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Database: PDB
Entry: 3F5X
LinkDB: 3F5X
Original site: 3F5X 
HEADER    TRANSFERASE/CELL CYCLE                  04-NOV-08   3F5X              
TITLE     CDK-2-CYCLIN COMPLEX WITH INDAZOLE INHIBITOR 9 BOUND AT ITS ACTIVE    
TITLE    2 SITE                                                                 
CAVEAT     3F5X    CHIRALITY ERRORS AT CA OF THR C97, VAL C163                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION PROTEIN KINASE 2;                            
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: P33 PROTEIN KINASE;                                         
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 177-432;                                      
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 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: SPODOPTERA FRUGIPERDA;                            
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    KINASE, PKC, PROTEIN KINASE, INHIBITOR, ATP-BINDING, CELL CYCLE, CELL 
KEYWDS   2 DIVISION, MITOSIS, NUCLEOTIDE-BINDING, PHOSPHOPROTEIN,               
KEYWDS   3 SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE, CYCLIN, NUCLEUS,       
KEYWDS   4 TRANSFERASE-CELL CYCLE COMPLEX                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.R.KIEFER,J.E.DAY,N.L.CASPERS,K.J.MATHIS,K.K.KRETZMER,R.A.WEINBERG,  
AUTHOR   2 B.A.REITZ,R.A.STEGEMAN,J.I.TRUJILLO,W.HUANG,A.THORARENSEN,L.XING,    
AUTHOR   3 A.WRIGHTSTONE,L.CHRISTINE,R.COMPTON,X.LI                             
REVDAT   2   13-JUL-11 3F5X    1       VERSN                                    
REVDAT   1   03-FEB-09 3F5X    0                                                
JRNL        AUTH   J.I.TRUJILLO,J.R.KIEFER,W.HUANG,A.THORARENSEN,L.XING,        
JRNL        AUTH 2 N.L.CASPERS,J.E.DAY,K.J.MATHIS,K.K.KRETZMER,B.A.REITZ,       
JRNL        AUTH 3 R.A.WEINBERG,R.A.STEGEMAN,A.WRIGHTSTONE,L.CHRISTINE,         
JRNL        AUTH 4 R.COMPTON,X.LI                                               
JRNL        TITL   2-(6-PHENYL-1H-INDAZOL-3-YL)-1H-BENZO[D]IMIDAZOLES: DESIGN   
JRNL        TITL 2 AND SYNTHESIS OF A POTENT AND ISOFORM SELECTIVE PKC-ZETA     
JRNL        TITL 3 INHIBITOR.                                                   
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  19   908 2009              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   19097791                                                     
JRNL        DOI    10.1016/J.BMCL.2008.11.105                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 83276                          
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) : 0.266                           
REMARK   3   R VALUE            (WORKING SET) : 0.266                           
REMARK   3   FREE R VALUE                     : 0.283                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4169                            
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5847                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3410                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 291                          
REMARK   3   BIN FREE R VALUE                    : 0.3480                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8920                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 81                                      
REMARK   3   SOLVENT ATOMS            : 68                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.98                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.98000                                              
REMARK   3    B22 (A**2) : 0.98000                                              
REMARK   3    B33 (A**2) : -1.48000                                             
REMARK   3    B12 (A**2) : 0.49000                                              
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): 0.299         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.234         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.198         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.656         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.910                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.894                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9229 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  6256 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12533 ; 1.155 ; 1.988       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 15317 ; 1.231 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1101 ; 6.526 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   394 ;39.217 ;23.858       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1622 ;16.031 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    46 ;17.446 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1408 ; 0.174 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10069 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1805 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1993 ; 0.204 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  6213 ; 0.182 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4536 ; 0.179 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  4532 ; 0.088 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   197 ; 0.146 ; 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):    12 ; 0.113 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    64 ; 0.197 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.188 ; 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):  5780 ; 0.518 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2194 ; 0.085 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9011 ; 0.902 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4024 ; 0.933 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3522 ; 1.484 ; 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 : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     10       A     285      2                      
REMARK   3           1     C     10       C     285      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1617 ; 0.050 ; 0.050           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   2145 ; 0.430 ; 0.500           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1617 ; 0.090 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   2145 ; 0.380 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B    185       B     420      2                      
REMARK   3           1     D    185       D     420      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    B    (A):   1396 ; 0.040 ; 0.050           
REMARK   3   MEDIUM POSITIONAL  2    B    (A):   1832 ; 0.410 ; 0.500           
REMARK   3   TIGHT THERMAL      2    B (A**2):   1396 ; 0.080 ; 0.500           
REMARK   3   MEDIUM THERMAL     2    B (A**2):   1832 ; 0.370 ; 2.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3F5X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-NOV-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB050186.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-DEC-06                          
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               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 94535                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09200                            
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 4000, 50MM HEPES PH 7.5, 50MM    
REMARK 280  AMMONIUM ACETATE, 10 MM DTT, VAPOR DIFFUSION, TEMPERATURE 291K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+2/3                                            
REMARK 290       6555   X-Y,X,Z+1/3                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+2/3                                            
REMARK 290      11555   -X+Y,Y,-Z                                               
REMARK 290      12555   X,X-Y,-Z+1/3                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      143.23200            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       71.61600            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      143.23200            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       71.61600            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      143.23200            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       71.61600            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      143.23200            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       71.61600            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 18730 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 90290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.500000  0.866025  0.000000       92.02550            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000     -159.39284            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000     -143.23200            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   3  0.500000 -0.866025  0.000000       92.02550            
REMARK 350   BIOMT2   3  0.866025  0.500000  0.000000     -159.39284            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000     -143.23200            
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8770 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 45740 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: 23860 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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: 4                                                       
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: 3440 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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     ASN A   272                                                      
REMARK 465     ASP D   177                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  42      -33.17   -133.83                                   
REMARK 500    LEU A  58       78.82   -117.21                                   
REMARK 500    THR A  72     -159.51   -135.70                                   
REMARK 500    GLU A  73      -77.44    -35.45                                   
REMARK 500    LEU A  96       33.10    -89.95                                   
REMARK 500    THR A  97      -20.31   -176.05                                   
REMARK 500    ASP A 127       40.15   -147.58                                   
REMARK 500    ASP A 145       79.18     51.69                                   
REMARK 500    HIS A 161     -108.90    -79.10                                   
REMARK 500    VAL A 164      102.57      3.68                                   
REMARK 500    THR A 165      146.61    -38.96                                   
REMARK 500    ASP A 288       27.12   -141.22                                   
REMARK 500    TRP B 372      109.25    -32.42                                   
REMARK 500    GLU C  42      -42.49   -131.09                                   
REMARK 500    LEU C  58       77.16   -119.03                                   
REMARK 500    GLU C  73      -79.07    -33.02                                   
REMARK 500    LEU C  96       42.93    -90.18                                   
REMARK 500    THR C  97       21.60    149.16                                   
REMARK 500    ARG C 126       -0.68     74.61                                   
REMARK 500    ASP C 127       42.21   -148.96                                   
REMARK 500    ASP C 145       80.85     51.86                                   
REMARK 500    HIS C 161     -122.70    -79.94                                   
REMARK 500    VAL C 163     -152.44    133.52                                   
REMARK 500    VAL C 164       96.30      7.07                                   
REMARK 500    THR C 165      145.34    -36.48                                   
REMARK 500    TRP D 372      107.13    -32.93                                   
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 HIS A  161     GLU A  162                 -118.23                    
REMARK 500 HIS C  161     GLU C  162                  -86.20                    
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    THR C  97        -7.3      L          D   EXPECTING SP3           
REMARK 500    THR C 158        22.6      L          L   OUTSIDE RANGE           
REMARK 500    TYR C 159        11.6      L          L   OUTSIDE RANGE           
REMARK 500    THR C 160        10.2      L          L   OUTSIDE RANGE           
REMARK 500    VAL C 163       -17.0      L          D   WRONG HAND              
REMARK 500    TYR D 280         4.4      L          L   EXPECTING SP3           
REMARK 500    MET D 392        14.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 299                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EZV A 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 299                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EZV C 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1                   
DBREF  3F5X A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  3F5X B  177   432  UNP    P20248   CCNA2_HUMAN    177    432             
DBREF  3F5X C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  3F5X D  177   432  UNP    P20248   CCNA2_HUMAN    177    432             
SEQRES   1 A  298  MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY          
SEQRES   2 A  298  THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR          
SEQRES   3 A  298  GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR          
SEQRES   4 A  298  GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 A  298  SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS          
SEQRES   6 A  298  LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU          
SEQRES   7 A  298  VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET          
SEQRES   8 A  298  ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE          
SEQRES   9 A  298  LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE          
SEQRES  10 A  298  CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  11 A  298  GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU          
SEQRES  12 A  298  ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL          
SEQRES  13 A  298  ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP TYR ARG          
SEQRES  14 A  298  ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR          
SEQRES  15 A  298  ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU          
SEQRES  16 A  298  MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU          
SEQRES  17 A  298  ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR          
SEQRES  18 A  298  PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO          
SEQRES  19 A  298  ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP          
SEQRES  20 A  298  PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG          
SEQRES  21 A  298  SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS          
SEQRES  22 A  298  ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE          
SEQRES  23 A  298  GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU              
SEQRES   1 B  256  ASP TYR HIS GLU ASP ILE HIS THR TYR LEU ARG GLU MET          
SEQRES   2 B  256  GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET LYS LYS          
SEQRES   3 B  256  GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE LEU VAL          
SEQRES   4 B  256  ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS LEU GLN          
SEQRES   5 B  256  ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE ASP ARG          
SEQRES   6 B  256  PHE LEU SER SER MET SER VAL LEU ARG GLY LYS LEU GLN          
SEQRES   7 B  256  LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER LYS PHE          
SEQRES   8 B  256  GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE VAL TYR          
SEQRES   9 B  256  ILE THR ASP ASP THR TYR THR LYS LYS GLN VAL LEU ARG          
SEQRES  10 B  256  MET GLU HIS LEU VAL LEU LYS VAL LEU THR PHE ASP LEU          
SEQRES  11 B  256  ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN TYR PHE          
SEQRES  12 B  256  LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL GLU SER LEU          
SEQRES  13 B  256  ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP ALA ASP          
SEQRES  14 B  256  PRO TYR LEU LYS TYR LEU PRO SER VAL ILE ALA GLY ALA          
SEQRES  15 B  256  ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY GLN SER          
SEQRES  16 B  256  TRP PRO GLU SER LEU ILE ARG LYS THR GLY TYR THR LEU          
SEQRES  17 B  256  GLU SER LEU LYS PRO CYS LEU MET ASP LEU HIS GLN THR          
SEQRES  18 B  256  TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER ILE ARG          
SEQRES  19 B  256  GLU LYS TYR LYS ASN SER LYS TYR HIS GLY VAL SER LEU          
SEQRES  20 B  256  LEU ASN PRO PRO GLU THR LEU ASN LEU                          
SEQRES   1 C  298  MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY          
SEQRES   2 C  298  THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR          
SEQRES   3 C  298  GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR          
SEQRES   4 C  298  GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 C  298  SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS          
SEQRES   6 C  298  LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU          
SEQRES   7 C  298  VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET          
SEQRES   8 C  298  ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE          
SEQRES   9 C  298  LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE          
SEQRES  10 C  298  CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  11 C  298  GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU          
SEQRES  12 C  298  ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL          
SEQRES  13 C  298  ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP TYR ARG          
SEQRES  14 C  298  ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR          
SEQRES  15 C  298  ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU          
SEQRES  16 C  298  MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU          
SEQRES  17 C  298  ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR          
SEQRES  18 C  298  PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO          
SEQRES  19 C  298  ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP          
SEQRES  20 C  298  PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG          
SEQRES  21 C  298  SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS          
SEQRES  22 C  298  ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE          
SEQRES  23 C  298  GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU              
SEQRES   1 D  256  ASP TYR HIS GLU ASP ILE HIS THR TYR LEU ARG GLU MET          
SEQRES   2 D  256  GLU VAL LYS CYS LYS PRO LYS VAL GLY TYR MET LYS LYS          
SEQRES   3 D  256  GLN PRO ASP ILE THR ASN SER MET ARG ALA ILE LEU VAL          
SEQRES   4 D  256  ASP TRP LEU VAL GLU VAL GLY GLU GLU TYR LYS LEU GLN          
SEQRES   5 D  256  ASN GLU THR LEU HIS LEU ALA VAL ASN TYR ILE ASP ARG          
SEQRES   6 D  256  PHE LEU SER SER MET SER VAL LEU ARG GLY LYS LEU GLN          
SEQRES   7 D  256  LEU VAL GLY THR ALA ALA MET LEU LEU ALA SER LYS PHE          
SEQRES   8 D  256  GLU GLU ILE TYR PRO PRO GLU VAL ALA GLU PHE VAL TYR          
SEQRES   9 D  256  ILE THR ASP ASP THR TYR THR LYS LYS GLN VAL LEU ARG          
SEQRES  10 D  256  MET GLU HIS LEU VAL LEU LYS VAL LEU THR PHE ASP LEU          
SEQRES  11 D  256  ALA ALA PRO THR VAL ASN GLN PHE LEU THR GLN TYR PHE          
SEQRES  12 D  256  LEU HIS GLN GLN PRO ALA ASN CYS LYS VAL GLU SER LEU          
SEQRES  13 D  256  ALA MET PHE LEU GLY GLU LEU SER LEU ILE ASP ALA ASP          
SEQRES  14 D  256  PRO TYR LEU LYS TYR LEU PRO SER VAL ILE ALA GLY ALA          
SEQRES  15 D  256  ALA PHE HIS LEU ALA LEU TYR THR VAL THR GLY GLN SER          
SEQRES  16 D  256  TRP PRO GLU SER LEU ILE ARG LYS THR GLY TYR THR LEU          
SEQRES  17 D  256  GLU SER LEU LYS PRO CYS LEU MET ASP LEU HIS GLN THR          
SEQRES  18 D  256  TYR LEU LYS ALA PRO GLN HIS ALA GLN GLN SER ILE ARG          
SEQRES  19 D  256  GLU LYS TYR LYS ASN SER LYS TYR HIS GLY VAL SER LEU          
SEQRES  20 D  256  LEU ASN PRO PRO GLU THR LEU ASN LEU                          
HET    GOL  A 299       6                                                       
HET    EZV  A 300      32                                                       
HET    GOL  C 299       6                                                       
HET    EZV  C 300      32                                                       
HET    SO4  D   1       5                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     EZV 4-{3-[7-(4-METHYLPIPERAZIN-1-YL)-1H-BENZIMIDAZOL-2-YL]-          
HETNAM   2 EZV  1H-INDAZOL-6-YL}ANILINE                                         
HETNAM     SO4 SULFATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  GOL    2(C3 H8 O3)                                                  
FORMUL   6  EZV    2(C25 H25 N7)                                                
FORMUL   9  SO4    O4 S 2-                                                      
FORMUL  10  HOH   *68(H2 O)                                                     
HELIX    1   1 PRO A   45  LYS A   56  1                                  12    
HELIX    2   2 LEU A   87  SER A   94  1                                   8    
HELIX    3   3 PRO A  100  HIS A  121  1                                  22    
HELIX    4   4 LYS A  129  GLN A  131  5                                   3    
HELIX    5   5 THR A  165  ARG A  169  5                                   5    
HELIX    6   6 ALA A  170  LEU A  175  1                                   6    
HELIX    7   7 THR A  182  ARG A  199  1                                  18    
HELIX    8   8 SER A  207  GLY A  220  1                                  14    
HELIX    9   9 GLY A  229  MET A  233  5                                   5    
HELIX   10  10 ASP A  247  VAL A  252  1                                   6    
HELIX   11  11 ASP A  256  LEU A  267  1                                  12    
HELIX   12  12 SER A  276  ALA A  282  1                                   7    
HELIX   13  13 HIS A  283  GLN A  287  5                                   5    
HELIX   14  14 TYR B  178  CYS B  193  1                                  16    
HELIX   15  15 THR B  207  TYR B  225  1                                  19    
HELIX   16  16 GLN B  228  SER B  244  1                                  17    
HELIX   17  17 LEU B  249  GLY B  251  5                                   3    
HELIX   18  18 LYS B  252  GLU B  269  1                                  18    
HELIX   19  19 GLU B  274  THR B  282  1                                   9    
HELIX   20  20 THR B  287  THR B  303  1                                  17    
HELIX   21  21 THR B  310  LEU B  320  1                                  11    
HELIX   22  22 ASN B  326  SER B  340  1                                  15    
HELIX   23  23 ASP B  343  LEU B  348  1                                   6    
HELIX   24  24 LEU B  351  GLY B  369  1                                  19    
HELIX   25  25 PRO B  373  GLY B  381  1                                   9    
HELIX   26  26 THR B  383  ALA B  401  1                                  19    
HELIX   27  27 PRO B  402  HIS B  404  5                                   3    
HELIX   28  28 GLN B  407  LYS B  414  1                                   8    
HELIX   29  29 ASN B  415  HIS B  419  5                                   5    
HELIX   30  30 GLY B  420  LEU B  424  5                                   5    
HELIX   31  31 PRO C   45  LYS C   56  1                                  12    
HELIX   32  32 LEU C   87  SER C   94  1                                   8    
HELIX   33  33 PRO C  100  HIS C  121  1                                  22    
HELIX   34  34 LYS C  129  GLN C  131  5                                   3    
HELIX   35  35 THR C  165  ARG C  169  5                                   5    
HELIX   36  36 ALA C  170  LEU C  175  1                                   6    
HELIX   37  37 THR C  182  ARG C  199  1                                  18    
HELIX   38  38 SER C  207  GLY C  220  1                                  14    
HELIX   39  39 GLY C  229  MET C  233  5                                   5    
HELIX   40  40 ASP C  247  VAL C  252  1                                   6    
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 THR D  207  TYR D  225  1                                  19    
HELIX   46  46 GLN D  228  SER D  244  1                                  17    
HELIX   47  47 LEU D  249  GLY D  251  5                                   3    
HELIX   48  48 LYS D  252  GLU D  269  1                                  18    
HELIX   49  49 GLU D  274  THR D  282  1                                   9    
HELIX   50  50 THR D  287  THR D  303  1                                  17    
HELIX   51  51 THR D  310  LEU D  320  1                                  11    
HELIX   52  52 ASN D  326  SER D  340  1                                  15    
HELIX   53  53 ASP D  343  LEU D  348  1                                   6    
HELIX   54  54 LEU D  351  GLY D  369  1                                  19    
HELIX   55  55 PRO D  373  GLY D  381  1                                   9    
HELIX   56  56 THR D  383  ALA D  401  1                                  19    
HELIX   57  57 PRO D  402  HIS D  404  5                                   3    
HELIX   58  58 GLN D  407  LYS D  414  1                                   8    
HELIX   59  59 ASN D  415  HIS D  419  5                                   5    
HELIX   60  60 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  VAL A  18   N  GLY A  11           
SHEET    3   A 5 VAL A  29  ARG A  36 -1  O  VAL A  30   N  ALA A  21           
SHEET    4   A 5 LYS A  75  GLU A  81 -1  O  PHE A  80   N  ALA A  31           
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  GLU C  12  0                                        
SHEET    2   D 5 VAL C  17  ASN C  23 -1  O  LYS C  20   N  GLU C   8           
SHEET    3   D 5 VAL C  29  ARG C  36 -1  O  VAL C  30   N  ALA C  21           
SHEET    4   D 5 LYS C  75  GLU C  81 -1  O  PHE C  80   N  ALA C  31           
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           
CISPEP   1 GLN B  323    PRO B  324          0       -10.79                     
CISPEP   2 ASP B  345    PRO B  346          0         6.37                     
CISPEP   3 GLN D  323    PRO D  324          0        -9.47                     
CISPEP   4 ASP D  345    PRO D  346          0         5.22                     
SITE     1 AC1  8 PHE A   4  ASN A  23  GLU A  28  LEU A  67                    
SITE     2 AC1  8 VAL A  79  HOH A 302  SER D 245  MET D 246                    
SITE     1 AC2 16 ILE A  10  ALA A  31  LYS A  33  GLU A  51                    
SITE     2 AC2 16 LEU A  55  PHE A  80  GLU A  81  PHE A  82                    
SITE     3 AC2 16 LEU A  83  HIS A  84  ASP A  86  LYS A  89                    
SITE     4 AC2 16 LEU A 134  ALA A 144  ASP A 145  PHE A 146                    
SITE     1 AC3  4 PHE C   4  ASN C  23  GLU C  28  ASP C  68                    
SITE     1 AC4 15 ILE C  10  ALA C  31  LYS C  33  GLU C  51                    
SITE     2 AC4 15 LEU C  55  PHE C  80  GLU C  81  PHE C  82                    
SITE     3 AC4 15 LEU C  83  HIS C  84  ASP C  86  LYS C  89                    
SITE     4 AC4 15 LEU C 134  ASP C 145  PHE C 146                               
SITE     1 AC5  3 ARG D 410  LYS D 414  LEU D 423                               
CRYST1  184.051  184.051  214.848  90.00  90.00 120.00 P 62 2 2     24          
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      0.005433  0.003137  0.000000        0.00000                         
SCALE2      0.000000  0.006274  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004654        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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