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Database: PDB
Entry: 2OW3
LinkDB: 2OW3
Original site: 2OW3 
HEADER    TRANSFERASE                             15-FEB-07   2OW3              
TITLE     GLYCOGEN SYNTHASE KINASE-3 BETA IN COMPLEX WITH BIS-(INDOLE)MALEIMIDE 
TITLE    2 PYRIDINOPHANE INHIBITOR                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLYCOGEN SYNTHASE KINASE-3 BETA;                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 35-386;                                           
COMPND   5 SYNONYM: GSK-3 BETA;                                                 
COMPND   6 EC: 2.7.11.26;                                                       
COMPND   7 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                                                          
KEYWDS    KINASE-INHIBITOR COMPLEX, TRANSFERASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.C.ZHANG,L.V.BONAGA,H.YE,C.K.DERIAN,B.P.DAMIANO,B.E.MARYANOFF        
REVDAT   3   18-OCT-17 2OW3    1       REMARK                                   
REVDAT   2   24-FEB-09 2OW3    1       VERSN                                    
REVDAT   1   19-FEB-08 2OW3    0                                                
JRNL        AUTH   H.C.ZHANG,L.V.BONAGA,H.YE,C.K.DERIAN,B.P.DAMIANO,            
JRNL        AUTH 2 B.E.MARYANOFF                                                
JRNL        TITL   NOVEL BIS(INDOLYL)MALEIMIDE PYRIDINOPHANES THAT ARE POTENT,  
JRNL        TITL 2 SELECTIVE INHIBITORS OF GLYCOGEN SYNTHASE KINASE-3.          
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  17  2863 2007              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   17350261                                                     
JRNL        DOI    10.1016/J.BMCL.2007.02.059                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 67.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 25427                          
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) : 0.248                           
REMARK   3   R VALUE            (WORKING SET) : 0.246                           
REMARK   3   FREE R VALUE                     : 0.295                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1032                            
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1277                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 66.13                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3540                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 35                           
REMARK   3   BIN FREE R VALUE                    : 0.4170                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5584                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 82                                      
REMARK   3   SOLVENT ATOMS            : 15                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 82.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 61.55                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.31000                                             
REMARK   3    B22 (A**2) : 6.45000                                              
REMARK   3    B33 (A**2) : -4.57000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.94000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 1.222         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.409         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.338         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.974        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.904                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.862                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5745 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  5265 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7836 ; 1.033 ; 1.998       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 12232 ; 0.742 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   686 ; 5.404 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   250 ;32.170 ;23.040       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   933 ;16.102 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    44 ;12.358 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   866 ; 0.060 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6284 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1186 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1179 ; 0.188 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4981 ; 0.166 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2778 ; 0.173 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2986 ; 0.081 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    69 ; 0.118 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    10 ; 0.075 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    27 ; 0.168 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     1 ; 0.061 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4491 ; 1.320 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1363 ; 0.184 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5656 ; 1.670 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2732 ; 2.145 ; 4.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2180 ; 3.245 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2OW3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-APR-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000041656.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-MAY-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : DYNAMICALLY BLENDABLE MIRROR       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25427                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 67.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.11500                            
REMARK 200  R SYM                      (I) : 0.11500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.08540                            
REMARK 200  R SYM FOR SHELL            (I) : 0.08540                            
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: CCP4                                                  
REMARK 200 STARTING MODEL: PREVIOUSLY DERIVED MODEL (ORIGINALLY FROM 1H8F)      
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG2000, BICINE PH9.0                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       58.66450            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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 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     SER A   119                                                      
REMARK 465     GLY A   120                                                      
REMARK 465     GLU A   121                                                      
REMARK 465     LYS A   122                                                      
REMARK 465     ALA A   386                                                      
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     ASP A  90    CB   CG   OD1  OD2                                  
REMARK 470     ARG A  92    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 292    CG   CD   CE   NZ                                   
REMARK 470     ASP B  90    CB   CG   OD1  OD2                                  
REMARK 470     ARG B  92    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 292    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    LYS A   292     CD1  PHE A   293              1.21            
REMARK 500   O    GLU B   125     CG2  VAL B   126              1.72            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    TYR B 117   O   -  C   -  N   ANGL. DEV. = -10.6 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    ASN A  64      102.67   -174.01                                   
REMARK 500    ASP A  90       88.93    -62.69                                   
REMARK 500    LYS A  91      -46.91    -27.93                                   
REMARK 500    ASP A 105       87.06   -153.07                                   
REMARK 500    ASP A 124      -66.77      0.41                                   
REMARK 500    VAL A 126      102.06     45.70                                   
REMARK 500    SER A 174        4.13    -70.00                                   
REMARK 500    ASP A 181       58.67   -166.82                                   
REMARK 500    ALA A 194       -4.52     87.71                                   
REMARK 500    ASP A 200       79.70     62.63                                   
REMARK 500    PHE A 201       38.01    -96.04                                   
REMARK 500    CYS A 218      154.82     77.18                                   
REMARK 500    ASP A 233       55.20   -119.61                                   
REMARK 500    PRO A 258      -91.28    -66.31                                   
REMARK 500    PRO A 286       43.28    -76.79                                   
REMARK 500    PHE A 293      117.04    165.11                                   
REMARK 500    PRO A 294      156.76    -33.43                                   
REMARK 500    LYS A 303       41.13    -96.33                                   
REMARK 500    ASN A 370       74.00   -161.40                                   
REMARK 500    ILE A 384      105.98    -54.00                                   
REMARK 500    THR B  57     -154.20   -149.70                                   
REMARK 500    ASN B  64       78.63   -153.92                                   
REMARK 500    GLU B 121     -127.02    -57.40                                   
REMARK 500    LYS B 122       69.84     18.08                                   
REMARK 500    LYS B 123     -135.34     51.36                                   
REMARK 500    ASP B 124     -123.51    -89.03                                   
REMARK 500    GLU B 125     -112.75     85.37                                   
REMARK 500    VAL B 126      149.76    144.92                                   
REMARK 500    ASP B 181       59.80   -162.35                                   
REMARK 500    ASN B 186       20.49    -74.81                                   
REMARK 500    ASP B 200       80.36     62.87                                   
REMARK 500    PHE B 201       34.08    -94.83                                   
REMARK 500    CYS B 218      163.87     81.52                                   
REMARK 500    THR B 235     -162.39   -112.40                                   
REMARK 500    PHE B 257       75.24   -116.00                                   
REMARK 500    PRO B 258      -90.83    -63.23                                   
REMARK 500    ASN B 285      110.66   -161.58                                   
REMARK 500    ASN B 287       17.09   -140.39                                   
REMARK 500    THR B 289      -53.72   -144.80                                   
REMARK 500    PHE B 340       30.61    -98.68                                   
REMARK 500    ASN B 361       51.36   -114.17                                   
REMARK 500    ASN B 370       77.02   -162.47                                   
REMARK 500    PRO B 372        7.83    -59.74                                   
REMARK 500    GLN B 385      -30.09   -134.88                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    TYR B 117        -17.92                                           
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 BIM A 387                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BIM B 387                 
DBREF  2OW3 A   35   386  UNP    P49841   GSK3B_HUMAN     35    386             
DBREF  2OW3 B   35   386  UNP    P49841   GSK3B_HUMAN     35    386             
SEQADV 2OW3 PTR A  216  UNP  P49841    TYR   216 MODIFIED RESIDUE               
SEQADV 2OW3 PTR B  216  UNP  P49841    TYR   216 MODIFIED RESIDUE               
SEQRES   1 A  352  SER LYS VAL THR THR VAL VAL ALA THR PRO GLY GLN GLY          
SEQRES   2 A  352  PRO ASP ARG PRO GLN GLU VAL SER TYR THR ASP THR LYS          
SEQRES   3 A  352  VAL ILE GLY ASN GLY SER PHE GLY VAL VAL TYR GLN ALA          
SEQRES   4 A  352  LYS LEU CYS ASP SER GLY GLU LEU VAL ALA ILE LYS LYS          
SEQRES   5 A  352  VAL LEU GLN ASP LYS ARG PHE LYS ASN ARG GLU LEU GLN          
SEQRES   6 A  352  ILE MET ARG LYS LEU ASP HIS CYS ASN ILE VAL ARG LEU          
SEQRES   7 A  352  ARG TYR PHE PHE TYR SER SER GLY GLU LYS LYS ASP GLU          
SEQRES   8 A  352  VAL TYR LEU ASN LEU VAL LEU ASP TYR VAL PRO GLU THR          
SEQRES   9 A  352  VAL TYR ARG VAL ALA ARG HIS TYR SER ARG ALA LYS GLN          
SEQRES  10 A  352  THR LEU PRO VAL ILE TYR VAL LYS LEU TYR MET TYR GLN          
SEQRES  11 A  352  LEU PHE ARG SER LEU ALA TYR ILE HIS SER PHE GLY ILE          
SEQRES  12 A  352  CYS HIS ARG ASP ILE LYS PRO GLN ASN LEU LEU LEU ASP          
SEQRES  13 A  352  PRO ASP THR ALA VAL LEU LYS LEU CYS ASP PHE GLY SER          
SEQRES  14 A  352  ALA LYS GLN LEU VAL ARG GLY GLU PRO ASN VAL SER PTR          
SEQRES  15 A  352  ILE CYS SER ARG TYR TYR ARG ALA PRO GLU LEU ILE PHE          
SEQRES  16 A  352  GLY ALA THR ASP TYR THR SER SER ILE ASP VAL TRP SER          
SEQRES  17 A  352  ALA GLY CYS VAL LEU ALA GLU LEU LEU LEU GLY GLN PRO          
SEQRES  18 A  352  ILE PHE PRO GLY ASP SER GLY VAL ASP GLN LEU VAL GLU          
SEQRES  19 A  352  ILE ILE LYS VAL LEU GLY THR PRO THR ARG GLU GLN ILE          
SEQRES  20 A  352  ARG GLU MET ASN PRO ASN TYR THR GLU PHE LYS PHE PRO          
SEQRES  21 A  352  GLN ILE LYS ALA HIS PRO TRP THR LYS VAL PHE ARG PRO          
SEQRES  22 A  352  ARG THR PRO PRO GLU ALA ILE ALA LEU CYS SER ARG LEU          
SEQRES  23 A  352  LEU GLU TYR THR PRO THR ALA ARG LEU THR PRO LEU GLU          
SEQRES  24 A  352  ALA CYS ALA HIS SER PHE PHE ASP GLU LEU ARG ASP PRO          
SEQRES  25 A  352  ASN VAL LYS LEU PRO ASN GLY ARG ASP THR PRO ALA LEU          
SEQRES  26 A  352  PHE ASN PHE THR THR GLN GLU LEU SER SER ASN PRO PRO          
SEQRES  27 A  352  LEU ALA THR ILE LEU ILE PRO PRO HIS ALA ARG ILE GLN          
SEQRES  28 A  352  ALA                                                          
SEQRES   1 B  352  SER LYS VAL THR THR VAL VAL ALA THR PRO GLY GLN GLY          
SEQRES   2 B  352  PRO ASP ARG PRO GLN GLU VAL SER TYR THR ASP THR LYS          
SEQRES   3 B  352  VAL ILE GLY ASN GLY SER PHE GLY VAL VAL TYR GLN ALA          
SEQRES   4 B  352  LYS LEU CYS ASP SER GLY GLU LEU VAL ALA ILE LYS LYS          
SEQRES   5 B  352  VAL LEU GLN ASP LYS ARG PHE LYS ASN ARG GLU LEU GLN          
SEQRES   6 B  352  ILE MET ARG LYS LEU ASP HIS CYS ASN ILE VAL ARG LEU          
SEQRES   7 B  352  ARG TYR PHE PHE TYR SER SER GLY GLU LYS LYS ASP GLU          
SEQRES   8 B  352  VAL TYR LEU ASN LEU VAL LEU ASP TYR VAL PRO GLU THR          
SEQRES   9 B  352  VAL TYR ARG VAL ALA ARG HIS TYR SER ARG ALA LYS GLN          
SEQRES  10 B  352  THR LEU PRO VAL ILE TYR VAL LYS LEU TYR MET TYR GLN          
SEQRES  11 B  352  LEU PHE ARG SER LEU ALA TYR ILE HIS SER PHE GLY ILE          
SEQRES  12 B  352  CYS HIS ARG ASP ILE LYS PRO GLN ASN LEU LEU LEU ASP          
SEQRES  13 B  352  PRO ASP THR ALA VAL LEU LYS LEU CYS ASP PHE GLY SER          
SEQRES  14 B  352  ALA LYS GLN LEU VAL ARG GLY GLU PRO ASN VAL SER PTR          
SEQRES  15 B  352  ILE CYS SER ARG TYR TYR ARG ALA PRO GLU LEU ILE PHE          
SEQRES  16 B  352  GLY ALA THR ASP TYR THR SER SER ILE ASP VAL TRP SER          
SEQRES  17 B  352  ALA GLY CYS VAL LEU ALA GLU LEU LEU LEU GLY GLN PRO          
SEQRES  18 B  352  ILE PHE PRO GLY ASP SER GLY VAL ASP GLN LEU VAL GLU          
SEQRES  19 B  352  ILE ILE LYS VAL LEU GLY THR PRO THR ARG GLU GLN ILE          
SEQRES  20 B  352  ARG GLU MET ASN PRO ASN TYR THR GLU PHE LYS PHE PRO          
SEQRES  21 B  352  GLN ILE LYS ALA HIS PRO TRP THR LYS VAL PHE ARG PRO          
SEQRES  22 B  352  ARG THR PRO PRO GLU ALA ILE ALA LEU CYS SER ARG LEU          
SEQRES  23 B  352  LEU GLU TYR THR PRO THR ALA ARG LEU THR PRO LEU GLU          
SEQRES  24 B  352  ALA CYS ALA HIS SER PHE PHE ASP GLU LEU ARG ASP PRO          
SEQRES  25 B  352  ASN VAL LYS LEU PRO ASN GLY ARG ASP THR PRO ALA LEU          
SEQRES  26 B  352  PHE ASN PHE THR THR GLN GLU LEU SER SER ASN PRO PRO          
SEQRES  27 B  352  LEU ALA THR ILE LEU ILE PRO PRO HIS ALA ARG ILE GLN          
SEQRES  28 B  352  ALA                                                          
MODRES 2OW3 PTR A  216  TYR  O-PHOSPHOTYROSINE                                  
MODRES 2OW3 PTR B  216  TYR  O-PHOSPHOTYROSINE                                  
HET    PTR  A 216      16                                                       
HET    PTR  B 216      16                                                       
HET    BIM  A 387      41                                                       
HET    BIM  B 387      41                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     BIM BIS-(INDOLE)MALEIMIDE PYRIDINOPHANE                              
HETSYN     PTR PHOSPHONOTYROSINE                                                
FORMUL   1  PTR    2(C9 H12 N O6 P)                                             
FORMUL   3  BIM    2(C34 H33 N5 O2)                                             
FORMUL   5  HOH   *15(H2 O)                                                     
HELIX    1   1 ASN A   95  ARG A  102  1                                   8    
HELIX    2   2 VAL A  139  ALA A  149  1                                  11    
HELIX    3   3 PRO A  154  SER A  174  1                                  21    
HELIX    4   4 LYS A  183  GLN A  185  5                                   3    
HELIX    5   5 SER A  219  ARG A  223  5                                   5    
HELIX    6   6 ALA A  224  GLY A  230  1                                   7    
HELIX    7   7 SER A  236  GLY A  253  1                                  18    
HELIX    8   8 ASP A  264  GLY A  274  1                                  11    
HELIX    9   9 THR A  277  ASN A  285  1                                   9    
HELIX   10  10 PRO A  310  LEU A  321  1                                  12    
HELIX   11  11 THR A  324  ARG A  328  5                                   5    
HELIX   12  12 THR A  330  ALA A  336  1                                   7    
HELIX   13  13 HIS A  337  ASP A  345  5                                   9    
HELIX   14  14 THR A  363  SER A  368  1                                   6    
HELIX   15  15 ASN A  370  PRO A  372  5                                   3    
HELIX   16  16 LEU A  373  ILE A  378  1                                   6    
HELIX   17  17 PRO A  379  ARG A  383  5                                   5    
HELIX   18  18 ASN B   95  LYS B  103  1                                   9    
HELIX   19  19 VAL B  139  ARG B  148  1                                  10    
HELIX   20  20 PRO B  154  SER B  174  1                                  21    
HELIX   21  21 LYS B  183  GLN B  185  5                                   3    
HELIX   22  22 SER B  219  ARG B  223  5                                   5    
HELIX   23  23 ALA B  224  PHE B  229  1                                   6    
HELIX   24  24 SER B  236  GLY B  253  1                                  18    
HELIX   25  25 VAL B  263  GLY B  274  1                                  12    
HELIX   26  26 THR B  277  ASN B  285  1                                   9    
HELIX   27  27 PRO B  300  VAL B  304  5                                   5    
HELIX   28  28 PRO B  310  ARG B  319  1                                  10    
HELIX   29  29 THR B  324  ARG B  328  5                                   5    
HELIX   30  30 THR B  330  ALA B  336  1                                   7    
HELIX   31  31 HIS B  337  ASP B  345  5                                   9    
HELIX   32  32 THR B  363  SER B  368  1                                   6    
HELIX   33  33 ASN B  370  PRO B  372  5                                   3    
HELIX   34  34 LEU B  373  ILE B  378  1                                   6    
HELIX   35  35 PRO B  379  ILE B  384  1                                   6    
SHEET    1   A 7 THR A  38  PRO A  44  0                                        
SHEET    2   A 7 GLN A  52  GLY A  65 -1  O  VAL A  54   N  VAL A  40           
SHEET    3   A 7 GLY A  68  LEU A  75 -1  O  GLN A  72   N  LYS A  60           
SHEET    4   A 7 LEU A  81  LEU A  88 -1  O  VAL A  82   N  ALA A  73           
SHEET    5   A 7 TYR A 127  ASP A 133 -1  O  LEU A 128   N  VAL A  87           
SHEET    6   A 7 LEU A 112  SER A 118 -1  N  TYR A 114   O  VAL A 131           
SHEET    7   A 7 THR A  38  PRO A  44 -1  N  THR A  43   O  PHE A 115           
SHEET    1   B 3 GLU A 137  THR A 138  0                                        
SHEET    2   B 3 LEU A 187  LEU A 189 -1  O  LEU A 189   N  GLU A 137           
SHEET    3   B 3 LEU A 196  LEU A 198 -1  O  LYS A 197   N  LEU A 188           
SHEET    1   C 2 ILE A 177  CYS A 178  0                                        
SHEET    2   C 2 LYS A 205  GLN A 206 -1  O  LYS A 205   N  CYS A 178           
SHEET    1   D 7 THR B  38  PRO B  44  0                                        
SHEET    2   D 7 GLN B  52  GLY B  65 -1  O  TYR B  56   N  THR B  38           
SHEET    3   D 7 GLY B  68  LEU B  75 -1  O  GLY B  68   N  GLY B  65           
SHEET    4   D 7 LEU B  81  LEU B  88 -1  O  ILE B  84   N  TYR B  71           
SHEET    5   D 7 TYR B 127  ASP B 133 -1  O  LEU B 128   N  VAL B  87           
SHEET    6   D 7 LEU B 112  PHE B 116 -1  N  PHE B 116   O  ASN B 129           
SHEET    7   D 7 THR B  38  PRO B  44 -1  N  THR B  43   O  PHE B 115           
SHEET    1   E 3 GLU B 137  THR B 138  0                                        
SHEET    2   E 3 LEU B 187  LEU B 189 -1  O  LEU B 189   N  GLU B 137           
SHEET    3   E 3 LEU B 196  LEU B 198 -1  O  LYS B 197   N  LEU B 188           
SHEET    1   F 2 ILE B 177  CYS B 178  0                                        
SHEET    2   F 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  1.33  
LINK         C   PTR A 216                 N   ILE A 217     1555   1555  1.33  
LINK         C   SER B 215                 N   PTR B 216     1555   1555  1.34  
LINK         C   PTR B 216                 N   ILE B 217     1555   1555  1.33  
SITE     1 AC1 12 ILE A  62  PHE A  67  ASP A 133  TYR A 134                    
SITE     2 AC1 12 VAL A 135  PRO A 136  THR A 138  GLN A 185                    
SITE     3 AC1 12 LEU A 188  CYS A 199  ASP A 200  HOH A 389                    
SITE     1 AC2 10 ILE B  62  ALA B  83  ASP B 133  TYR B 134                    
SITE     2 AC2 10 VAL B 135  PRO B 136  THR B 138  ASN B 186                    
SITE     3 AC2 10 CYS B 199  ASP B 200                                          
CRYST1   69.472  117.329   69.461  90.00 103.22  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014394  0.000000  0.003380        0.00000                         
SCALE2      0.000000  0.008523  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014788        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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