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Database: PDB
Entry: 4FX3
LinkDB: 4FX3
Original site: 4FX3 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       02-JUL-12   4FX3              
TITLE     CRYSTAL STRUCTURE OF THE CDK2/CYCLIN A COMPLEX WITH OXINDOLE INHIBITOR
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 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CYCLIN-A2;                                                 
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: UNP RESIDUES 175-432;                                      
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, CDKN2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HIGH-FIVE;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PFB1;                                     
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 GENE: CCN1, CCNA, CCNA2, CYCLIN A;                                   
SOURCE  17 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  18 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    COMPLEX (TRANSFERASE-CYCLIN), TRANSFERASE-TRANSFERASE INHIBITOR       
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.N.KANG,J.A.STUCKEY                                                  
REVDAT   2   15-NOV-17 4FX3    1       REMARK                                   
REVDAT   1   15-MAY-13 4FX3    0                                                
JRNL        AUTH   Y.N.KANG,J.A.STUCKEY                                         
JRNL        TITL   CRYSTAL STRUCTURE OF THE CDK2/CYCLIN A COMPLEX WITH OXINDOLE 
JRNL        TITL 2 INHIBITOR                                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER-TNT BUSTER 2.11.1                             
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.91                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 40541                          
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)  : 0.192                          
REMARK   3   R VALUE            (WORKING SET)  : 0.190                          
REMARK   3   FREE R VALUE                      : 0.240                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.030                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2038                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.74                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.81                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 97.86                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2342                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2275                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2213                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2250                   
REMARK   3   BIN FREE R VALUE                        : 0.2664                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.51                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 129                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8835                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 74                                      
REMARK   3   SOLVENT ATOMS            : 154                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.02                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -11.64100                                            
REMARK   3    B22 (A**2) : -3.49490                                             
REMARK   3    B33 (A**2) : 15.13580                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -12.73400                                            
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.345               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.773               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.905                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.875                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 9169   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 12488  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 4187   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 198    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1378   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 9169   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1187   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 10583  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.011                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.13                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.01                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 2.98                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: {A|1 - 298}                                            
REMARK   3    ORIGIN FOR THE GROUP (A):   -1.1364   14.2305   37.2831           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0304 T22:   -0.0993                                    
REMARK   3     T33:   -0.0401 T12:    0.0380                                    
REMARK   3     T13:    0.0770 T23:    0.0140                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.6578 L22:    1.7910                                    
REMARK   3     L33:    0.4806 L12:    0.0895                                    
REMARK   3     L13:   -0.0092 L23:    0.2164                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0253 S12:   -0.0738 S13:    0.0433                     
REMARK   3     S21:    0.0001 S22:    0.0367 S23:    0.1068                     
REMARK   3     S31:    0.0519 S32:    0.0878 S33:   -0.0113                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: {B|176 - 432}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):   16.6465   10.0079    9.6261           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0025 T22:   -0.0763                                    
REMARK   3     T33:   -0.0787 T12:    0.0106                                    
REMARK   3     T13:    0.0921 T23:   -0.0323                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.0828 L22:    0.4942                                    
REMARK   3     L33:    1.7051 L12:    0.3324                                    
REMARK   3     L13:    0.1790 L23:    0.0512                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0013 S12:   -0.1121 S13:    0.0037                     
REMARK   3     S21:   -0.1083 S22:    0.0828 S23:    0.0963                     
REMARK   3     S31:   -0.0626 S32:    0.3059 S33:   -0.0841                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: {C|1 - 298}                                            
REMARK   3    ORIGIN FOR THE GROUP (A):    9.5191  -37.5525    3.1991           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0018 T22:   -0.1089                                    
REMARK   3     T33:   -0.0707 T12:   -0.0325                                    
REMARK   3     T13:    0.0396 T23:   -0.0033                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.5532 L22:    1.5033                                    
REMARK   3     L33:    0.9118 L12:   -0.1529                                    
REMARK   3     L13:   -0.0562 L23:    0.1665                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0229 S12:    0.0078 S13:   -0.0047                     
REMARK   3     S21:   -0.0609 S22:    0.1010 S23:    0.0466                     
REMARK   3     S31:    0.0417 S32:    0.0327 S33:   -0.0781                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: {D|175 - 432}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):    9.1617  -32.8332   35.9279           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0178 T22:   -0.0556                                    
REMARK   3     T33:   -0.0596 T12:    0.0211                                    
REMARK   3     T13:    0.0208 T23:   -0.0152                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.4321 L22:    0.7666                                    
REMARK   3     L33:    0.6708 L12:   -0.4293                                    
REMARK   3     L13:   -0.2420 L23:   -0.0273                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0660 S12:   -0.0722 S13:    0.0398                     
REMARK   3     S21:    0.0534 S22:    0.0789 S23:    0.0825                     
REMARK   3     S31:    0.1160 S32:    0.1959 S33:   -0.0129                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4FX3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000073462.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-OCT-11                          
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                       : 21-ID-G                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97856                            
REMARK 200  MONOCHROMATOR                  : DIAMOND [111]                      
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40559                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.11800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46500                            
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: PHASER                                                
REMARK 200 STARTING MODEL: 1FIN                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% POLYACRYLIC ACID 5100, 0.1M HEPES,   
REMARK 280  0.02M MGCL2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K,    
REMARK 280  PH 7.5, VAPOR DIFFUSION, SITTING DROP                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       81.81150            
REMARK 290   SMTRY3   2  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: 3690 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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: 3450 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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     VAL B   175                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A   5    CG   CD   OE1  NE2                                  
REMARK 470     LYS A   9    CG   CD   CE   NZ                                   
REMARK 470     ARG A  36    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A  38    CG   OD1  OD2                                       
REMARK 470     LYS A  75    CG   CD   CE   NZ                                   
REMARK 470     LEU A  96    CG   CD1  CD2                                       
REMARK 470     ARG A 157    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR A 159    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     VAL A 163    CG1  CG2                                            
REMARK 470     LYS A 178    CG   CD   CE   NZ                                   
REMARK 470     LYS A 250    CG   CD   CE   NZ                                   
REMARK 470     ARG A 297    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 196    CG   CD   CE   NZ                                   
REMARK 470     LYS B 202    CG   CD   CE   NZ                                   
REMARK 470     GLN B 370    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 428    CG   CD   OE1  OE2                                  
REMARK 470     TYR C  15    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG C  36    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN C  74    CG   OD1  ND2                                       
REMARK 470     LYS C  75    CG   CD   CE   NZ                                   
REMARK 470     LEU C 101    CG   CD1  CD2                                       
REMARK 470     VAL C 163    CG1  CG2                                            
REMARK 470     LYS C 178    CG   CD   CE   NZ                                   
REMARK 470     LYS C 250    CG   CD   CE   NZ                                   
REMARK 470     ARG C 297    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL D 175    CG1  CG2                                            
REMARK 470     LYS D 201    CG   CD   CE   NZ                                   
REMARK 470     GLN D 323    CG   CD   OE1  NE2                                  
REMARK 470     GLU D 428    CG   CD   OE1  OE2                                  
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    ASP A 127       48.15   -152.85                                   
REMARK 500    ASP A 145       93.46     49.10                                   
REMARK 500    THR A 218      -60.16    -93.61                                   
REMARK 500    PRO A 254       37.12    -88.03                                   
REMARK 500    LYS A 291       78.46   -119.87                                   
REMARK 500    PHE B 304       13.61     59.15                                   
REMARK 500    HIS B 321       47.41   -106.62                                   
REMARK 500    GLN B 322       83.82   -157.35                                   
REMARK 500    ASN B 431       69.30     65.47                                   
REMARK 500    ILE C  10       58.27   -106.26                                   
REMARK 500    ARG C 126       -6.08     69.82                                   
REMARK 500    ASP C 127       51.81   -142.94                                   
REMARK 500    ASP C 145       89.74     44.13                                   
REMARK 500    HIS C 161      -88.74   -159.63                                   
REMARK 500    PHE C 203       68.83   -118.30                                   
REMARK 500    PRO D 176     -179.30    -69.74                                   
REMARK 500    PHE D 304       19.80     55.28                                   
REMARK 500    HIS D 321       51.62   -108.93                                   
REMARK 500    GLN D 323       79.60   -118.70                                   
REMARK 500    HIS D 419       28.31     44.69                                   
REMARK 500    ASN D 431       68.63     63.39                                   
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 60K A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 60K C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT D 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4EK3   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF APO CDK2                                        
REMARK 900 RELATED ID: 4EK4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH AMINOPYRAZOLE          
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 4EK5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH AMINOPYRAZOLE          
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 4EK6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH AMINOPYRAZOLE          
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 4EK8   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH THIAZOLYLPYRIMIDINE    
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 4FKG   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH AMINOPYRAZOLE          
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 4FKI   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH AMINOPYRAZOLE          
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 4FKJ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH AMINOPYRAZOLE          
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 4FKL   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH THIAZOLYLPYRIMIDINE    
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 4FKO   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH THIAZOLYLPYRIMIDINE    
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 4FKP   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH OXINDOLE INHIBITOR     
REMARK 900 RELATED ID: 4FKQ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH OXINDOLE INHIBITOR     
REMARK 900 RELATED ID: 4FKR   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH OXINDOLE INHIBITOR     
REMARK 900 RELATED ID: 4FKS   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH OXINDOLE INHIBITOR     
REMARK 900 RELATED ID: 4FKT   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH OXINDOLE INHIBITOR     
REMARK 900 RELATED ID: 4FKU   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH OXINDOLE INHIBITOR     
REMARK 900 RELATED ID: 4FKV   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH OXINDOLE INHIBITOR     
REMARK 900 RELATED ID: 4FKW   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CDK2 IN COMPLEX WITH OXINDOLE INHIBITOR     
DBREF  4FX3 A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4FX3 B  175   432  UNP    P20248   CCNA2_HUMAN    175    432             
DBREF  4FX3 C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  4FX3 D  175   432  UNP    P20248   CCNA2_HUMAN    175    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  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  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  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                  
HET    60K  A 301      37                                                       
HET    DTT  A 302       8                                                       
HET    DTT  B 501       8                                                       
HET    60K  C 301      37                                                       
HET    DTT  D 501       8                                                       
HETNAM     60K (3Z)-2-OXO-3-[2-(4-SULFAMOYLPHENYL)HYDRAZINYLIDENE]-2,           
HETNAM   2 60K  3-DIHYDRO-1H-INDOLE-5-CARBOXYLIC ACID                           
HETNAM     DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE                                   
HETSYN     DTT 1,4-DITHIOTHREITOL                                               
FORMUL   5  60K    2(C15 H12 N4 O5 S)                                           
FORMUL   6  DTT    3(C4 H10 O2 S2)                                              
FORMUL  10  HOH   *154(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  GLY A  176  1                                   7    
HELIX    7   7 THR A  182  ARG A  199  1                                  18    
HELIX    8   8 SER A  207  GLY A  220  1                                  14    
HELIX    9   9 GLY A  229  MET A  233  5                                   5    
HELIX   10  10 ASP A  247  VAL A  252  1                                   6    
HELIX   11  11 ASP A  256  LEU A  267  1                                  12    
HELIX   12  12 SER A  276  LEU A  281  1                                   6    
HELIX   13  13 ALA A  282  VAL A  289  5                                   8    
HELIX   14  14 TYR B  178  CYS B  193  1                                  16    
HELIX   15  15 GLY B  198  GLN B  203  5                                   6    
HELIX   16  16 THR B  207  LYS B  226  1                                  20    
HELIX   17  17 GLN B  228  MET B  246  1                                  19    
HELIX   18  18 LEU B  249  GLU B  269  1                                  21    
HELIX   19  19 GLU B  274  ILE B  281  1                                   8    
HELIX   20  20 THR B  287  LEU B  302  1                                  16    
HELIX   21  21 THR B  310  LEU B  320  1                                  11    
HELIX   22  22 ASN B  326  ASP B  343  1                                  18    
HELIX   23  23 ASP B  343  LEU B  348  1                                   6    
HELIX   24  24 LEU B  351  THR B  368  1                                  18    
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 GLN B  407  LYS B  414  1                                   8    
HELIX   28  28 ASN B  415  HIS B  419  5                                   5    
HELIX   29  29 GLY B  420  LEU B  424  5                                   5    
HELIX   30  30 PRO C   45  LYS C   56  1                                  12    
HELIX   31  31 LEU C   87  SER C   94  1                                   8    
HELIX   32  32 PRO C  100  HIS C  121  1                                  22    
HELIX   33  33 LYS C  129  GLN C  131  5                                   3    
HELIX   34  34 THR C  165  ARG C  169  5                                   5    
HELIX   35  35 ALA C  170  LEU C  175  1                                   6    
HELIX   36  36 THR C  182  ARG C  199  1                                  18    
HELIX   37  37 SER C  207  GLY C  220  1                                  14    
HELIX   38  38 GLY C  229  MET C  233  5                                   5    
HELIX   39  39 ASP C  247  VAL C  252  1                                   6    
HELIX   40  40 ASP C  256  LEU C  267  1                                  12    
HELIX   41  41 SER C  276  ALA C  282  1                                   7    
HELIX   42  42 HIS C  283  GLN C  287  5                                   5    
HELIX   43  43 ASP D  177  CYS D  193  1                                  17    
HELIX   44  44 THR D  207  TYR D  225  1                                  19    
HELIX   45  45 GLN D  228  SER D  244  1                                  17    
HELIX   46  46 LEU D  249  GLU D  269  1                                  21    
HELIX   47  47 GLU D  274  THR D  282  1                                   9    
HELIX   48  48 THR D  287  LEU D  302  1                                  16    
HELIX   49  49 THR D  310  PHE D  319  1                                  10    
HELIX   50  50 LEU D  320  GLN D  322  5                                   3    
HELIX   51  51 ASN D  326  ASP D  343  1                                  18    
HELIX   52  52 ASP D  343  LEU D  348  1                                   6    
HELIX   53  53 LEU D  351  THR D  368  1                                  18    
HELIX   54  54 PRO D  373  GLY D  381  1                                   9    
HELIX   55  55 THR D  383  LYS D  400  1                                  18    
HELIX   56  56 ALA D  401  HIS D  404  5                                   4    
HELIX   57  57 GLN D  407  TYR D  413  1                                   7    
HELIX   58  58 GLY D  420  LEU D  424  5                                   5    
SHEET    1   A 5 PHE A   4  LYS A   9  0                                        
SHEET    2   A 5 VAL A  17  ASN A  23 -1  O  LYS A  20   N  GLU A   8           
SHEET    3   A 5 VAL A  29  ARG A  36 -1  O  LYS A  34   N  VAL A  17           
SHEET    4   A 5 LYS A  75  GLU A  81 -1  O  LEU A  76   N  ILE A  35           
SHEET    5   A 5 LEU A  66  HIS A  71 -1  N  ASP A  68   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  VAL C   7           
SHEET    3   D 5 VAL C  29  ARG C  36 -1  O  VAL C  30   N  ALA C  21           
SHEET    4   D 5 LYS C  75  GLU C  81 -1  O  PHE C  80   N  ALA C  31           
SHEET    5   D 5 LEU C  66  HIS C  71 -1  N  ILE C  70   O  TYR C  77           
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         0.90                     
CISPEP   2 ASP B  345    PRO B  346          0        14.68                     
CISPEP   3 GLN D  323    PRO D  324          0        -5.23                     
CISPEP   4 ASP D  345    PRO D  346          0        12.28                     
SITE     1 AC1 14 ILE A  10  ALA A  31  LYS A  33  VAL A  64                    
SITE     2 AC1 14 PHE A  80  GLU A  81  PHE A  82  LEU A  83                    
SITE     3 AC1 14 HIS A  84  GLN A  85  ASP A  86  LYS A  89                    
SITE     4 AC1 14 LEU A 134  ASP A 145                                          
SITE     1 AC2  4 LYS A  56  LEU A  66  ASP A  68  VAL A  69                    
SITE     1 AC3  3 ILE B 213  LEU B 214  LEU B 253                               
SITE     1 AC4 13 ILE C  10  ALA C  31  LYS C  33  PHE C  80                    
SITE     2 AC4 13 GLU C  81  PHE C  82  LEU C  83  HIS C  84                    
SITE     3 AC4 13 GLN C  85  ASP C  86  LYS C  89  LEU C 134                    
SITE     4 AC4 13 ASP C 145                                                     
SITE     1 AC5  4 MET D 210  ILE D 213  LEU D 214  GLN D 254                    
CRYST1   70.661  163.623   72.609  90.00 106.78  90.00 P 1 21 1      4          
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      0.014152  0.000000  0.004267        0.00000                         
SCALE2      0.000000  0.006112  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014385        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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