 LYS A  129  GLU A  131  5                                   3    
HELIX    6   6 ASP A  145  ALA A  149  5                                   5    
HELIX    7   7 THR A  165  ARG A  169  5                                   5    
HELIX    8   8 ALA A  170  LEU A  175  1                                   6    
HELIX    9   9 THR A  182  ARG A  199  1                                  18    
HELIX   10  10 SER A  207  GLY A  220  1                                  14    
HELIX   11  11 GLY A  229  MET A  233  5                                   5    
HELIX   12  12 ASP A  247  VAL A  252  1                                   6    
HELIX   13  13 ASP A  256  LEU A  267  1                                  12    
HELIX   14  14 SER A  276  LEU A  281  1                                   6    
HELIX   15  15 ALA A  282  GLN A  287  5                                   6    
HELIX   16  16 TYR B  178  CYS B  193  1                                  16    
HELIX   17  17 GLY B  198  GLN B  203  1                                   6    
HELIX   18  18 THR B  207  TYR B  225  1                                  19    
HELIX   19  19 GLN B  228  SER B  244  1                                  17    
HELIX   20  20 LEU B  249  GLY B  251  5                                   3    
HELIX   21  21 LYS B  252  GLU B  269  1                                  18    
HELIX   22  22 GLU B  274  ILE B  281  1                                   8    
HELIX   23  23 THR B  287  LEU B  302  1                                  16    
HELIX   24  24 THR B  310  LEU B  320  1                                  11    
HELIX   25  25 ASN B  326  ASP B  343  1                                  18    
HELIX   26  26 ASP B  343  LEU B  348  1                                   6    
HELIX   27  27 LEU B  351  THR B  368  1                                  18    
HELIX   28  28 PRO B  373  GLY B  381  1                                   9    
HELIX   29  29 THR B  383  ALA B  401  1                                  19    
HELIX   30  30 PRO B  402  HIS B  404  5                                   3    
HELIX   31  31 GLN B  407  TYR B  413  1                                   7    
HELIX   32  32 LYS B  414  HIS B  419  5                                   6    
HELIX   33  33 GLY B  420  LEU B  424  5                                   5    
HELIX   34  34 PRO C   45  LEU C   58  1                                  14    
HELIX   35  35 LEU C   87  SER C   94  1                                   8    
HELIX   36  36 PRO C  100  HIS C  121  1                                  22    
HELIX   37  37 LYS C  129  GLU C  131  5                                   3    
HELIX   38  38 ASP C  145  ALA C  149  5                                   5    
HELIX   39  39 THR C  165  ARG C  169  5                                   5    
HELIX   40  40 ALA C  170  LEU C  175  1                                   6    
HELIX   41  41 THR C  182  ARG C  199  1                                  18    
HELIX   42  42 SER C  207  GLY C  220  1                                  14    
HELIX   43  43 ASP C  247  VAL C  251  5                                   5    
HELIX   44  44 ASP C  256  LEU C  267  1                                  12    
HELIX   45  45 SER C  276  LEU C  281  1                                   6    
HELIX   46  46 ALA C  282  GLN C  287  5                                   6    
HELIX   47  47 HIS D  179  CYS D  193  1                                  15    
HELIX   48  48 TYR D  199  GLN D  203  5                                   5    
HELIX   49  49 THR D  207  TYR D  225  1                                  19    
HELIX   50  50 GLN D  228  MET D  246  1                                  19    
HELIX   51  51 LEU D  249  GLY D  251  5                                   3    
HELIX   52  52 LYS D  252  GLU D  269  1                                  18    
HELIX   53  53 GLU D  274  ILE D  281  1                                   8    
HELIX   54  54 THR D  287  LEU D  302  1                                  16    
HELIX   55  55 THR D  310  LEU D  320  1                                  11    
HELIX   56  56 ASN D  326  ASP D  343  1                                  18    
HELIX   57  57 ASP D  343  LEU D  348  1                                   6    
HELIX   58  58 LEU D  351  THR D  368  1                                  18    
HELIX   59  59 PRO D  373  GLY D  381  1                                   9    
HELIX   60  60 LEU D  387  ALA D  401  1                                  15    
HELIX   61  61 PRO D  402  HIS D  404  5                                   3    
HELIX   62  62 GLN D  407  TYR D  413  1                                   7    
HELIX   63  63 LYS D  414  HIS D  419  5                                   6    
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  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  GLU C  12  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  ILE C  70 -1  N  LEU C  67   O  VAL C  79           
SHEET    1   E 3 GLN C  85  ASP C  86  0                                        
SHEET    2   E 3 LEU C 133  ILE C 135 -1  O  ILE C 135   N  GLN C  85           
SHEET    3   E 3 ILE C 141  LEU C 143 -1  O  LYS C 142   N  LEU C 134           
SHEET    1   F 2 VAL C 123  LEU C 124  0                                        
SHEET    2   F 2 ARG C 150  ALA C 151 -1  O  ARG C 150   N  LEU C 124           
LINK         C   TYR A 159                 N   TPO A 160     1555   1555  1.33  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.33  
LINK         C   TYR C 159                 N   TPO C 160     1555   1555  1.33  
LINK         C   TPO C 160                 N   HIS C 161     1555   1555  1.33  
CISPEP   1 VAL A  154    PRO A  155          0        -5.42                     
CISPEP   2 GLN B  323    PRO B  324          0        -5.93                     
CISPEP   3 ASP B  345    PRO B  346          0         9.27                     
CISPEP   4 VAL C  154    PRO C  155          0        -3.51                     
CISPEP   5 GLN D  323    PRO D  324          0        -1.37                     
CISPEP   6 ASP D  345    PRO D  346          0         5.61                     
SITE     1 AC1 13 GLU A  12  GLY A  13  ALA A  31  LYS A  33                    
SITE     2 AC1 13 GLU A  81  PHE A  82  LEU A  83  ASP A  86                    
SITE     3 AC1 13 GLU A 131  ASN A 132  LEU A 134  ASP A 145                    
SITE     4 AC1 13 HOH A 434                                                     
SITE     1 AC2  3 ARG A 214  ARG A 217  LYS A 278                               
SITE     1 AC3  5 MET B 189  CYS B 193  ARG B 241  ASP B 305                    
SITE     2 AC3  5 HOH B 660                                                     
SITE     1 AC4 10 GLY C  13  LYS C  33  GLU C  81  PHE C  82                    
SITE     2 AC4 10 LEU C  83  ASP C  86  GLU C 131  ASN C 132                    
SITE     3 AC4 10 LEU C 134  ASP C 145                                          
SITE     1 AC5  4 LYS D 192  CYS D 193  ARG D 241  ASP D 305                    
CRYST1   74.130  132.930  148.080  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  0.007523  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006753        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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