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Database: PDB
Entry: 6HK3
LinkDB: 6HK3
Original site: 6HK3 
HEADER    TRANSFERASE                             05-SEP-18   6HK3              
TITLE     CRYSTAL STRUCTURE OF GSK-3B IN COMPLEX WITH PYRAZINE INHIBITOR C44    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLYCOGEN SYNTHASE KINASE-3 BETA;                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: GSK-3 BETA,SERINE/THREONINE-PROTEIN KINASE GSK3B;           
COMPND   5 EC: 2.7.11.26,2.7.11.1;                                              
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: GLY-SER-HIS-GLY-HIS-HIS-HIS-HIS;                           
COMPND   9 CHAIN: N;                                                            
COMPND  10 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: GSK3B;                                                         
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS EXPRESSION VECTOR         
SOURCE   9 PFASTBAC1-HM;                                                        
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS EXPRESSION VECTOR         
SOURCE  16 PFASTBAC1-HM                                                         
KEYWDS    GSK 3B, COMPLEX, PYRAZINE, INHIBITOR, TRANSFERASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.PIRETTI,B.GIABBAI,N.DEMITRI,R.DI MARTINO,S.K.TRIPATHI,D.GOBBO,      
AUTHOR   2 S.DECHERCHI,P.STORICI,S.GIROTTO,A.CAVALLI                            
REVDAT   2   21-AUG-19 6HK3    1       JRNL                                     
REVDAT   1   17-JUL-19 6HK3    0                                                
JRNL        AUTH   D.GOBBO,V.PIRETTI,R.M.C.DI MARTINO,S.K.TRIPATHI,B.GIABBAI,   
JRNL        AUTH 2 P.STORICI,N.DEMITRI,S.GIROTTO,S.DECHERCHI,A.CAVALLI          
JRNL        TITL   INVESTIGATING DRUG-TARGET RESIDENCE TIME IN KINASES THROUGH  
JRNL        TITL 2 ENHANCED SAMPLING SIMULATIONS.                               
JRNL        REF    J CHEM THEORY COMPUT          V.  15  4646 2019              
JRNL        REFN                   ISSN 1549-9626                               
JRNL        PMID   31246463                                                     
JRNL        DOI    10.1021/ACS.JCTC.9B00104                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.98                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.960                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 43734                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2182                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.450           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6HK3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-SEP-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200011689.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAR-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ELETTRA                            
REMARK 200  BEAMLINE                       : 5.2R                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.6.2                      
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46585                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.220                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY                : 2.400                              
REMARK 200  R MERGE                    (I) : 0.09800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.45400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4ACD                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M POTASSIUM FLUORIDE 22% PEG 3350,    
REMARK 280  PH 7.4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 960 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 16630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1680 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 APPLY THE FOLLOWING TO CHAINS: N                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000       64.31800            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  50    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  92    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE A  93    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A  94    CG   CD   CE   NZ                                   
REMARK 470     GLN A  99    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 121    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 123    CG   CD   CE   NZ                                   
REMARK 470     GLU A 125    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 278    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 279    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 291    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 292    CG   CD   CE   NZ                                   
REMARK 470     ARG A 306    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B  46    CG   CD   OE1  NE2                                  
REMARK 470     PHE B  93    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU B 121    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 122    CG   CD   CE   NZ                                   
REMARK 470     LYS B 123    CG   CD   CE   NZ                                   
REMARK 470     ASP B 124    CG   OD1  OD2                                       
REMARK 470     GLU B 211    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 303    CG   CD   CE   NZ                                   
REMARK 470     ARG B 306    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS N 426    CG   ND1  CD2  CE1  NE2                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  49       55.49    -61.38                                   
REMARK 500    ASP A  77      -75.48    -72.16                                   
REMARK 500    LYS A  91      170.95    -56.96                                   
REMARK 500    GLU A 121      -20.12     59.98                                   
REMARK 500    ARG A 180       15.80     59.71                                   
REMARK 500    ASP A 181       44.15   -150.44                                   
REMARK 500    ASP A 200       89.98     53.43                                   
REMARK 500    CYS A 218      141.48     66.82                                   
REMARK 500    CYS A 218      142.28     65.54                                   
REMARK 500    ASN A 285      115.24   -175.33                                   
REMARK 500    PRO A 286       52.09    -93.19                                   
REMARK 500    ASN A 287       24.53   -153.58                                   
REMARK 500    PHE A 291     -115.69     50.93                                   
REMARK 500    LYS A 292      -11.11   -174.40                                   
REMARK 500    PHE A 293      151.86     59.60                                   
REMARK 500    ASN A 370       63.43   -163.70                                   
REMARK 500    ASP B  49       66.41    -67.26                                   
REMARK 500    ASP B  58       51.79     72.32                                   
REMARK 500    ILE B  62       10.67   -141.47                                   
REMARK 500    ALA B 149        4.53    -67.73                                   
REMARK 500    ASP B 181       37.67   -156.98                                   
REMARK 500    ASP B 200       95.88     49.94                                   
REMARK 500    CYS B 218      150.32     73.00                                   
REMARK 500    CYS B 218      150.58     72.73                                   
REMARK 500    GLU B 290       26.33     45.14                                   
REMARK 500    ARG B 308       41.38    -95.90                                   
REMARK 500    ASN B 370       68.73   -164.83                                   
REMARK 500    HIS B 381       10.43    -62.69                                   
REMARK 500    HIS N 425      121.29     -5.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 602        DISTANCE =  7.88 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue G8B A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 406                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue G8B B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 405                 
DBREF  6HK3 A   35   384  UNP    P49841   GSK3B_HUMAN     35    384             
DBREF  6HK3 B   35   384  UNP    P49841   GSK3B_HUMAN     35    384             
DBREF  6HK3 N  419   426  PDB    6HK3     6HK3           419    426             
SEQRES   1 A  350  SER LYS VAL THR THR VAL VAL ALA THR PRO GLY GLN GLY          
SEQRES   2 A  350  PRO ASP ARG PRO GLN GLU VAL SER TYR THR ASP THR LYS          
SEQRES   3 A  350  VAL ILE GLY ASN GLY SER PHE GLY VAL VAL TYR GLN ALA          
SEQRES   4 A  350  LYS LEU CYS ASP SER GLY GLU LEU VAL ALA ILE LYS LYS          
SEQRES   5 A  350  VAL LEU GLN ASP LYS ARG PHE LYS ASN ARG GLU LEU GLN          
SEQRES   6 A  350  ILE MET ARG LYS LEU ASP HIS CYS ASN ILE VAL ARG LEU          
SEQRES   7 A  350  ARG TYR PHE PHE TYR SER SER GLY GLU LYS LYS ASP GLU          
SEQRES   8 A  350  VAL TYR LEU ASN LEU VAL LEU ASP TYR VAL PRO GLU THR          
SEQRES   9 A  350  VAL TYR ARG VAL ALA ARG HIS TYR SER ARG ALA LYS GLN          
SEQRES  10 A  350  THR LEU PRO VAL ILE TYR VAL LYS LEU TYR MET TYR GLN          
SEQRES  11 A  350  LEU PHE ARG SER LEU ALA TYR ILE HIS SER PHE GLY ILE          
SEQRES  12 A  350  CYS HIS ARG ASP ILE LYS PRO GLN ASN LEU LEU LEU ASP          
SEQRES  13 A  350  PRO ASP THR ALA VAL LEU LYS LEU CYS ASP PHE GLY SER          
SEQRES  14 A  350  ALA LYS GLN LEU VAL ARG GLY GLU PRO ASN VAL SER PTR          
SEQRES  15 A  350  ILE CYS SER ARG TYR TYR ARG ALA PRO GLU LEU ILE PHE          
SEQRES  16 A  350  GLY ALA THR ASP TYR THR SER SER ILE ASP VAL TRP SER          
SEQRES  17 A  350  ALA GLY CYS VAL LEU ALA GLU LEU LEU LEU GLY GLN PRO          
SEQRES  18 A  350  ILE PHE PRO GLY ASP SER GLY VAL ASP GLN LEU VAL GLU          
SEQRES  19 A  350  ILE ILE LYS VAL LEU GLY THR PRO THR ARG GLU GLN ILE          
SEQRES  20 A  350  ARG GLU MET ASN PRO ASN TYR THR GLU PHE LYS PHE PRO          
SEQRES  21 A  350  GLN ILE LYS ALA HIS PRO TRP THR LYS VAL PHE ARG PRO          
SEQRES  22 A  350  ARG THR PRO PRO GLU ALA ILE ALA LEU CYS SER ARG LEU          
SEQRES  23 A  350  LEU GLU TYR THR PRO THR ALA ARG LEU THR PRO LEU GLU          
SEQRES  24 A  350  ALA CYS ALA HIS SER PHE PHE ASP GLU LEU ARG ASP PRO          
SEQRES  25 A  350  ASN VAL LYS LEU PRO ASN GLY ARG ASP THR PRO ALA LEU          
SEQRES  26 A  350  PHE ASN PHE THR THR GLN GLU LEU SER SER ASN PRO PRO          
SEQRES  27 A  350  LEU ALA THR ILE LEU ILE PRO PRO HIS ALA ARG ILE              
SEQRES   1 B  350  SER LYS VAL THR THR VAL VAL ALA THR PRO GLY GLN GLY          
SEQRES   2 B  350  PRO ASP ARG PRO GLN GLU VAL SER TYR THR ASP THR LYS          
SEQRES   3 B  350  VAL ILE GLY ASN GLY SER PHE GLY VAL VAL TYR GLN ALA          
SEQRES   4 B  350  LYS LEU CYS ASP SER GLY GLU LEU VAL ALA ILE LYS LYS          
SEQRES   5 B  350  VAL LEU GLN ASP LYS ARG PHE LYS ASN ARG GLU LEU GLN          
SEQRES   6 B  350  ILE MET ARG LYS LEU ASP HIS CYS ASN ILE VAL ARG LEU          
SEQRES   7 B  350  ARG TYR PHE PHE TYR SER SER GLY GLU LYS LYS ASP GLU          
SEQRES   8 B  350  VAL TYR LEU ASN LEU VAL LEU ASP TYR VAL PRO GLU THR          
SEQRES   9 B  350  VAL TYR ARG VAL ALA ARG HIS TYR SER ARG ALA LYS GLN          
SEQRES  10 B  350  THR LEU PRO VAL ILE TYR VAL LYS LEU TYR MET TYR GLN          
SEQRES  11 B  350  LEU PHE ARG SER LEU ALA TYR ILE HIS SER PHE GLY ILE          
SEQRES  12 B  350  CYS HIS ARG ASP ILE LYS PRO GLN ASN LEU LEU LEU ASP          
SEQRES  13 B  350  PRO ASP THR ALA VAL LEU LYS LEU CYS ASP PHE GLY SER          
SEQRES  14 B  350  ALA LYS GLN LEU VAL ARG GLY GLU PRO ASN VAL SER PTR          
SEQRES  15 B  350  ILE CYS SER ARG TYR TYR ARG ALA PRO GLU LEU ILE PHE          
SEQRES  16 B  350  GLY ALA THR ASP TYR THR SER SER ILE ASP VAL TRP SER          
SEQRES  17 B  350  ALA GLY CYS VAL LEU ALA GLU LEU LEU LEU GLY GLN PRO          
SEQRES  18 B  350  ILE PHE PRO GLY ASP SER GLY VAL ASP GLN LEU VAL GLU          
SEQRES  19 B  350  ILE ILE LYS VAL LEU GLY THR PRO THR ARG GLU GLN ILE          
SEQRES  20 B  350  ARG GLU MET ASN PRO ASN TYR THR GLU PHE LYS PHE PRO          
SEQRES  21 B  350  GLN ILE LYS ALA HIS PRO TRP THR LYS VAL PHE ARG PRO          
SEQRES  22 B  350  ARG THR PRO PRO GLU ALA ILE ALA LEU CYS SER ARG LEU          
SEQRES  23 B  350  LEU GLU TYR THR PRO THR ALA ARG LEU THR PRO LEU GLU          
SEQRES  24 B  350  ALA CYS ALA HIS SER PHE PHE ASP GLU LEU ARG ASP PRO          
SEQRES  25 B  350  ASN VAL LYS LEU PRO ASN GLY ARG ASP THR PRO ALA LEU          
SEQRES  26 B  350  PHE ASN PHE THR THR GLN GLU LEU SER SER ASN PRO PRO          
SEQRES  27 B  350  LEU ALA THR ILE LEU ILE PRO PRO HIS ALA ARG ILE              
SEQRES   1 N    8  GLY SER HIS GLY HIS HIS HIS HIS                              
MODRES 6HK3 PTR A  216  TYR  MODIFIED RESIDUE                                   
MODRES 6HK3 PTR B  216  TYR  MODIFIED RESIDUE                                   
HET    PTR  A 216      16                                                       
HET    PTR  B 216      16                                                       
HET    G8B  A 401      34                                                       
HET    MLI  A 402       7                                                       
HET    GOL  A 403       6                                                       
HET    GOL  A 404       6                                                       
HET    GOL  A 405       6                                                       
HET     CL  A 406       1                                                       
HET    DMS  A 407       4                                                       
HET    G8B  B 401      34                                                       
HET    MLI  B 402       7                                                       
HET    GOL  B 403       6                                                       
HET     CL  B 404       1                                                       
HET    DMS  B 405       4                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     G8B 3-AZANYL-~{N}-(2-METHOXYPHENYL)-6-[4-(4-                         
HETNAM   2 G8B  METHYLPIPERAZIN-1-YL)SULFONYLPHENYL]PYRAZINE-2-                 
HETNAM   3 G8B  CARBOXAMIDE                                                     
HETNAM     MLI MALONATE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETSYN     PTR PHOSPHONOTYROSINE                                                
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  PTR    2(C9 H12 N O6 P)                                             
FORMUL   4  G8B    2(C23 H26 N6 O4 S)                                           
FORMUL   5  MLI    2(C3 H2 O4 2-)                                               
FORMUL   6  GOL    4(C3 H8 O3)                                                  
FORMUL   9   CL    2(CL 1-)                                                     
FORMUL  10  DMS    2(C2 H6 O S)                                                 
FORMUL  16  HOH   *188(H2 O)                                                    
HELIX    1 AA1 ASN A   95  LYS A  103  1                                   9    
HELIX    2 AA2 VAL A  139  ALA A  149  1                                  11    
HELIX    3 AA3 PRO A  154  SER A  174  1                                  21    
HELIX    4 AA4 LYS A  183  GLN A  185  5                                   3    
HELIX    5 AA5 SER A  219  ARG A  223  5                                   5    
HELIX    6 AA6 ALA A  224  PHE A  229  1                                   6    
HELIX    7 AA7 SER A  236  GLY A  253  1                                  18    
HELIX    8 AA8 VAL A  263  GLY A  274  1                                  12    
HELIX    9 AA9 THR A  277  ASN A  285  1                                   9    
HELIX   10 AB1 PRO A  300  PHE A  305  1                                   6    
HELIX   11 AB2 PRO A  310  ARG A  319  1                                  10    
HELIX   12 AB3 THR A  330  ALA A  336  1                                   7    
HELIX   13 AB4 HIS A  337  PHE A  339  5                                   3    
HELIX   14 AB5 PHE A  340  ASP A  345  1                                   6    
HELIX   15 AB6 GLN A  365  PRO A  372  5                                   8    
HELIX   16 AB7 LEU A  373  ILE A  378  1                                   6    
HELIX   17 AB8 PRO A  379  ARG A  383  5                                   5    
HELIX   18 AB9 ASN B   95  LEU B  104  1                                  10    
HELIX   19 AC1 VAL B  139  ALA B  149  1                                  11    
HELIX   20 AC2 PRO B  154  PHE B  175  1                                  22    
HELIX   21 AC3 LYS B  183  GLN B  185  5                                   3    
HELIX   22 AC4 SER B  219  ARG B  223  5                                   5    
HELIX   23 AC5 ALA B  224  PHE B  229  1                                   6    
HELIX   24 AC6 SER B  236  GLY B  253  1                                  18    
HELIX   25 AC7 VAL B  263  GLY B  274  1                                  12    
HELIX   26 AC8 THR B  277  ASN B  285  1                                   9    
HELIX   27 AC9 PRO B  300  PHE B  305  5                                   6    
HELIX   28 AD1 PRO B  310  ARG B  319  1                                  10    
HELIX   29 AD2 THR B  324  ARG B  328  5                                   5    
HELIX   30 AD3 THR B  330  ALA B  336  1                                   7    
HELIX   31 AD4 HIS B  337  ARG B  344  5                                   8    
HELIX   32 AD5 ASN B  370  PRO B  372  5                                   3    
HELIX   33 AD6 LEU B  373  ILE B  378  1                                   6    
HELIX   34 AD7 PRO B  379  ARG B  383  5                                   5    
SHEET    1 AA1 7 VAL A  37  PRO A  44  0                                        
SHEET    2 AA1 7 GLN A  52  ASN A  64 -1  O  VAL A  54   N  VAL A  40           
SHEET    3 AA1 7 GLY A  68  LEU A  75 -1  O  LYS A  74   N  THR A  57           
SHEET    4 AA1 7 LEU A  81  LEU A  88 -1  O  LYS A  86   N  VAL A  69           
SHEET    5 AA1 7 TYR A 127  ASP A 133 -1  O  LEU A 132   N  ALA A  83           
SHEET    6 AA1 7 LEU A 112  SER A 118 -1  N  SER A 118   O  TYR A 127           
SHEET    7 AA1 7 VAL A  37  PRO A  44 -1  N  THR A  43   O  PHE A 115           
SHEET    1 AA2 3 GLU A 137  THR A 138  0                                        
SHEET    2 AA2 3 LEU A 187  LEU A 189 -1  O  LEU A 189   N  GLU A 137           
SHEET    3 AA2 3 LEU A 196  LEU A 198 -1  O  LYS A 197   N  LEU A 188           
SHEET    1 AA3 2 ILE A 177  CYS A 178  0                                        
SHEET    2 AA3 2 LYS A 205  GLN A 206 -1  O  LYS A 205   N  CYS A 178           
SHEET    1 AA4 7 VAL B  37  PRO B  44  0                                        
SHEET    2 AA4 7 GLN B  52  GLY B  65 -1  O  VAL B  54   N  VAL B  40           
SHEET    3 AA4 7 GLY B  68  LEU B  75 -1  O  LYS B  74   N  THR B  57           
SHEET    4 AA4 7 LEU B  81  LEU B  88 -1  O  VAL B  82   N  ALA B  73           
SHEET    5 AA4 7 VAL B 126  ASP B 133 -1  O  LEU B 132   N  ALA B  83           
SHEET    6 AA4 7 LEU B 112  SER B 119 -1  N  TYR B 114   O  VAL B 131           
SHEET    7 AA4 7 VAL B  37  PRO B  44 -1  N  THR B  43   O  PHE B 115           
SHEET    1 AA5 3 GLU B 137  THR B 138  0                                        
SHEET    2 AA5 3 LEU B 187  ASP B 190 -1  O  LEU B 189   N  GLU B 137           
SHEET    3 AA5 3 VAL B 195  LEU B 198 -1  O  LYS B 197   N  LEU B 188           
SHEET    1 AA6 2 ILE B 177  CYS B 178  0                                        
SHEET    2 AA6 2 LYS B 205  GLN B 206 -1  O  LYS B 205   N  CYS B 178           
LINK         C   SER A 215                 N   PTR A 216     1555   1555  1.32  
LINK         C   PTR A 216                 N   ILE A 217     1555   1555  1.34  
LINK         C   SER B 215                 N   PTR B 216     1555   1555  1.32  
LINK         C   PTR B 216                 N   ILE B 217     1555   1555  1.33  
SITE     1 AC1 14 ALA A  83  LYS A  85  VAL A 110  ASP A 133                    
SITE     2 AC1 14 TYR A 134  VAL A 135  PRO A 136  ARG A 141                    
SITE     3 AC1 14 LEU A 188  ASP A 200  GOL A 404  HOH A 522                    
SITE     4 AC1 14 HOH A 533  HOH A 540                                          
SITE     1 AC2  6 ARG A  96  ARG A 180  LYS A 205  ASN A 213                    
SITE     2 AC2  6 VAL A 214  HOH A 546                                          
SITE     1 AC3  6 TYR A  56  THR A  59  TYR A  71  LYS A  86                    
SITE     2 AC3  6 ASN A 129  GLU B 290                                          
SITE     1 AC4  5 TYR A 140  ARG A 141  GLN A 185  G8B A 401                    
SITE     2 AC4  5 HOH A 530                                                     
SITE     1 AC5  3 PTR A 216  SER A 219  ARG A 220                               
SITE     1 AC6  2 ARG A 167  GLU A 366                                          
SITE     1 AC7  3 TYR A 146  TYR A 157  TYR A 161                               
SITE     1 AC8 12 ALA B  83  LYS B  85  VAL B 110  ASP B 133                    
SITE     2 AC8 12 TYR B 134  VAL B 135  PRO B 136  ARG B 141                    
SITE     3 AC8 12 LEU B 188  ASP B 200  HOH B 537  HOH B 559                    
SITE     1 AC9  6 ARG B  96  ARG B 180  LYS B 205  ASN B 213                    
SITE     2 AC9  6 VAL B 214  HOH B 536                                          
SITE     1 AD1  3 TYR B  56  LYS B  86  ASN B 129                               
SITE     1 AD2  2 HIS B 106  GLU B 366                                          
SITE     1 AD3  3 PRO A  51  TYR B 157  TYR B 161                               
CRYST1   64.318   67.117   67.238  79.84  76.21  89.63 P 1           2          
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      0.015548 -0.000100 -0.003861        0.00000                         
SCALE2      0.000000  0.014900 -0.002727        0.00000                         
SCALE3      0.000000  0.000000  0.015568        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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