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Database: PDB
Entry: 3SAY
LinkDB: 3SAY
Original site: 3SAY 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       03-JUN-11   3SAY              
TITLE     CRYSTAL STRUCTURE OF HUMAN GLYCOGEN SYNTHASE KINASE 3 BETA (GSK3B) IN 
TITLE    2 COMPLEX WITH INHIBITOR 142                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLYCOGEN SYNTHASE KINASE-3 BETA;                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: GSK-3 BETA;                                                 
COMPND   5 EC: 2.7.11.26;                                                       
COMPND   6 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: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PTRI-EX                                   
KEYWDS    KINASE, ATP HYDROLYSIS, PHOSPHORYLATION, TRANSFERASE-TRANSFERASE      
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.P.MAZANETZ,R.K.Y.CHENG,F.ROWAN,C.A.LAUGHTON,J.J.BARKER,P.M.FISCHER  
REVDAT   4   28-DEC-16 3SAY    1       AUTHOR                                   
REVDAT   3   07-DEC-16 3SAY    1       AUTHOR                                   
REVDAT   2   29-APR-15 3SAY    1       HETSYN                                   
REVDAT   1   13-JUN-12 3SAY    0                                                
JRNL        AUTH   R.K.Y.CHENG,F.ROWAN,J.J.BARKER                               
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN GLYCOGEN SYNTHASE KINASE 3 BETA   
JRNL        TITL 2 (GSK3B) IN COMPLEX WITH INHIBITOR 142                        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.23 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 2.23                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.14                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 44525                          
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) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2373                            
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) : 2.23                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.29                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2474                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 73.75                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3080                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 142                          
REMARK   3   BIN FREE R VALUE                    : 0.3700                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5474                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 83                                      
REMARK   3   SOLVENT ATOMS            : 221                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 41.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.11                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.64000                                             
REMARK   3    B22 (A**2) : 9.63000                                              
REMARK   3    B33 (A**2) : -5.99000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -11.31000                                            
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.051         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.040         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.136         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.911         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.926                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5796 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7942 ; 1.592 ; 1.994       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   722 ; 5.980 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   245 ;35.929 ;23.224       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   923 ;16.289 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    40 ;22.291 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   898 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4430 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  3549 ; 0.850 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5798 ; 1.564 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2247 ; 1.973 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2128 ; 3.227 ; 4.500       
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  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 2                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H, K, L                                         
REMARK   3      TWIN FRACTION : 0.864                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : L, -K, H                                        
REMARK   3      TWIN FRACTION : 0.136                                           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 3SAY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB065981.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-SEP-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I24                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9778                             
REMARK 200  MONOCHROMATOR                  : ACCEL FIXED EXIT DOUBLE CRYSTAL    
REMARK 200  OPTICS                         : OXFORD DANFYSIK/SESO TWO STAGE     
REMARK 200                                   DEMAGNIFICATION USING TWO K-B      
REMARK 200                                   PAIRS OF BIMORPH TYPE MIRRORS      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46924                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.231                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.140                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : 0.10000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.23                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.56100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
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: PDB ENTRY 2JLD CHAIN A                               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.1M SODIUM HEPES PH 7.0,   
REMARK 280  2% (V/V) TACSIMATE PH 7.0, VAPOR DIFFUSION, SITTING DROP,           
REMARK 280  TEMPERATURE 296K                                                    
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       55.39000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     ARG A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     PHE A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     GLU A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     CYS A    14                                                      
REMARK 465     LYS A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     VAL A    17                                                      
REMARK 465     GLN A    18                                                      
REMARK 465     GLN A    19                                                      
REMARK 465     PRO A    20                                                      
REMARK 465     SER A    21                                                      
REMARK 465     ALA A    22                                                      
REMARK 465     PHE A    23                                                      
REMARK 465     GLY A    24                                                      
REMARK 465     SER A    25                                                      
REMARK 465     MET A    26                                                      
REMARK 465     LYS A    27                                                      
REMARK 465     VAL A    28                                                      
REMARK 465     SER A    29                                                      
REMARK 465     ARG A    30                                                      
REMARK 465     ASP A    31                                                      
REMARK 465     LYS A    32                                                      
REMARK 465     ASP A    33                                                      
REMARK 465     GLY A    34                                                      
REMARK 465     THR A   289                                                      
REMARK 465     GLU A   290                                                      
REMARK 465     GLN A   385                                                      
REMARK 465     ALA A   386                                                      
REMARK 465     ALA A   387                                                      
REMARK 465     ALA A   388                                                      
REMARK 465     SER A   389                                                      
REMARK 465     THR A   390                                                      
REMARK 465     PRO A   391                                                      
REMARK 465     THR A   392                                                      
REMARK 465     ASN A   393                                                      
REMARK 465     ALA A   394                                                      
REMARK 465     THR A   395                                                      
REMARK 465     ALA A   396                                                      
REMARK 465     ALA A   397                                                      
REMARK 465     SER A   398                                                      
REMARK 465     ASP A   399                                                      
REMARK 465     ALA A   400                                                      
REMARK 465     ASN A   401                                                      
REMARK 465     THR A   402                                                      
REMARK 465     GLY A   403                                                      
REMARK 465     ASP A   404                                                      
REMARK 465     ARG A   405                                                      
REMARK 465     GLY A   406                                                      
REMARK 465     GLN A   407                                                      
REMARK 465     THR A   408                                                      
REMARK 465     ASN A   409                                                      
REMARK 465     ASN A   410                                                      
REMARK 465     ALA A   411                                                      
REMARK 465     ALA A   412                                                      
REMARK 465     SER A   413                                                      
REMARK 465     ALA A   414                                                      
REMARK 465     SER A   415                                                      
REMARK 465     ALA A   416                                                      
REMARK 465     SER A   417                                                      
REMARK 465     ASN A   418                                                      
REMARK 465     SER A   419                                                      
REMARK 465     THR A   420                                                      
REMARK 465     LEU A   421                                                      
REMARK 465     GLU A   422                                                      
REMARK 465     HIS A   423                                                      
REMARK 465     HIS A   424                                                      
REMARK 465     HIS A   425                                                      
REMARK 465     HIS A   426                                                      
REMARK 465     HIS A   427                                                      
REMARK 465     HIS A   428                                                      
REMARK 465     HIS A   429                                                      
REMARK 465     HIS A   430                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     ARG B     4                                                      
REMARK 465     PRO B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     THR B     8                                                      
REMARK 465     SER B     9                                                      
REMARK 465     PHE B    10                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     GLU B    12                                                      
REMARK 465     SER B    13                                                      
REMARK 465     CYS B    14                                                      
REMARK 465     LYS B    15                                                      
REMARK 465     PRO B    16                                                      
REMARK 465     VAL B    17                                                      
REMARK 465     GLN B    18                                                      
REMARK 465     GLN B    19                                                      
REMARK 465     PRO B    20                                                      
REMARK 465     SER B    21                                                      
REMARK 465     ALA B    22                                                      
REMARK 465     PHE B    23                                                      
REMARK 465     GLY B    24                                                      
REMARK 465     SER B    25                                                      
REMARK 465     MET B    26                                                      
REMARK 465     LYS B    27                                                      
REMARK 465     VAL B    28                                                      
REMARK 465     SER B    29                                                      
REMARK 465     ARG B    30                                                      
REMARK 465     ASP B    31                                                      
REMARK 465     LYS B    32                                                      
REMARK 465     ASP B    33                                                      
REMARK 465     GLY B    34                                                      
REMARK 465     ARG B   383                                                      
REMARK 465     ILE B   384                                                      
REMARK 465     GLN B   385                                                      
REMARK 465     ALA B   386                                                      
REMARK 465     ALA B   387                                                      
REMARK 465     ALA B   388                                                      
REMARK 465     SER B   389                                                      
REMARK 465     THR B   390                                                      
REMARK 465     PRO B   391                                                      
REMARK 465     THR B   392                                                      
REMARK 465     ASN B   393                                                      
REMARK 465     ALA B   394                                                      
REMARK 465     THR B   395                                                      
REMARK 465     ALA B   396                                                      
REMARK 465     ALA B   397                                                      
REMARK 465     SER B   398                                                      
REMARK 465     ASP B   399                                                      
REMARK 465     ALA B   400                                                      
REMARK 465     ASN B   401                                                      
REMARK 465     THR B   402                                                      
REMARK 465     GLY B   403                                                      
REMARK 465     ASP B   404                                                      
REMARK 465     ARG B   405                                                      
REMARK 465     GLY B   406                                                      
REMARK 465     GLN B   407                                                      
REMARK 465     THR B   408                                                      
REMARK 465     ASN B   409                                                      
REMARK 465     ASN B   410                                                      
REMARK 465     ALA B   411                                                      
REMARK 465     ALA B   412                                                      
REMARK 465     SER B   413                                                      
REMARK 465     ALA B   414                                                      
REMARK 465     SER B   415                                                      
REMARK 465     ALA B   416                                                      
REMARK 465     SER B   417                                                      
REMARK 465     ASN B   418                                                      
REMARK 465     SER B   419                                                      
REMARK 465     THR B   420                                                      
REMARK 465     LEU B   421                                                      
REMARK 465     GLU B   422                                                      
REMARK 465     HIS B   423                                                      
REMARK 465     HIS B   424                                                      
REMARK 465     HIS B   425                                                      
REMARK 465     HIS B   426                                                      
REMARK 465     HIS B   427                                                      
REMARK 465     HIS B   428                                                      
REMARK 465     HIS B   429                                                      
REMARK 465     HIS B   430                                                      
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  92    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE A  93    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     LYS A  94    CG   CD   CE   NZ                                   
REMARK 470     GLU A 121    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 122    CD   CE   NZ                                        
REMARK 470     LYS A 123    CG   CD   CE   NZ                                   
REMARK 470     ASP A 124    CG   OD1  OD2                                       
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     LYS B  91    CG   CD   CE   NZ                                   
REMARK 470     ARG B  92    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  94    CG   CD   CE   NZ                                   
REMARK 470     LYS B 123    CG   CD   CE   NZ                                   
REMARK 470     ASP B 124    CG   OD1  OD2                                       
REMARK 470     ARG B 278    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 279    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 282    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE B 291    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 292    CG   CD   CE   NZ                                   
REMARK 470     LYS B 297    CG   CD   CE   NZ                                   
REMARK 470     LYS B 349    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   OD1  ASP B   341     O    HOH B   511              2.03            
REMARK 500   NZ   LYS B   159     OE1  GLU B   342              2.17            
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    ASP A  77      -71.51    -34.38                                   
REMARK 500    ASP A 181       50.26   -156.81                                   
REMARK 500    ASP A 200       80.75     58.10                                   
REMARK 500    CYS A 218      150.20     70.36                                   
REMARK 500    PRO A 286       21.88    -59.20                                   
REMARK 500    ASN A 287      -46.15   -132.39                                   
REMARK 500    ASN A 370       73.67   -165.16                                   
REMARK 500    ARG A 383      -67.83    -93.07                                   
REMARK 500    LYS B  36      116.53    -38.23                                   
REMARK 500    ASP B  49       37.13    -70.29                                   
REMARK 500    ARG B  92      -72.97    -51.16                                   
REMARK 500    ASP B 181       54.84   -144.89                                   
REMARK 500    ASP B 200       82.08     59.40                                   
REMARK 500    CYS B 218      152.54     72.51                                   
REMARK 500    TYR B 288      -98.31   -116.11                                   
REMARK 500    THR B 289      -25.07     46.41                                   
REMARK 500    GLU B 290       64.07    -61.98                                   
REMARK 500    ARG B 308       -6.98     79.03                                   
REMARK 500    LEU B 321       71.89   -101.23                                   
REMARK 500    ASN B 370       73.81   -170.91                                   
REMARK 500    PRO B 380      -61.40    -21.71                                   
REMARK 500    HIS B 381       19.00    -65.51                                   
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 OFT A 431                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLA A 432                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 433                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OFT B 431                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLA B 432                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 433                 
DBREF  3SAY A    1   420  UNP    P49841   GSK3B_HUMAN      1    420             
DBREF  3SAY B    1   420  UNP    P49841   GSK3B_HUMAN      1    420             
SEQADV 3SAY LEU A  421  UNP  P49841              EXPRESSION TAG                 
SEQADV 3SAY GLU A  422  UNP  P49841              EXPRESSION TAG                 
SEQADV 3SAY HIS A  423  UNP  P49841              EXPRESSION TAG                 
SEQADV 3SAY HIS A  424  UNP  P49841              EXPRESSION TAG                 
SEQADV 3SAY HIS A  425  UNP  P49841              EXPRESSION TAG                 
SEQADV 3SAY HIS A  426  UNP  P49841              EXPRESSION TAG                 
SEQADV 3SAY HIS A  427  UNP  P49841              EXPRESSION TAG                 
SEQADV 3SAY HIS A  428  UNP  P49841              EXPRESSION TAG                 
SEQADV 3SAY HIS A  429  UNP  P49841              EXPRESSION TAG                 
SEQADV 3SAY HIS A  430  UNP  P49841              EXPRESSION TAG                 
SEQADV 3SAY LEU B  421  UNP  P49841              EXPRESSION TAG                 
SEQADV 3SAY GLU B  422  UNP  P49841              EXPRESSION TAG                 
SEQADV 3SAY HIS B  423  UNP  P49841              EXPRESSION TAG                 
SEQADV 3SAY HIS B  424  UNP  P49841              EXPRESSION TAG                 
SEQADV 3SAY HIS B  425  UNP  P49841              EXPRESSION TAG                 
SEQADV 3SAY HIS B  426  UNP  P49841              EXPRESSION TAG                 
SEQADV 3SAY HIS B  427  UNP  P49841              EXPRESSION TAG                 
SEQADV 3SAY HIS B  428  UNP  P49841              EXPRESSION TAG                 
SEQADV 3SAY HIS B  429  UNP  P49841              EXPRESSION TAG                 
SEQADV 3SAY HIS B  430  UNP  P49841              EXPRESSION TAG                 
SEQRES   1 A  430  MET SER GLY ARG PRO ARG THR THR SER PHE ALA GLU SER          
SEQRES   2 A  430  CYS LYS PRO VAL GLN GLN PRO SER ALA PHE GLY SER MET          
SEQRES   3 A  430  LYS VAL SER ARG ASP LYS ASP GLY SER LYS VAL THR THR          
SEQRES   4 A  430  VAL VAL ALA THR PRO GLY GLN GLY PRO ASP ARG PRO GLN          
SEQRES   5 A  430  GLU VAL SER TYR THR ASP THR LYS VAL ILE GLY ASN GLY          
SEQRES   6 A  430  SER PHE GLY VAL VAL TYR GLN ALA LYS LEU CYS ASP SER          
SEQRES   7 A  430  GLY GLU LEU VAL ALA ILE LYS LYS VAL LEU GLN ASP LYS          
SEQRES   8 A  430  ARG PHE LYS ASN ARG GLU LEU GLN ILE MET ARG LYS LEU          
SEQRES   9 A  430  ASP HIS CYS ASN ILE VAL ARG LEU ARG TYR PHE PHE TYR          
SEQRES  10 A  430  SER SER GLY GLU LYS LYS ASP GLU VAL TYR LEU ASN LEU          
SEQRES  11 A  430  VAL LEU ASP TYR VAL PRO GLU THR VAL TYR ARG VAL ALA          
SEQRES  12 A  430  ARG HIS TYR SER ARG ALA LYS GLN THR LEU PRO VAL ILE          
SEQRES  13 A  430  TYR VAL LYS LEU TYR MET TYR GLN LEU PHE ARG SER LEU          
SEQRES  14 A  430  ALA TYR ILE HIS SER PHE GLY ILE CYS HIS ARG ASP ILE          
SEQRES  15 A  430  LYS PRO GLN ASN LEU LEU LEU ASP PRO ASP THR ALA VAL          
SEQRES  16 A  430  LEU LYS LEU CYS ASP PHE GLY SER ALA LYS GLN LEU VAL          
SEQRES  17 A  430  ARG GLY GLU PRO ASN VAL SER PTR ILE CYS SER ARG TYR          
SEQRES  18 A  430  TYR ARG ALA PRO GLU LEU ILE PHE GLY ALA THR ASP TYR          
SEQRES  19 A  430  THR SER SER ILE ASP VAL TRP SER ALA GLY CYS VAL LEU          
SEQRES  20 A  430  ALA GLU LEU LEU LEU GLY GLN PRO ILE PHE PRO GLY ASP          
SEQRES  21 A  430  SER GLY VAL ASP GLN LEU VAL GLU ILE ILE LYS VAL LEU          
SEQRES  22 A  430  GLY THR PRO THR ARG GLU GLN ILE ARG GLU MET ASN PRO          
SEQRES  23 A  430  ASN TYR THR GLU PHE LYS PHE PRO GLN ILE LYS ALA HIS          
SEQRES  24 A  430  PRO TRP THR LYS VAL PHE ARG PRO ARG THR PRO PRO GLU          
SEQRES  25 A  430  ALA ILE ALA LEU CYS SER ARG LEU LEU GLU TYR THR PRO          
SEQRES  26 A  430  THR ALA ARG LEU THR PRO LEU GLU ALA CYS ALA HIS SER          
SEQRES  27 A  430  PHE PHE ASP GLU LEU ARG ASP PRO ASN VAL LYS LEU PRO          
SEQRES  28 A  430  ASN GLY ARG ASP THR PRO ALA LEU PHE ASN PHE THR THR          
SEQRES  29 A  430  GLN GLU LEU SER SER ASN PRO PRO LEU ALA THR ILE LEU          
SEQRES  30 A  430  ILE PRO PRO HIS ALA ARG ILE GLN ALA ALA ALA SER THR          
SEQRES  31 A  430  PRO THR ASN ALA THR ALA ALA SER ASP ALA ASN THR GLY          
SEQRES  32 A  430  ASP ARG GLY GLN THR ASN ASN ALA ALA SER ALA SER ALA          
SEQRES  33 A  430  SER ASN SER THR LEU GLU HIS HIS HIS HIS HIS HIS HIS          
SEQRES  34 A  430  HIS                                                          
SEQRES   1 B  430  MET SER GLY ARG PRO ARG THR THR SER PHE ALA GLU SER          
SEQRES   2 B  430  CYS LYS PRO VAL GLN GLN PRO SER ALA PHE GLY SER MET          
SEQRES   3 B  430  LYS VAL SER ARG ASP LYS ASP GLY SER LYS VAL THR THR          
SEQRES   4 B  430  VAL VAL ALA THR PRO GLY GLN GLY PRO ASP ARG PRO GLN          
SEQRES   5 B  430  GLU VAL SER TYR THR ASP THR LYS VAL ILE GLY ASN GLY          
SEQRES   6 B  430  SER PHE GLY VAL VAL TYR GLN ALA LYS LEU CYS ASP SER          
SEQRES   7 B  430  GLY GLU LEU VAL ALA ILE LYS LYS VAL LEU GLN ASP LYS          
SEQRES   8 B  430  ARG PHE LYS ASN ARG GLU LEU GLN ILE MET ARG LYS LEU          
SEQRES   9 B  430  ASP HIS CYS ASN ILE VAL ARG LEU ARG TYR PHE PHE TYR          
SEQRES  10 B  430  SER SER GLY GLU LYS LYS ASP GLU VAL TYR LEU ASN LEU          
SEQRES  11 B  430  VAL LEU ASP TYR VAL PRO GLU THR VAL TYR ARG VAL ALA          
SEQRES  12 B  430  ARG HIS TYR SER ARG ALA LYS GLN THR LEU PRO VAL ILE          
SEQRES  13 B  430  TYR VAL LYS LEU TYR MET TYR GLN LEU PHE ARG SER LEU          
SEQRES  14 B  430  ALA TYR ILE HIS SER PHE GLY ILE CYS HIS ARG ASP ILE          
SEQRES  15 B  430  LYS PRO GLN ASN LEU LEU LEU ASP PRO ASP THR ALA VAL          
SEQRES  16 B  430  LEU LYS LEU CYS ASP PHE GLY SER ALA LYS GLN LEU VAL          
SEQRES  17 B  430  ARG GLY GLU PRO ASN VAL SER PTR ILE CYS SER ARG TYR          
SEQRES  18 B  430  TYR ARG ALA PRO GLU LEU ILE PHE GLY ALA THR ASP TYR          
SEQRES  19 B  430  THR SER SER ILE ASP VAL TRP SER ALA GLY CYS VAL LEU          
SEQRES  20 B  430  ALA GLU LEU LEU LEU GLY GLN PRO ILE PHE PRO GLY ASP          
SEQRES  21 B  430  SER GLY VAL ASP GLN LEU VAL GLU ILE ILE LYS VAL LEU          
SEQRES  22 B  430  GLY THR PRO THR ARG GLU GLN ILE ARG GLU MET ASN PRO          
SEQRES  23 B  430  ASN TYR THR GLU PHE LYS PHE PRO GLN ILE LYS ALA HIS          
SEQRES  24 B  430  PRO TRP THR LYS VAL PHE ARG PRO ARG THR PRO PRO GLU          
SEQRES  25 B  430  ALA ILE ALA LEU CYS SER ARG LEU LEU GLU TYR THR PRO          
SEQRES  26 B  430  THR ALA ARG LEU THR PRO LEU GLU ALA CYS ALA HIS SER          
SEQRES  27 B  430  PHE PHE ASP GLU LEU ARG ASP PRO ASN VAL LYS LEU PRO          
SEQRES  28 B  430  ASN GLY ARG ASP THR PRO ALA LEU PHE ASN PHE THR THR          
SEQRES  29 B  430  GLN GLU LEU SER SER ASN PRO PRO LEU ALA THR ILE LEU          
SEQRES  30 B  430  ILE PRO PRO HIS ALA ARG ILE GLN ALA ALA ALA SER THR          
SEQRES  31 B  430  PRO THR ASN ALA THR ALA ALA SER ASP ALA ASN THR GLY          
SEQRES  32 B  430  ASP ARG GLY GLN THR ASN ASN ALA ALA SER ALA SER ALA          
SEQRES  33 B  430  SER ASN SER THR LEU GLU HIS HIS HIS HIS HIS HIS HIS          
SEQRES  34 B  430  HIS                                                          
MODRES 3SAY PTR A  216  TYR  O-PHOSPHOTYROSINE                                  
MODRES 3SAY PTR B  216  TYR  O-PHOSPHOTYROSINE                                  
HET    PTR  A 216      16                                                       
HET    PTR  B 216      16                                                       
HET    OFT  A 431      29                                                       
HET    MLA  A 432       7                                                       
HET    FMT  A 433       3                                                       
HET    OFT  B 431      29                                                       
HET    MLA  B 432       7                                                       
HET    MPD  B 433       8                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     OFT (3Z)-N,N-DIETHYL-3-[(3E)-3-(HYDROXYIMINO)-1,3-DIHYDRO-           
HETNAM   2 OFT  2H-INDOL-2-YLIDENE]-2-OXO-2,3-DIHYDRO-1H-INDOLE-5-              
HETNAM   3 OFT  SULFONAMIDE                                                     
HETNAM     MLA MALONIC ACID                                                     
HETNAM     FMT FORMIC ACID                                                      
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
HETSYN     PTR PHOSPHONOTYROSINE                                                
HETSYN     MLA DICARBOXYLIC ACID C3; PROPANEDIOLIC ACID;                        
HETSYN   2 MLA  METHANEDICARBOXYLIC ACID                                        
FORMUL   1  PTR    2(C9 H12 N O6 P)                                             
FORMUL   3  OFT    2(C20 H20 N4 O4 S)                                           
FORMUL   4  MLA    2(C3 H4 O4)                                                  
FORMUL   5  FMT    C H2 O2                                                      
FORMUL   8  MPD    C6 H14 O2                                                    
FORMUL   9  HOH   *221(H2 O)                                                    
HELIX    1   1 ASN A   95  LYS A  103  1                                   9    
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  PHE A  229  1                                   6    
HELIX    7   7 SER A  236  GLY A  253  1                                  18    
HELIX    8   8 SER A  261  GLY A  274  1                                  14    
HELIX    9   9 THR A  277  ASN A  285  1                                   9    
HELIX   10  10 PRO A  300  VAL A  304  5                                   5    
HELIX   11  11 PRO A  310  ARG A  319  1                                  10    
HELIX   12  12 THR A  324  ARG A  328  5                                   5    
HELIX   13  13 THR A  330  ALA A  336  1                                   7    
HELIX   14  14 HIS A  337  ASP A  345  5                                   9    
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  LEU B  104  1                                  10    
HELIX   19  19 VAL B  139  ALA B  149  1                                  11    
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 SER B  261  GLY B  274  1                                  14    
HELIX   26  26 THR B  277  ASN B  285  1                                   9    
HELIX   27  27 PRO B  300  PHE B  305  1                                   6    
HELIX   28  28 PRO B  310  LEU B  321  1                                  12    
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  ARG B  344  5                                   8    
HELIX   32  32 THR B  363  SER B  368  1                                   6    
HELIX   33  33 SER B  369  PRO B  372  5                                   4    
HELIX   34  34 LEU B  373  ILE B  378  1                                   6    
SHEET    1   A 7 VAL A  37  PRO A  44  0                                        
SHEET    2   A 7 GLN A  52  GLY A  65 -1  O  GLN A  52   N  ALA A  42           
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  LYS A  86   N  VAL A  69           
SHEET    5   A 7 TYR A 127  ASP A 133 -1  O  LEU A 130   N  LYS A  85           
SHEET    6   A 7 LEU A 112  SER A 118 -1  N  PHE A 116   O  ASN A 129           
SHEET    7   A 7 VAL A  37  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  ASP A 190 -1  O  LEU A 189   N  GLU A 137           
SHEET    3   B 3 VAL A 195  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  ASN B  64 -1  O  TYR B  56   N  THR B  38           
SHEET    3   D 7 GLY B  68  LEU B  75 -1  O  GLN B  72   N  LYS B  60           
SHEET    4   D 7 LEU B  81  LEU B  88 -1  O  VAL B  82   N  ALA B  73           
SHEET    5   D 7 TYR B 127  ASP B 133 -1  O  LEU B 132   N  ALA B  83           
SHEET    6   D 7 LEU B 112  SER B 118 -1  N  TYR B 114   O  VAL B 131           
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  1.32  
LINK         C   PTR A 216                 N   ILE A 217     1555   1555  1.34  
LINK         C   SER B 215                 N   PTR B 216     1555   1555  1.33  
LINK         C   PTR B 216                 N   ILE B 217     1555   1555  1.34  
SITE     1 AC1 16 PHE A  67  VAL A  70  ALA A  83  LYS A  85                    
SITE     2 AC1 16 LEU A 132  ASP A 133  TYR A 134  VAL A 135                    
SITE     3 AC1 16 PRO A 136  ARG A 141  GLN A 185  ASN A 186                    
SITE     4 AC1 16 LEU A 188  CYS A 199  ASP A 200  HOH A 472                    
SITE     1 AC2  5 ARG A  96  ARG A 180  LYS A 205  ASN A 213                    
SITE     2 AC2  5 VAL A 214                                                     
SITE     1 AC3  1 TYR A  56                                                     
SITE     1 AC4 15 PHE B  67  VAL B  70  ALA B  83  LYS B  85                    
SITE     2 AC4 15 LEU B 132  ASP B 133  TYR B 134  VAL B 135                    
SITE     3 AC4 15 PRO B 136  ARG B 141  ASN B 186  LEU B 188                    
SITE     4 AC4 15 CYS B 199  ASP B 200  HOH B 453                               
SITE     1 AC5  5 ARG B  96  ARG B 180  LYS B 205  ASN B 213                    
SITE     2 AC5  5 VAL B 214                                                     
SITE     1 AC6  3 ILE B 228  VAL B 263  TYR B 288                               
CRYST1   67.520  110.780   67.910  90.00  97.08  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      0.014810  0.000000  0.001839        0.00000                         
SCALE2      0.000000  0.009027  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014839        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system