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Database: PDB
Entry: 6GUF
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Original site: 6GUF 
HEADER    CELL CYCLE                              19-JUN-18   6GUF              
TITLE     CDK2/CYCLINA IN COMPLEX WITH CGP74514A                                
CAVEAT     6GUF    23D A 301 HAS WRONG CHIRALITY AT ATOM CAA 23D C 301 HAS      
CAVEAT   2 6GUF    WRONG CHIRALITY AT ATOM CAA                                  
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 6GUF    1       JRNL                                     
REVDAT   1   05-DEC-18 6GUF    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.    2.65 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) : 2.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 101.17                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 43626                          
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) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2243                            
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) : 2.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.72                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3165                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.85                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3050                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 165                          
REMARK   3   BIN FREE R VALUE                    : 0.3510                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8994                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 54                                      
REMARK   3   SOLVENT ATOMS            : 124                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.68                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.47000                                             
REMARK   3    B22 (A**2) : 0.12000                                              
REMARK   3    B33 (A**2) : 3.35000                                              
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): 0.629         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.315         
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      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.909                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9277 ; 0.013 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  8805 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12602 ; 1.719 ; 1.974       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 20441 ; 3.689 ; 2.992       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1111 ; 6.153 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   400 ;40.312 ;23.950       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1618 ;20.170 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    46 ;18.168 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1428 ; 0.101 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10033 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1839 ; 0.008 ; 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):  4459 ; 3.773 ; 4.879       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4458 ; 3.772 ; 4.878       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5565 ; 6.050 ; 7.305       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  5566 ; 6.050 ; 7.307       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4818 ; 4.177 ; 5.263       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  4818 ; 4.176 ; 5.263       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  7038 ; 6.909 ; 7.757       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 10038 ;10.037 ;56.681       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 10031 ;10.038 ;56.694       
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 6GUF 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_1200010587.                                   
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) : 0.92819                            
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   : 45869                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 101.170                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : 0.20000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.300                              
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   (%): 58.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97                     
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       37.65900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.22700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       68.34350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       75.22700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.65900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       68.34350            
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: 4340 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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: 4540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -3                                                      
REMARK 465     PRO A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     ASP A    38                                                      
REMARK 465     THR A    39                                                      
REMARK 465     GLU A    40                                                      
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     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: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B 324   C   -  N   -  CA  ANGL. DEV. =  13.5 DEGREES          
REMARK 500    PRO B 324   C   -  N   -  CD  ANGL. DEV. = -18.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  72       17.17    -55.43                                   
REMARK 500    GLU A  73      -19.42     64.62                                   
REMARK 500    THR A  97      -52.40     87.24                                   
REMARK 500    HIS A 125      -71.76    -59.96                                   
REMARK 500    ARG A 126       -6.29     90.26                                   
REMARK 500    ASP A 127       47.49   -150.77                                   
REMARK 500    ASP A 145       81.44     60.50                                   
REMARK 500    VAL A 164      137.33     70.93                                   
REMARK 500    SER A 181     -157.05   -136.70                                   
REMARK 500    ASP A 223     -168.98   -121.66                                   
REMARK 500    TRP A 227       86.76   -155.70                                   
REMARK 500    ASP A 247      132.65    -39.61                                   
REMARK 500    ASP A 256     -179.12    -62.93                                   
REMARK 500    VAL B 175       60.42     33.08                                   
REMARK 500    THR C  41      -80.56   -125.93                                   
REMARK 500    ASP C 127       50.54   -165.37                                   
REMARK 500    ASP C 145       82.88     48.40                                   
REMARK 500    VAL C 163     -119.25     39.73                                   
REMARK 500    SER C 181     -157.59   -139.88                                   
REMARK 500    SER C 239       87.07   -161.22                                   
REMARK 500    ARG C 245       78.71   -168.92                                   
REMARK 500    LYS C 250      -30.51     94.21                                   
REMARK 500    PRO C 254     -146.48    -73.36                                   
REMARK 500    LEU C 255      120.25     73.98                                   
REMARK 500    VAL D 175       58.77     33.08                                   
REMARK 500    ASP D 284       28.64     43.07                                   
REMARK 500    PHE D 304       13.30     59.35                                   
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 23D A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 23D C 301                 
DBREF  6GUF A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  6GUF B  172   432  UNP    P30274   CCNA2_BOVIN    170    430             
DBREF  6GUF C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  6GUF D  172   432  UNP    P30274   CCNA2_BOVIN    170    430             
SEQADV 6GUF GLY A   -3  UNP  P24941              EXPRESSION TAG                 
SEQADV 6GUF PRO A   -2  UNP  P24941              EXPRESSION TAG                 
SEQADV 6GUF GLY A   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 6GUF SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 6GUF GLY B  171  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUF HIS B  433  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUF HIS B  434  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUF HIS B  435  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUF HIS B  436  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUF HIS B  437  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUF HIS B  438  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUF GLY C   -3  UNP  P24941              EXPRESSION TAG                 
SEQADV 6GUF PRO C   -2  UNP  P24941              EXPRESSION TAG                 
SEQADV 6GUF GLY C   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 6GUF SER C    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 6GUF GLY D  171  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUF HIS D  433  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUF HIS D  434  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUF HIS D  435  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUF HIS D  436  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUF HIS D  437  UNP  P30274              EXPRESSION TAG                 
SEQADV 6GUF 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 6GUF TPO A  160  THR  MODIFIED RESIDUE                                   
MODRES 6GUF TPO C  160  THR  MODIFIED RESIDUE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET    23D  A 301      27                                                       
HET    23D  C 301      27                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     23D N2-[(1R,2S)-2-AMINOCYCLOHEXYL]-N6-(3-CHLOROPHENYL)-9-            
HETNAM   2 23D  ETHYL-9H-PURINE-2,6-DIAMINE                                     
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   5  23D    2(C19 H24 CL N7)                                             
FORMUL   7  HOH   *124(H2 O)                                                    
HELIX    1 AA1 SER A    0  GLU A    2  5                                   3    
HELIX    2 AA2 PRO A   45  LEU A   58  1                                  14    
HELIX    3 AA3 LEU A   87  SER A   94  1                                   8    
HELIX    4 AA4 PRO A  100  SER A  120  1                                  21    
HELIX    5 AA5 LYS A  129  GLN A  131  5                                   3    
HELIX    6 AA6 THR A  165  ARG A  169  5                                   5    
HELIX    7 AA7 ALA A  170  LEU A  175  1                                   6    
HELIX    8 AA8 THR A  182  ARG A  199  1                                  18    
HELIX    9 AA9 SER A  207  GLY A  220  1                                  14    
HELIX   10 AB1 GLY A  229  MET A  233  5                                   5    
HELIX   11 AB2 ASP A  247  VAL A  252  1                                   6    
HELIX   12 AB3 ASP A  256  LEU A  267  1                                  12    
HELIX   13 AB4 SER A  276  LEU A  281  1                                   6    
HELIX   14 AB5 ALA A  282  GLN A  287  5                                   6    
HELIX   15 AB6 TYR B  178  CYS B  193  1                                  16    
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  ILE B  281  1                                   8    
HELIX   21 AC3 THR B  287  ALA B  303  1                                  17    
HELIX   22 AC4 THR B  310  PHE B  319  1                                  10    
HELIX   23 AC5 LEU B  320  GLN B  322  5                                   3    
HELIX   24 AC6 ASN B  326  LEU B  341  1                                  16    
HELIX   25 AC7 ASP B  343  LEU B  348  1                                   6    
HELIX   26 AC8 LEU B  351  GLY B  369  1                                  19    
HELIX   27 AC9 PRO B  373  GLY B  381  1                                   9    
HELIX   28 AD1 THR B  383  ALA B  401  1                                  19    
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  SER C  120  1                                  21    
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  256  LEU C  267  1                                  12    
HELIX   42 AE6 SER C  276  LEU C  281  1                                   6    
HELIX   43 AE7 ALA C  282  GLN C  287  5                                   6    
HELIX   44 AE8 TYR D  178  CYS D  193  1                                  16    
HELIX   45 AE9 THR D  207  TYR D  225  1                                  19    
HELIX   46 AF1 GLN D  228  SER D  244  1                                  17    
HELIX   47 AF2 LEU D  249  GLY D  251  5                                   3    
HELIX   48 AF3 LYS D  252  GLU D  269  1                                  18    
HELIX   49 AF4 GLU D  274  ILE D  281  1                                   8    
HELIX   50 AF5 THR D  287  ALA D  303  1                                  17    
HELIX   51 AF6 THR D  310  LEU D  320  1                                  11    
HELIX   52 AF7 ASN D  326  LEU D  341  1                                  16    
HELIX   53 AF8 ASP D  343  LEU D  348  1                                   6    
HELIX   54 AF9 LEU D  351  GLY D  369  1                                  19    
HELIX   55 AG1 PRO D  373  GLY D  381  1                                   9    
HELIX   56 AG2 THR D  383  ARG D  400  1                                  18    
HELIX   57 AG3 GLN D  407  TYR D  413  1                                   7    
HELIX   58 AG4 LYS D  414  HIS D  419  5                                   6    
HELIX   59 AG5 GLY D  420  LEU D  424  5                                   5    
SHEET    1 AA1 5 PHE A   4  GLU A  12  0                                        
SHEET    2 AA1 5 VAL A  17  ASN A  23 -1  O  VAL A  18   N  GLY A  11           
SHEET    3 AA1 5 VAL A  29  ARG A  36 -1  O  LEU A  32   N  TYR A  19           
SHEET    4 AA1 5 LYS A  75  GLU A  81 -1  O  LEU A  78   N  LYS A  33           
SHEET    5 AA1 5 LEU A  66  ILE A  70 -1  N  ASP A  68   O  VAL A  79           
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  GLU C  12  0                                        
SHEET    2 AA4 5 VAL C  17  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  LEU C  78   N  LYS C  33           
SHEET    5 AA4 5 LEU C  66  HIS C  71 -1  N  ASP C  68   O  VAL C  79           
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  1.31  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.33  
LINK         C   TYR C 159                 N   TPO C 160     1555   1555  1.32  
LINK         C   TPO C 160                 N   HIS C 161     1555   1555  1.33  
CISPEP   1 VAL A  154    PRO A  155          0       -14.15                     
CISPEP   2 ASP B  345    PRO B  346          0        12.37                     
CISPEP   3 VAL C  154    PRO C  155          0       -11.26                     
CISPEP   4 GLN D  323    PRO D  324          0       -13.87                     
CISPEP   5 ASP D  345    PRO D  346          0         9.20                     
SITE     1 AC1 10 ALA A  31  PHE A  80  GLU A  81  LEU A  83                    
SITE     2 AC1 10 HIS A  84  ASP A  86  LYS A  89  GLN A 131                    
SITE     3 AC1 10 LEU A 134  HOH A 434                                          
SITE     1 AC2 10 GLU C  12  ALA C  31  PHE C  80  GLU C  81                    
SITE     2 AC2 10 LEU C  83  HIS C  84  ASP C  86  GLN C 131                    
SITE     3 AC2 10 LEU C 134  HOH C 401                                          
CRYST1   75.318  136.687  150.454  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      0.013277  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007316  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006647        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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