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Database: PDB
Entry: 6GUC
LinkDB: 6GUC
Original site: 6GUC 
HEADER    CELL CYCLE                              19-JUN-18   6GUC              
TITLE     CDK2/CYCLINA IN COMPLEX WITH SU9516                                   
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 SYNONYM: CYCLIN-A;                                                   
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CDK2, CDKN2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PGEX6P1;                                  
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  11 ORGANISM_COMMON: CATTLE;                                             
SOURCE  12 ORGANISM_TAXID: 9913;                                                
SOURCE  13 GENE: CCNA2;                                                         
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PET21D                                    
KEYWDS    CDK2, CYCLINA, INHIBITOR, CELL CYCLE                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.J.WOOD,S.KOROLCHUK,N.J.TATUM,L.Z.WANG,J.A.ENDICOTT,M.E.M.NOBLE,     
AUTHOR   2 M.P.MARTIN                                                           
REVDAT   2   30-JAN-19 6GUC    1       JRNL                                     
REVDAT   1   05-DEC-18 6GUC    0                                                
JRNL        AUTH   D.J.WOOD,S.KOROLCHUK,N.J.TATUM,L.Z.WANG,J.A.ENDICOTT,        
JRNL        AUTH 2 M.E.M.NOBLE,M.P.MARTIN                                       
JRNL        TITL   DIFFERENCES IN THE CONFORMATIONAL ENERGY LANDSCAPE OF CDK1   
JRNL        TITL 2 AND CDK2 SUGGEST A MECHANISM FOR ACHIEVING SELECTIVE CDK     
JRNL        TITL 3 INHIBITION.                                                  
JRNL        REF    CELL CHEM BIOL                V.  26   121 2019              
JRNL        REFN                   ESSN 2451-9448                               
JRNL        PMID   30472117                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2018.10.015                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100.77                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 99091                          
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) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5195                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7223                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.79                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2600                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 377                          
REMARK   3   BIN FREE R VALUE                    : 0.2900                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8945                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 537                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.11                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.34000                                             
REMARK   3    B22 (A**2) : -0.44000                                             
REMARK   3    B33 (A**2) : 0.78000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.154         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.141         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9208 ; 0.018 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  8718 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12509 ; 1.723 ; 1.974       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 20241 ; 3.644 ; 2.997       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1106 ; 5.700 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   399 ;40.868 ;23.985       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1605 ;15.780 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    43 ;19.411 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1417 ; 0.112 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9993 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1826 ; 0.012 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4439 ; 4.148 ; 4.174       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4438 ; 4.147 ; 4.173       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5540 ; 5.574 ; 6.231       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  5541 ; 5.575 ; 6.232       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4769 ; 5.097 ; 4.733       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  4770 ; 5.096 ; 4.732       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  6970 ; 7.630 ; 6.910       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 10008 ;10.288 ;49.029       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  9898 ;10.310 ;48.857       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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 6GUC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JUN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200010583.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUL-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.987                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 104286                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.770                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
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: 1H1S                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN AT 5MG PER ML. 0.6 TO 0.8M       
REMARK 280  KCL, 0.9 TO 1.2M (NH402SO4, AND 100MM HEPES (PH 7.0), 0.5MM         
REMARK 280  INHIBITOR, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       37.67650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.81250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       67.91250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       74.81250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.67650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       67.91250            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4180 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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: 4280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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     GLY A    -3                                                      
REMARK 465     PRO A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     ARG A    36                                                      
REMARK 465     LEU A    37                                                      
REMARK 465     ASP A    38                                                      
REMARK 465     THR A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 465     ARG A   297                                                      
REMARK 465     LEU A   298                                                      
REMARK 465     GLY B   171                                                      
REMARK 465     HIS B   433                                                      
REMARK 465     HIS B   434                                                      
REMARK 465     HIS B   435                                                      
REMARK 465     HIS B   436                                                      
REMARK 465     HIS B   437                                                      
REMARK 465     HIS B   438                                                      
REMARK 465     GLY C    -3                                                      
REMARK 465     PRO C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     ARG C   297                                                      
REMARK 465     LEU C   298                                                      
REMARK 465     GLY D   171                                                      
REMARK 465     HIS D   433                                                      
REMARK 465     HIS D   434                                                      
REMARK 465     HIS D   435                                                      
REMARK 465     HIS D   436                                                      
REMARK 465     HIS D   437                                                      
REMARK 465     HIS D   438                                                      
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    ALA A  95      -69.19    -22.40                                   
REMARK 500    ASP A 127       47.75   -154.93                                   
REMARK 500    ASP A 145       87.40     59.83                                   
REMARK 500    VAL A 164      131.29     82.25                                   
REMARK 500    SER A 181     -156.66   -143.95                                   
REMARK 500    ARG A 199        5.88     83.22                                   
REMARK 500    ASP A 223     -168.33   -123.48                                   
REMARK 500    ASP A 247      120.79    -27.29                                   
REMARK 500    ASP A 256     -168.27    -73.87                                   
REMARK 500    THR A 290     -167.02   -124.25                                   
REMARK 500    VAL B 175       62.21     36.89                                   
REMARK 500    PHE B 304       18.28     56.95                                   
REMARK 500    TRP B 372      112.94    -39.44                                   
REMARK 500    GLU C  12      147.31   -172.44                                   
REMARK 500    THR C  41      -81.11   -137.55                                   
REMARK 500    GLU C  73      -39.27    -25.57                                   
REMARK 500    ASP C 127       46.01   -155.21                                   
REMARK 500    ASP C 145       85.55     59.27                                   
REMARK 500    VAL C 164      127.31     73.90                                   
REMARK 500    SER C 181     -156.77   -144.43                                   
REMARK 500    ARG C 199        1.53     86.90                                   
REMARK 500    THR C 290     -166.50   -121.19                                   
REMARK 500    VAL D 175       61.43     36.13                                   
REMARK 500    PHE D 304       16.87     56.20                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 597        DISTANCE =  6.87 ANGSTROMS                       
REMARK 525    HOH B 684        DISTANCE =  6.48 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SU9 A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SU9 C 301                 
DBREF  6GUC A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  6GUC B  172   432  UNP    P30274   CCNA2_BOVIN    170    430             
DBREF  6GUC C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  6GUC D  172   432  UNP    P30274   CCNA2_BOVIN    170    430             
SEQADV 6GUC GLY A   -3  UNP  P24941              EXPRESSION TAG                 
SEQADV 6GUC PRO A   -2  UNP  P24941              EXPRESSION TAG                 
SEQADV 6GUC GLY A   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 6GUC SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 6GUC GLY B  171  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUC HIS B  433  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUC HIS B  434  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUC HIS B  435  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUC HIS B  436  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUC HIS B  437  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUC HIS B  438  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUC GLY C   -3  UNP  P24941              EXPRESSION TAG                 
SEQADV 6GUC PRO C   -2  UNP  P24941              EXPRESSION TAG                 
SEQADV 6GUC GLY C   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 6GUC SER C    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 6GUC GLY D  171  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUC HIS D  433  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUC HIS D  434  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUC HIS D  435  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUC HIS D  436  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUC HIS D  437  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUC HIS D  438  UNP  P30274              EXPRESSION TAG                 
SEQRES   1 A  302  GLY PRO GLY SER MET GLU ASN PHE GLN LYS VAL GLU LYS          
SEQRES   2 A  302  ILE GLY GLU GLY THR TYR GLY VAL VAL TYR LYS ALA ARG          
SEQRES   3 A  302  ASN LYS LEU THR GLY GLU VAL VAL ALA LEU LYS LYS ILE          
SEQRES   4 A  302  ARG LEU ASP THR GLU THR GLU GLY VAL PRO SER THR ALA          
SEQRES   5 A  302  ILE ARG GLU ILE SER LEU LEU LYS GLU LEU ASN HIS PRO          
SEQRES   6 A  302  ASN ILE VAL LYS LEU LEU ASP VAL ILE HIS THR GLU ASN          
SEQRES   7 A  302  LYS LEU TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU          
SEQRES   8 A  302  LYS LYS PHE MET ASP ALA SER ALA LEU THR GLY ILE PRO          
SEQRES   9 A  302  LEU PRO LEU ILE LYS SER TYR LEU PHE GLN LEU LEU GLN          
SEQRES  10 A  302  GLY LEU ALA PHE CYS HIS SER HIS ARG VAL LEU HIS ARG          
SEQRES  11 A  302  ASP LEU LYS PRO GLN ASN LEU LEU ILE ASN THR GLU GLY          
SEQRES  12 A  302  ALA ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE          
SEQRES  13 A  302  GLY VAL PRO VAL ARG THR TYR TPO HIS GLU VAL VAL THR          
SEQRES  14 A  302  LEU TRP TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS          
SEQRES  15 A  302  TYR TYR SER THR ALA VAL ASP ILE TRP SER LEU GLY CYS          
SEQRES  16 A  302  ILE PHE ALA GLU MET VAL THR ARG ARG ALA LEU PHE PRO          
SEQRES  17 A  302  GLY ASP SER GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG          
SEQRES  18 A  302  THR LEU GLY THR PRO ASP GLU VAL VAL TRP PRO GLY VAL          
SEQRES  19 A  302  THR SER MET PRO ASP TYR LYS PRO SER PHE PRO LYS TRP          
SEQRES  20 A  302  ALA ARG GLN ASP PHE SER LYS VAL VAL PRO PRO LEU ASP          
SEQRES  21 A  302  GLU ASP GLY ARG SER LEU LEU SER GLN MET LEU HIS TYR          
SEQRES  22 A  302  ASP PRO ASN LYS ARG ILE SER ALA LYS ALA ALA LEU ALA          
SEQRES  23 A  302  HIS PRO PHE PHE GLN ASP VAL THR LYS PRO VAL PRO HIS          
SEQRES  24 A  302  LEU ARG LEU                                                  
SEQRES   1 B  268  GLY VAL ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS          
SEQRES   2 B  268  THR TYR LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS          
SEQRES   3 B  268  VAL GLY TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER          
SEQRES   4 B  268  MET ARG ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY          
SEQRES   5 B  268  GLU GLU TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA          
SEQRES   6 B  268  VAL ASN TYR ILE ASP ARG PHE LEU SER SER MET SER VAL          
SEQRES   7 B  268  LEU ARG GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET          
SEQRES   8 B  268  LEU LEU ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU          
SEQRES   9 B  268  VAL ALA GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR          
SEQRES  10 B  268  LYS LYS GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS          
SEQRES  11 B  268  VAL LEU ALA PHE ASP LEU ALA ALA PRO THR ILE ASN GLN          
SEQRES  12 B  268  PHE LEU THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN          
SEQRES  13 B  268  CYS LYS VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU          
SEQRES  14 B  268  SER LEU ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO          
SEQRES  15 B  268  SER VAL ILE ALA ALA ALA ALA PHE HIS LEU ALA LEU TYR          
SEQRES  16 B  268  THR VAL THR GLY GLN SER TRP PRO GLU SER LEU VAL GLN          
SEQRES  17 B  268  LYS THR GLY TYR THR LEU GLU THR LEU LYS PRO CYS LEU          
SEQRES  18 B  268  LEU ASP LEU HIS GLN THR TYR LEU ARG ALA PRO GLN HIS          
SEQRES  19 B  268  ALA GLN GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS          
SEQRES  20 B  268  TYR HIS GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU          
SEQRES  21 B  268  ASN VAL HIS HIS HIS HIS HIS HIS                              
SEQRES   1 C  302  GLY PRO GLY SER MET GLU ASN PHE GLN LYS VAL GLU LYS          
SEQRES   2 C  302  ILE GLY GLU GLY THR TYR GLY VAL VAL TYR LYS ALA ARG          
SEQRES   3 C  302  ASN LYS LEU THR GLY GLU VAL VAL ALA LEU LYS LYS ILE          
SEQRES   4 C  302  ARG LEU ASP THR GLU THR GLU GLY VAL PRO SER THR ALA          
SEQRES   5 C  302  ILE ARG GLU ILE SER LEU LEU LYS GLU LEU ASN HIS PRO          
SEQRES   6 C  302  ASN ILE VAL LYS LEU LEU ASP VAL ILE HIS THR GLU ASN          
SEQRES   7 C  302  LYS LEU TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU          
SEQRES   8 C  302  LYS LYS PHE MET ASP ALA SER ALA LEU THR GLY ILE PRO          
SEQRES   9 C  302  LEU PRO LEU ILE LYS SER TYR LEU PHE GLN LEU LEU GLN          
SEQRES  10 C  302  GLY LEU ALA PHE CYS HIS SER HIS ARG VAL LEU HIS ARG          
SEQRES  11 C  302  ASP LEU LYS PRO GLN ASN LEU LEU ILE ASN THR GLU GLY          
SEQRES  12 C  302  ALA ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE          
SEQRES  13 C  302  GLY VAL PRO VAL ARG THR TYR TPO HIS GLU VAL VAL THR          
SEQRES  14 C  302  LEU TRP TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS          
SEQRES  15 C  302  TYR TYR SER THR ALA VAL ASP ILE TRP SER LEU GLY CYS          
SEQRES  16 C  302  ILE PHE ALA GLU MET VAL THR ARG ARG ALA LEU PHE PRO          
SEQRES  17 C  302  GLY ASP SER GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG          
SEQRES  18 C  302  THR LEU GLY THR PRO ASP GLU VAL VAL TRP PRO GLY VAL          
SEQRES  19 C  302  THR SER MET PRO ASP TYR LYS PRO SER PHE PRO LYS TRP          
SEQRES  20 C  302  ALA ARG GLN ASP PHE SER LYS VAL VAL PRO PRO LEU ASP          
SEQRES  21 C  302  GLU ASP GLY ARG SER LEU LEU SER GLN MET LEU HIS TYR          
SEQRES  22 C  302  ASP PRO ASN LYS ARG ILE SER ALA LYS ALA ALA LEU ALA          
SEQRES  23 C  302  HIS PRO PHE PHE GLN ASP VAL THR LYS PRO VAL PRO HIS          
SEQRES  24 C  302  LEU ARG LEU                                                  
SEQRES   1 D  268  GLY VAL ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS          
SEQRES   2 D  268  THR TYR LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS          
SEQRES   3 D  268  VAL GLY TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER          
SEQRES   4 D  268  MET ARG ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY          
SEQRES   5 D  268  GLU GLU TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA          
SEQRES   6 D  268  VAL ASN TYR ILE ASP ARG PHE LEU SER SER MET SER VAL          
SEQRES   7 D  268  LEU ARG GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET          
SEQRES   8 D  268  LEU LEU ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU          
SEQRES   9 D  268  VAL ALA GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR          
SEQRES  10 D  268  LYS LYS GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS          
SEQRES  11 D  268  VAL LEU ALA PHE ASP LEU ALA ALA PRO THR ILE ASN GLN          
SEQRES  12 D  268  PHE LEU THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN          
SEQRES  13 D  268  CYS LYS VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU          
SEQRES  14 D  268  SER LEU ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO          
SEQRES  15 D  268  SER VAL ILE ALA ALA ALA ALA PHE HIS LEU ALA LEU TYR          
SEQRES  16 D  268  THR VAL THR GLY GLN SER TRP PRO GLU SER LEU VAL GLN          
SEQRES  17 D  268  LYS THR GLY TYR THR LEU GLU THR LEU LYS PRO CYS LEU          
SEQRES  18 D  268  LEU ASP LEU HIS GLN THR TYR LEU ARG ALA PRO GLN HIS          
SEQRES  19 D  268  ALA GLN GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS          
SEQRES  20 D  268  TYR HIS GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU          
SEQRES  21 D  268  ASN VAL HIS HIS HIS HIS HIS HIS                              
MODRES 6GUC TPO A  160  THR  MODIFIED RESIDUE                                   
MODRES 6GUC TPO C  160  THR  MODIFIED RESIDUE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET    SU9  A 301      18                                                       
HET    SU9  C 301      18                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SU9 (3Z)-3-(1H-IMIDAZOL-5-YLMETHYLENE)-5-METHOXY-1H-INDOL-           
HETNAM   2 SU9  2(3H)-ONE                                                       
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     SU9 SU9516                                                           
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   5  SU9    2(C13 H11 N3 O2)                                             
FORMUL   7  HOH   *537(H2 O)                                                    
HELIX    1 AA1 PRO A   45  LYS A   56  1                                  12    
HELIX    2 AA2 LEU A   87  SER A   94  1                                   8    
HELIX    3 AA3 PRO A  100  HIS A  121  1                                  22    
HELIX    4 AA4 LYS A  129  GLN A  131  5                                   3    
HELIX    5 AA5 THR A  165  ARG A  169  5                                   5    
HELIX    6 AA6 ALA A  170  LEU A  175  1                                   6    
HELIX    7 AA7 THR A  182  ARG A  199  1                                  18    
HELIX    8 AA8 SER A  207  GLY A  220  1                                  14    
HELIX    9 AA9 GLY A  229  MET A  233  5                                   5    
HELIX   10 AB1 ASP A  247  VAL A  252  1                                   6    
HELIX   11 AB2 ASP A  256  LEU A  267  1                                  12    
HELIX   12 AB3 SER A  276  LEU A  281  1                                   6    
HELIX   13 AB4 ALA A  282  GLN A  287  5                                   6    
HELIX   14 AB5 TYR B  178  CYS B  193  1                                  16    
HELIX   15 AB6 GLY B  198  GLN B  203  5                                   6    
HELIX   16 AB7 THR B  207  TYR B  225  1                                  19    
HELIX   17 AB8 GLN B  228  SER B  244  1                                  17    
HELIX   18 AB9 LEU B  249  GLY B  251  5                                   3    
HELIX   19 AC1 LYS B  252  GLU B  269  1                                  18    
HELIX   20 AC2 GLU B  274  THR B  282  1                                   9    
HELIX   21 AC3 THR B  287  ALA B  303  1                                  17    
HELIX   22 AC4 THR B  310  LEU B  320  1                                  11    
HELIX   23 AC5 ASN B  326  ASP B  343  1                                  18    
HELIX   24 AC6 ASP B  343  LEU B  348  1                                   6    
HELIX   25 AC7 LEU B  351  GLY B  369  1                                  19    
HELIX   26 AC8 PRO B  373  GLY B  381  1                                   9    
HELIX   27 AC9 THR B  383  ALA B  401  1                                  19    
HELIX   28 AD1 PRO B  402  HIS B  404  5                                   3    
HELIX   29 AD2 GLN B  407  TYR B  413  1                                   7    
HELIX   30 AD3 LYS B  414  HIS B  419  5                                   6    
HELIX   31 AD4 GLY B  420  LEU B  424  5                                   5    
HELIX   32 AD5 PRO C   45  LEU C   58  1                                  14    
HELIX   33 AD6 LEU C   87  SER C   94  1                                   8    
HELIX   34 AD7 PRO C  100  HIS C  121  1                                  22    
HELIX   35 AD8 LYS C  129  GLN C  131  5                                   3    
HELIX   36 AD9 THR C  165  ARG C  169  5                                   5    
HELIX   37 AE1 ALA C  170  LEU C  175  1                                   6    
HELIX   38 AE2 THR C  182  ARG C  199  1                                  18    
HELIX   39 AE3 SER C  207  GLY C  220  1                                  14    
HELIX   40 AE4 GLY C  229  MET C  233  5                                   5    
HELIX   41 AE5 ASP C  247  VAL C  251  5                                   5    
HELIX   42 AE6 ASP C  256  LEU C  267  1                                  12    
HELIX   43 AE7 SER C  276  ALA C  282  1                                   7    
HELIX   44 AE8 HIS C  283  GLN C  287  5                                   5    
HELIX   45 AE9 TYR D  178  CYS D  193  1                                  16    
HELIX   46 AF1 GLY D  198  GLN D  203  5                                   6    
HELIX   47 AF2 THR D  207  TYR D  225  1                                  19    
HELIX   48 AF3 GLN D  228  MET D  246  1                                  19    
HELIX   49 AF4 LEU D  249  GLY D  251  5                                   3    
HELIX   50 AF5 LYS D  252  GLU D  269  1                                  18    
HELIX   51 AF6 GLU D  274  THR D  282  1                                   9    
HELIX   52 AF7 THR D  287  LEU D  302  1                                  16    
HELIX   53 AF8 THR D  310  LEU D  320  1                                  11    
HELIX   54 AF9 ASN D  326  ASP D  343  1                                  18    
HELIX   55 AG1 ASP D  343  LEU D  348  1                                   6    
HELIX   56 AG2 LEU D  351  GLY D  369  1                                  19    
HELIX   57 AG3 PRO D  373  GLY D  381  1                                   9    
HELIX   58 AG4 THR D  383  ALA D  401  1                                  19    
HELIX   59 AG5 PRO D  402  HIS D  404  5                                   3    
HELIX   60 AG6 GLN D  407  TYR D  413  1                                   7    
HELIX   61 AG7 LYS D  414  HIS D  419  5                                   6    
HELIX   62 AG8 GLY D  420  LEU D  424  5                                   5    
SHEET    1 AA1 5 PHE A   4  GLY A  13  0                                        
SHEET    2 AA1 5 GLY A  16  ASN A  23 -1  O  VAL A  18   N  ILE A  10           
SHEET    3 AA1 5 VAL A  29  ILE A  35 -1  O  LEU A  32   N  TYR A  19           
SHEET    4 AA1 5 LEU A  76  GLU A  81 -1  O  PHE A  80   N  ALA A  31           
SHEET    5 AA1 5 LEU A  66  HIS A  71 -1  N  ILE A  70   O  TYR A  77           
SHEET    1 AA2 3 GLN A  85  ASP A  86  0                                        
SHEET    2 AA2 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3 AA2 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1 AA3 2 VAL A 123  LEU A 124  0                                        
SHEET    2 AA3 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SHEET    1 AA4 5 PHE C   4  GLY C  13  0                                        
SHEET    2 AA4 5 GLY C  16  ASN C  23 -1  O  VAL C  18   N  ILE C  10           
SHEET    3 AA4 5 VAL C  29  ARG C  36 -1  O  LEU C  32   N  TYR C  19           
SHEET    4 AA4 5 LYS C  75  GLU C  81 -1  O  PHE C  80   N  ALA C  31           
SHEET    5 AA4 5 LEU C  66  HIS C  71 -1  N  ILE C  70   O  TYR C  77           
SHEET    1 AA5 3 GLN C  85  ASP C  86  0                                        
SHEET    2 AA5 3 LEU C 133  ILE C 135 -1  O  ILE C 135   N  GLN C  85           
SHEET    3 AA5 3 ILE C 141  LEU C 143 -1  O  LYS C 142   N  LEU C 134           
SHEET    1 AA6 2 VAL C 123  LEU C 124  0                                        
SHEET    2 AA6 2 ARG C 150  ALA C 151 -1  O  ARG C 150   N  LEU C 124           
LINK         C   TYR A 159                 N   TPO A 160     1555   1555  1.33  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.33  
LINK         C   TYR C 159                 N   TPO C 160     1555   1555  1.34  
LINK         C   TPO C 160                 N   HIS C 161     1555   1555  1.33  
CISPEP   1 VAL A  154    PRO A  155          0       -11.08                     
CISPEP   2 GLN B  323    PRO B  324          0        -8.75                     
CISPEP   3 ASP B  345    PRO B  346          0        13.71                     
CISPEP   4 VAL C  154    PRO C  155          0        -8.35                     
CISPEP   5 GLN D  323    PRO D  324          0        -7.75                     
CISPEP   6 ASP D  345    PRO D  346          0        14.31                     
SITE     1 AC1  9 ILE A  10  ALA A  31  LYS A  33  PHE A  80                    
SITE     2 AC1  9 GLU A  81  PHE A  82  LEU A  83  LEU A 134                    
SITE     3 AC1  9 HOH A 488                                                     
SITE     1 AC2  8 ALA C  31  LYS C  33  PHE C  80  GLU C  81                    
SITE     2 AC2  8 PHE C  82  LEU C  83  HIS C  84  LEU C 134                    
CRYST1   75.353  135.825  149.625  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013271  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007362  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006683        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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