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Database: PDB
Entry: 4WBB
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Original site: 4WBB 
HEADER    TRANSFERASE                             02-SEP-14   4WBB              
TITLE     SINGLE TURNOVER AUTOPHOSPHORYLATION CYCLE OF THE PKA RIIB HOLOENZYME  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE TYPE II-BETA REGULATORY      
COMPND   3 SUBUNIT;                                                             
COMPND   4 CHAIN: A;                                                            
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;     
COMPND   8 CHAIN: B;                                                            
COMPND   9 SYNONYM: PKA C-ALPHA;                                                
COMPND  10 EC: 2.7.11.11;                                                       
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: PRKAR2B;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  10 ORGANISM_COMMON: MOUSE;                                              
SOURCE  11 ORGANISM_TAXID: 10090;                                               
SOURCE  12 GENE: PRKACA, PKACA;                                                 
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PKA, COMPLEX, SINGLE TURNOVER, OSCILLATIONS, TRANSFERASE              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.ZHANG,M.J.KNAPE,L.G.AHUJA,M.M.KESHWANI,C.C.KING,M.SASTRI,           
AUTHOR   2 F.W.HERBERG,S.S.TAYLOR                                               
REVDAT   5   25-DEC-19 4WBB    1       REMARK                                   
REVDAT   4   20-SEP-17 4WBB    1       REMARK                                   
REVDAT   3   26-AUG-15 4WBB    1       REMARK                                   
REVDAT   2   22-JUL-15 4WBB    1       JRNL                                     
REVDAT   1   20-MAY-15 4WBB    0                                                
JRNL        AUTH   P.ZHANG,M.J.KNAPE,L.G.AHUJA,M.M.KESHWANI,C.C.KING,M.SASTRI,  
JRNL        AUTH 2 F.W.HERBERG,S.S.TAYLOR                                       
JRNL        TITL   SINGLE TURNOVER AUTOPHOSPHORYLATION CYCLE OF THE PKA RII     
JRNL        TITL 2 BETA HOLOENZYME.                                             
JRNL        REF    PLOS BIOL.                    V.  13 02192 2015              
JRNL        REFN                   ESSN 1545-7885                               
JRNL        PMID   26158466                                                     
JRNL        DOI    10.1371/JOURNAL.PBIO.1002192                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : NULL                                                 
REMARK   3   AUTHORS     : NULL                                                 
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 23056                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE R-VALUE                    
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.232                           
REMARK   3   FREE R VALUE                     : 0.279                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4915                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 42                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4WBB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-SEP-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000203515.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-SEP-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 1                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23056                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.7                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: THE RIIB (R230K):C APO COMPLEX WAS       
REMARK 280  CRYSTALLIZED IN 20%PEG8000, 8% ETHYLENE GLYCOL, 20MM MESPH7.5       
REMARK 280  HEPES . TO MAKE CAATP BINDING HOLOENZYME CRYSTALS, THE APO          
REMARK 280  HOLOENZYME CRYSTALS WERE SOAKED WITH 20%PEG8000, 8% ETHYLENE        
REMARK 280  GLYCOL, 20MM MESPH7.5 HEPES, 5MM CACL2 AND 1MM ATP AT PH5.8         
REMARK 280  SOLUTION OVERNIGHT, BATCH MODE, TEMPERATURE 298K                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z                                         
REMARK 290       7555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       75.19000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      106.97550            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       75.19000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      106.97550            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       75.19000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      106.97550            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       75.19000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      106.97550            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4930 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ILE A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     ILE A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     THR A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     LEU A    12                                                      
REMARK 465     LEU A    13                                                      
REMARK 465     GLN A    14                                                      
REMARK 465     GLY A    15                                                      
REMARK 465     PHE A    16                                                      
REMARK 465     THR A    17                                                      
REMARK 465     VAL A    18                                                      
REMARK 465     GLU A    19                                                      
REMARK 465     VAL A    20                                                      
REMARK 465     LEU A    21                                                      
REMARK 465     ARG A    22                                                      
REMARK 465     HIS A    23                                                      
REMARK 465     GLN A    24                                                      
REMARK 465     PRO A    25                                                      
REMARK 465     ALA A    26                                                      
REMARK 465     ASP A    27                                                      
REMARK 465     LEU A    28                                                      
REMARK 465     LEU A    29                                                      
REMARK 465     GLU A    30                                                      
REMARK 465     PHE A    31                                                      
REMARK 465     ALA A    32                                                      
REMARK 465     LEU A    33                                                      
REMARK 465     GLN A    34                                                      
REMARK 465     HIS A    35                                                      
REMARK 465     PHE A    36                                                      
REMARK 465     THR A    37                                                      
REMARK 465     ARG A    38                                                      
REMARK 465     LEU A    39                                                      
REMARK 465     GLN A    40                                                      
REMARK 465     GLN A    41                                                      
REMARK 465     GLU A    42                                                      
REMARK 465     ASN A    43                                                      
REMARK 465     GLU A    44                                                      
REMARK 465     ARG A    45                                                      
REMARK 465     LYS A    46                                                      
REMARK 465     GLY A    47                                                      
REMARK 465     ALA A    48                                                      
REMARK 465     ALA A    49                                                      
REMARK 465     ARG A    50                                                      
REMARK 465     PHE A    51                                                      
REMARK 465     GLY A    52                                                      
REMARK 465     HIS A    53                                                      
REMARK 465     GLU A    54                                                      
REMARK 465     GLY A    55                                                      
REMARK 465     ARG A    56                                                      
REMARK 465     THR A    57                                                      
REMARK 465     TRP A    58                                                      
REMARK 465     GLY A    59                                                      
REMARK 465     ASP A    60                                                      
REMARK 465     ALA A    61                                                      
REMARK 465     GLY A    62                                                      
REMARK 465     ALA A    63                                                      
REMARK 465     ALA A    64                                                      
REMARK 465     ALA A    65                                                      
REMARK 465     GLY A    66                                                      
REMARK 465     GLY A    67                                                      
REMARK 465     GLY A    68                                                      
REMARK 465     ILE A    69                                                      
REMARK 465     PRO A    70                                                      
REMARK 465     SER A    71                                                      
REMARK 465     LYS A    72                                                      
REMARK 465     GLY A    73                                                      
REMARK 465     VAL A    74                                                      
REMARK 465     ASN A    75                                                      
REMARK 465     PHE A    76                                                      
REMARK 465     ALA A    77                                                      
REMARK 465     GLU A    78                                                      
REMARK 465     GLU A    79                                                      
REMARK 465     PRO A    80                                                      
REMARK 465     MET A    81                                                      
REMARK 465     ARG A    82                                                      
REMARK 465     SER A    83                                                      
REMARK 465     ASP A    84                                                      
REMARK 465     SER A    85                                                      
REMARK 465     GLU A    86                                                      
REMARK 465     ASN A    87                                                      
REMARK 465     GLY A    88                                                      
REMARK 465     GLU A    89                                                      
REMARK 465     GLU A    90                                                      
REMARK 465     GLU A    91                                                      
REMARK 465     GLU A    92                                                      
REMARK 465     ALA A    93                                                      
REMARK 465     ALA A    94                                                      
REMARK 465     GLU A    95                                                      
REMARK 465     ALA A    96                                                      
REMARK 465     GLY A    97                                                      
REMARK 465     ALA A    98                                                      
REMARK 465     PHE A    99                                                      
REMARK 465     ASN A   100                                                      
REMARK 465     ALA A   101                                                      
REMARK 465     PRO A   102                                                      
REMARK 465     VAL A   103                                                      
REMARK 465     GLU A   122                                                      
REMARK 465     GLU A   123                                                      
REMARK 465     GLU A   124                                                      
REMARK 465     ASP A   125                                                      
REMARK 465     ASP A   126                                                      
REMARK 465     ALA A   127                                                      
REMARK 465     GLU A   128                                                      
REMARK 465     SER A   129                                                      
REMARK 465     ARG A   325                                                      
REMARK 465     LYS A   326                                                      
REMARK 465     GLY A   327                                                      
REMARK 465     LYS A   328                                                      
REMARK 465     SER A   329                                                      
REMARK 465     GLU A   330                                                      
REMARK 465     VAL A   331                                                      
REMARK 465     GLU A   332                                                      
REMARK 465     GLU A   333                                                      
REMARK 465     ASN A   334                                                      
REMARK 465     GLY A   335                                                      
REMARK 465     ALA A   336                                                      
REMARK 465     ASN A   393                                                      
REMARK 465     ILE A   394                                                      
REMARK 465     ALA A   395                                                      
REMARK 465     THR A   396                                                      
REMARK 465     TYR A   397                                                      
REMARK 465     GLU A   398                                                      
REMARK 465     GLU A   399                                                      
REMARK 465     GLN A   400                                                      
REMARK 465     LEU A   401                                                      
REMARK 465     VAL A   402                                                      
REMARK 465     ALA A   403                                                      
REMARK 465     LEU A   404                                                      
REMARK 465     PHE A   405                                                      
REMARK 465     GLY A   406                                                      
REMARK 465     THR A   407                                                      
REMARK 465     ASN A   408                                                      
REMARK 465     MET A   409                                                      
REMARK 465     ASP A   410                                                      
REMARK 465     ILE A   411                                                      
REMARK 465     VAL A   412                                                      
REMARK 465     GLU A   413                                                      
REMARK 465     PRO A   414                                                      
REMARK 465     THR A   415                                                      
REMARK 465     ALA A   416                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     ASN B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     LYS B     7                                                      
REMARK 465     LYS B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     SER B    10                                                      
REMARK 465     GLU B    11                                                      
REMARK 465     GLN B    12                                                      
REMARK 465     GLU B    13                                                      
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     ILE A 104    N                                                   
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   N    ASN A   257     O    HOH A   618              1.76            
REMARK 500   O    ASP B    25     O    HOH B   517              1.91            
REMARK 500   O    CYS A   209     O    HOH A   601              1.92            
REMARK 500   O    VAL A   337     O    HOH A   602              1.95            
REMARK 500   N    LYS B    29     O    HOH B   517              1.97            
REMARK 500   O    ASP A   185     O    HOH A   609              1.97            
REMARK 500   O    ILE A   254     O    HOH A   618              2.01            
REMARK 500   CG1  VAL A   337     O    HOH A   602              2.01            
REMARK 500   O    GLY A   367     O    HOH A   623              2.01            
REMARK 500   O    ASP A   184     O    HOH A   611              2.02            
REMARK 500   O    PHE A   107     O    HOH A   603              2.06            
REMARK 500   O    HOH A   608     O    HOH A   612              2.06            
REMARK 500   OG1  THR A   196     OG1  THR A   237              2.06            
REMARK 500   OD2  ASP A   297     O    HOH A   621              2.08            
REMARK 500   O    TYR A   295     O    HOH A   623              2.08            
REMARK 500   OD1  ASP A   138     O    HOH A   604              2.10            
REMARK 500   N    THR B   299     O    HOH B   518              2.10            
REMARK 500   CB   PRO B    33     NE2  GLN B    96              2.12            
REMARK 500   O3P  SEP A   112     O    HOH A   607              2.13            
REMARK 500   O    THR A   108     O    HOH A   613              2.14            
REMARK 500   N    PHE A   197     O    HOH A   624              2.14            
REMARK 500   CA   THR A   368     O    HOH A   623              2.15            
REMARK 500   C    ILE A   254     O    HOH A   618              2.15            
REMARK 500   O    GLU A   266     N    ILE A   269              2.16            
REMARK 500   O    MET A   264     O    HOH A   612              2.16            
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    PRO A 229   C   -  N   -  CA  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    PRO A 358   C   -  N   -  CA  ANGL. DEV. =  12.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 105       24.19    -78.09                                   
REMARK 500    ASN A 155       65.07   -109.53                                   
REMARK 500    ASP A 193      -65.14    -94.51                                   
REMARK 500    ASP A 204     -101.99   -123.69                                   
REMARK 500    VAL A 210     -144.43   -104.75                                   
REMARK 500    ASN A 215        4.51     58.11                                   
REMARK 500    SER A 238      175.67    174.70                                   
REMARK 500    ARG A 262     -100.55    -97.66                                   
REMARK 500    SER A 310      159.38    179.72                                   
REMARK 500    ALA A 340      155.32    175.48                                   
REMARK 500    PHE A 343     -167.02   -108.51                                   
REMARK 500    GLU A 350        3.18    -61.40                                   
REMARK 500    PRO A 358      133.43    -31.07                                   
REMARK 500    MET A 390       14.26    -68.17                                   
REMARK 500    LYS A 391     -108.11    -92.91                                   
REMARK 500    LEU B  19      -73.96    -42.12                                   
REMARK 500    ALA B  20      -38.47    -39.84                                   
REMARK 500    GLN B  35     -133.62   -119.74                                   
REMARK 500    ASN B  36       74.83    -66.04                                   
REMARK 500    THR B  37      -70.51    -53.49                                   
REMARK 500    ALA B  38     -141.01   -108.84                                   
REMARK 500    ARG B  56      109.22    160.79                                   
REMARK 500    ASP B  75      104.86    -59.38                                   
REMARK 500    ILE B  85      -70.86    -42.05                                   
REMARK 500    PHE B 100      137.01   -171.19                                   
REMARK 500    PHE B 110     -179.75   -173.29                                   
REMARK 500    ARG B 165       10.07     55.43                                   
REMARK 500    ASP B 166       47.32   -140.95                                   
REMARK 500    THR B 183      -40.66   -133.99                                   
REMARK 500    ASN B 216     -117.62   -131.01                                   
REMARK 500    ASP B 241      -72.70    -57.74                                   
REMARK 500    LEU B 273       47.52    -81.87                                   
REMARK 500    ASN B 293       34.64    -90.89                                   
REMARK 500    HIS B 294     -166.36    -70.66                                   
REMARK 500    PRO B 313       13.52    -69.24                                   
REMARK 500    PHE B 314      123.26   -179.09                                   
REMARK 500    LYS B 319     -120.72   -117.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SEP A 112   O3P                                                    
REMARK 620 2 ASP B 184   OD1  82.3                                              
REMARK 620 3 ASP B 184   OD2 130.5  50.4                                        
REMARK 620 4 ADP A 502   O2B  85.3  62.1  84.2                                  
REMARK 620 5 HOH B 505   O    85.5  71.3  68.1 133.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 401  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B 171   OD1                                                    
REMARK 620 2 ASP B 184   OD1  89.4                                              
REMARK 620 3 ADP A 502   O2B 137.6  55.1                                        
REMARK 620 4 ADP A 502   O3B 143.2 104.8  50.5                                  
REMARK 620 5 ADP A 502   O2A  85.1  76.3  66.0  66.4                            
REMARK 620 6 HOH B 504   O    62.7 148.5 139.1  91.6  86.4                      
REMARK 620 7 HOH A 607   O    97.4  80.8  98.4 118.0 156.9 115.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 401                  
DBREF  4WBB A    1   416  UNP    P31324   KAP3_MOUSE       1    416             
DBREF  4WBB B    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
SEQADV 4WBB LYS A  230  UNP  P31324    ARG   230 ENGINEERED MUTATION            
SEQRES   1 A  416  MET SER ILE GLU ILE PRO ALA GLY LEU THR GLU LEU LEU          
SEQRES   2 A  416  GLN GLY PHE THR VAL GLU VAL LEU ARG HIS GLN PRO ALA          
SEQRES   3 A  416  ASP LEU LEU GLU PHE ALA LEU GLN HIS PHE THR ARG LEU          
SEQRES   4 A  416  GLN GLN GLU ASN GLU ARG LYS GLY ALA ALA ARG PHE GLY          
SEQRES   5 A  416  HIS GLU GLY ARG THR TRP GLY ASP ALA GLY ALA ALA ALA          
SEQRES   6 A  416  GLY GLY GLY ILE PRO SER LYS GLY VAL ASN PHE ALA GLU          
SEQRES   7 A  416  GLU PRO MET ARG SER ASP SER GLU ASN GLY GLU GLU GLU          
SEQRES   8 A  416  GLU ALA ALA GLU ALA GLY ALA PHE ASN ALA PRO VAL ILE          
SEQRES   9 A  416  ASN ARG PHE THR ARG ARG ALA SEP VAL CYS ALA GLU ALA          
SEQRES  10 A  416  TYR ASN PRO ASP GLU GLU GLU ASP ASP ALA GLU SER ARG          
SEQRES  11 A  416  ILE ILE HIS PRO LYS THR ASP ASP GLN ARG ASN ARG LEU          
SEQRES  12 A  416  GLN GLU ALA CYS LYS ASP ILE LEU LEU PHE LYS ASN LEU          
SEQRES  13 A  416  ASP PRO GLU GLN MET SER GLN VAL LEU ASP ALA MET PHE          
SEQRES  14 A  416  GLU LYS LEU VAL LYS GLU GLY GLU HIS VAL ILE ASP GLN          
SEQRES  15 A  416  GLY ASP ASP GLY ASP ASN PHE TYR VAL ILE ASP ARG GLY          
SEQRES  16 A  416  THR PHE ASP ILE TYR VAL LYS CYS ASP GLY VAL GLY ARG          
SEQRES  17 A  416  CYS VAL GLY ASN TYR ASP ASN ARG GLY SER PHE GLY GLU          
SEQRES  18 A  416  LEU ALA LEU MET TYR ASN THR PRO LYS ALA ALA THR ILE          
SEQRES  19 A  416  THR ALA THR SER PRO GLY ALA LEU TRP GLY LEU ASP ARG          
SEQRES  20 A  416  VAL THR PHE ARG ARG ILE ILE VAL LYS ASN ASN ALA LYS          
SEQRES  21 A  416  LYS ARG LYS MET TYR GLU SER PHE ILE GLU SER LEU PRO          
SEQRES  22 A  416  PHE LEU LYS SER LEU GLU VAL SER GLU ARG LEU LYS VAL          
SEQRES  23 A  416  VAL ASP VAL ILE GLY THR LYS VAL TYR ASN ASP GLY GLU          
SEQRES  24 A  416  GLN ILE ILE ALA GLN GLY ASP LEU ALA ASP SER PHE PHE          
SEQRES  25 A  416  ILE VAL GLU SER GLY GLU VAL LYS ILE THR MET LYS ARG          
SEQRES  26 A  416  LYS GLY LYS SER GLU VAL GLU GLU ASN GLY ALA VAL GLU          
SEQRES  27 A  416  ILE ALA ARG CYS PHE ARG GLY GLN TYR PHE GLY GLU LEU          
SEQRES  28 A  416  ALA LEU VAL THR ASN LYS PRO ARG ALA ALA SER ALA HIS          
SEQRES  29 A  416  ALA ILE GLY THR VAL LYS CYS LEU ALA MET ASP VAL GLN          
SEQRES  30 A  416  ALA PHE GLU ARG LEU LEU GLY PRO CYS MET GLU ILE MET          
SEQRES  31 A  416  LYS ARG ASN ILE ALA THR TYR GLU GLU GLN LEU VAL ALA          
SEQRES  32 A  416  LEU PHE GLY THR ASN MET ASP ILE VAL GLU PRO THR ALA          
SEQRES   1 B  350  GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN GLU          
SEQRES   2 B  350  SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE          
SEQRES   3 B  350  LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN          
SEQRES   4 B  350  LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY          
SEQRES   5 B  350  SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER          
SEQRES   6 B  350  GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS          
SEQRES   7 B  350  VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU          
SEQRES   8 B  350  LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL          
SEQRES   9 B  350  LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR          
SEQRES  10 B  350  MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER          
SEQRES  11 B  350  HIS LEU ARG ARG ILE GLY ARG PHE SEP GLU PRO HIS ALA          
SEQRES  12 B  350  ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR          
SEQRES  13 B  350  LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO          
SEQRES  14 B  350  GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL          
SEQRES  15 B  350  THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR          
SEQRES  16 B  350  TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU          
SEQRES  17 B  350  ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP          
SEQRES  18 B  350  TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY          
SEQRES  19 B  350  TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR          
SEQRES  20 B  350  GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS          
SEQRES  21 B  350  PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU          
SEQRES  22 B  350  GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN          
SEQRES  23 B  350  GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR          
SEQRES  24 B  350  THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA          
SEQRES  25 B  350  PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER          
SEQRES  26 B  350  ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP          
SEQRES  27 B  350  ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE              
MODRES 4WBB SEP A  112  SER  MODIFIED RESIDUE                                   
MODRES 4WBB SEP B  139  SER  MODIFIED RESIDUE                                   
MODRES 4WBB TPO B  197  THR  MODIFIED RESIDUE                                   
MODRES 4WBB SEP B  338  SER  MODIFIED RESIDUE                                   
HET    SEP  A 112      10                                                       
HET    SEP  B 139      10                                                       
HET    TPO  B 197      11                                                       
HET    SEP  B 338      10                                                       
HET     CA  A 501       1                                                       
HET    ADP  A 502      27                                                       
HET     CA  B 401       1                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM      CA CALCIUM ION                                                      
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  SEP    3(C3 H8 N O6 P)                                              
FORMUL   2  TPO    C4 H10 N O6 P                                                
FORMUL   3   CA    2(CA 2+)                                                     
FORMUL   4  ADP    C10 H15 N5 O10 P2                                            
FORMUL   6  HOH   *42(H2 O)                                                     
HELIX    1 AA1 ILE A  104  THR A  108  5                                   5    
HELIX    2 AA2 THR A  136  ALA A  146  1                                  11    
HELIX    3 AA3 ILE A  150  ASN A  155  1                                   6    
HELIX    4 AA4 ASP A  157  MET A  168  1                                  12    
HELIX    5 AA5 GLY A  220  MET A  225  5                                   6    
HELIX    6 AA6 ARG A  247  LYS A  261  1                                  15    
HELIX    7 AA7 TYR A  265  SER A  271  1                                   7    
HELIX    8 AA8 LEU A  272  LYS A  276  5                                   5    
HELIX    9 AA9 GLU A  279  ILE A  290  1                                  12    
HELIX   10 AB1 GLY A  349  VAL A  354  5                                   6    
HELIX   11 AB2 VAL A  376  GLY A  384  1                                   9    
HELIX   12 AB3 PRO A  385  MET A  390  1                                   6    
HELIX   13 AB4 LYS B   16  THR B   32  1                                  17    
HELIX   14 AB5 GLN B   39  ASP B   41  5                                   3    
HELIX   15 AB6 LYS B   76  LEU B   82  1                                   7    
HELIX   16 AB7 GLN B   84  GLN B   96  1                                  13    
HELIX   17 AB8 GLU B  127  GLY B  136  1                                  10    
HELIX   18 AB9 SEP B  139  LEU B  160  1                                  22    
HELIX   19 AC1 THR B  201  LEU B  205  5                                   5    
HELIX   20 AC2 ALA B  206  LEU B  211  1                                   6    
HELIX   21 AC3 LYS B  217  GLY B  234  1                                  18    
HELIX   22 AC4 GLN B  242  GLY B  253  1                                  12    
HELIX   23 AC5 SER B  262  LEU B  273  1                                  12    
HELIX   24 AC6 ASP B  276  ARG B  280  5                                   5    
HELIX   25 AC7 VAL B  288  ASN B  293  1                                   6    
HELIX   26 AC8 ASP B  301  GLN B  307  1                                   7    
HELIX   27 AC9 GLY B  344  THR B  348  5                                   5    
SHEET    1 AA1 2 VAL A 113  CYS A 114  0                                        
SHEET    2 AA1 2 CYS B 199  GLY B 200 -1  O  GLY B 200   N  VAL A 113           
SHEET    1 AA2 4 PHE A 169  VAL A 173  0                                        
SHEET    2 AA2 4 GLY A 240  ASP A 246 -1  O  GLY A 240   N  VAL A 173           
SHEET    3 AA2 4 ASN A 188  ARG A 194 -1  N  PHE A 189   O  LEU A 245           
SHEET    4 AA2 4 SER A 218  PHE A 219 -1  O  PHE A 219   N  TYR A 190           
SHEET    1 AA3 4 HIS A 178  ILE A 180  0                                        
SHEET    2 AA3 4 THR A 233  ALA A 236 -1  O  ILE A 234   N  VAL A 179           
SHEET    3 AA3 4 THR A 196  TYR A 200 -1  N  TYR A 200   O  THR A 233           
SHEET    4 AA3 4 ASN A 212  ASP A 214 -1  O  TYR A 213   N  PHE A 197           
SHEET    1 AA4 4 GLY A 291  TYR A 295  0                                        
SHEET    2 AA4 4 SER A 362  ASP A 375 -1  O  CYS A 371   N  LYS A 293           
SHEET    3 AA4 4 SER A 310  THR A 322 -1  N  ILE A 313   O  LEU A 372           
SHEET    4 AA4 4 GLU A 338  CYS A 342 -1  O  ILE A 339   N  ILE A 321           
SHEET    1 AA5 4 GLN A 300  ILE A 302  0                                        
SHEET    2 AA5 4 SER A 362  ASP A 375 -1  O  ALA A 363   N  ILE A 302           
SHEET    3 AA5 4 SER A 310  THR A 322 -1  N  ILE A 313   O  LEU A 372           
SHEET    4 AA5 4 TYR A 347  PHE A 348 -1  O  PHE A 348   N  PHE A 312           
SHEET    1 AA6 5 PHE B  43  GLY B  50  0                                        
SHEET    2 AA6 5 VAL B  57  HIS B  62 -1  O  VAL B  57   N  LEU B  49           
SHEET    3 AA6 5 HIS B  68  ASP B  75 -1  O  MET B  71   N  MET B  58           
SHEET    4 AA6 5 ASN B 115  GLU B 121 -1  O  MET B 118   N  LYS B  72           
SHEET    5 AA6 5 LEU B 106  LYS B 111 -1  N  PHE B 110   O  TYR B 117           
SHEET    1 AA7 2 LEU B 162  ILE B 163  0                                        
SHEET    2 AA7 2 LYS B 189  ARG B 190 -1  O  LYS B 189   N  ILE B 163           
SHEET    1 AA8 2 LEU B 172  ILE B 174  0                                        
SHEET    2 AA8 2 ILE B 180  VAL B 182 -1  O  GLN B 181   N  LEU B 173           
LINK         C   ALA A 111                 N   SEP A 112     1555   1555  1.33  
LINK         C   SEP A 112                 N   VAL A 113     1555   1555  1.32  
LINK         O3P SEP A 112                CA    CA A 501     1555   1555  2.41  
LINK         C   PHE B 138                 N   SEP B 139     1555   1555  1.33  
LINK         C   SEP B 139                 N   GLU B 140     1555   1555  1.32  
LINK         OD1 ASN B 171                CA    CA B 401     1555   1555  2.56  
LINK         OD1 ASP B 184                CA    CA A 501     1555   1555  2.41  
LINK         OD1 ASP B 184                CA    CA B 401     1555   1555  2.30  
LINK         OD2 ASP B 184                CA    CA A 501     1555   1555  2.69  
LINK         C   TRP B 196                 N   TPO B 197     1555   1555  1.33  
LINK         C   TPO B 197                 N   LEU B 198     1555   1555  1.32  
LINK         C   VAL B 337                 N   SEP B 338     1555   1555  1.33  
LINK         C   SEP B 338                 N   ILE B 339     1555   1555  1.33  
LINK        CA    CA A 501                 O2B ADP A 502     1555   1555  2.10  
LINK        CA    CA A 501                 O   HOH B 505     1555   1555  2.51  
LINK         O2B ADP A 502                CA    CA B 401     1555   1555  2.70  
LINK         O3B ADP A 502                CA    CA B 401     1555   1555  3.16  
LINK         O2A ADP A 502                CA    CA B 401     1555   1555  2.11  
LINK        CA    CA B 401                 O   HOH B 504     1555   1555  2.70  
LINK        CA    CA B 401                 O   HOH A 607     1555   1555  2.09  
CISPEP   1 ASP A  204    GLY A  205          0         6.13                     
CISPEP   2 LYS A  263    MET A  264          0        14.33                     
CISPEP   3 SER B   53    PHE B   54          0         2.96                     
CISPEP   4 PHE B   54    GLY B   55          0         1.36                     
SITE     1 AC1  4 SEP A 112  ADP A 502  ASP B 184  HOH B 505                    
SITE     1 AC2 16 SEP A 112   CA A 501  GLY B  52  SER B  53                    
SITE     2 AC2 16 VAL B  57  ALA B  70  LYS B  72  GLU B 121                    
SITE     3 AC2 16 VAL B 123  GLU B 127  ASN B 171  LEU B 173                    
SITE     4 AC2 16 THR B 183  ASP B 184  PHE B 327   CA B 401                    
SITE     1 AC3  6 SEP A 112  ADP A 502  HOH A 607  ASN B 171                    
SITE     2 AC3  6 ASP B 184  HOH B 504                                          
CRYST1  150.380  213.951   61.967  90.00  90.00  90.00 C 2 2 2       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006650  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004674  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016138        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system