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Database: PDB
Entry: 1YHW
LinkDB: 1YHW
Original site: 1YHW 
HEADER    SIGNALING PROTEIN, TRANSFERASE          10-JAN-05   1YHW              
TITLE     CRYSTAL STRUCTURE OF PAK1 KINASE DOMAIN WITH ONE POINT                
TITLE    2 MUTATIONS (K299R)                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PAK 1;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: KINASE DOMAIN;                                             
COMPND   5 SYNONYM: P21-ACTIVATED KINASE 1; PAK-1; P65-PAK; ALPHA-PAK;          
COMPND   6 EC: 2.7.1.37;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PAK1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: NB42;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PASMID;                               
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX2T                                    
KEYWDS    KINASE; ACTIVE CONFORMATION; ACTIVATION LOOP; ATP BINDING             
KEYWDS   2 SITE, SIGNALING PROTEIN, TRANSFERASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.LEI,M.A.ROBINSON,S.C.HARRISON                                       
REVDAT   2   24-FEB-09 1YHW    1       VERSN                                    
REVDAT   1   24-MAY-05 1YHW    0                                                
JRNL        AUTH   M.LEI,M.A.ROBINSON,S.C.HARRISON                              
JRNL        TITL   THE ACTIVE CONFORMATION OF THE PAK1 KINASE DOMAIN            
JRNL        REF    STRUCTURE                     V.  13   769 2005              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   15893667                                                     
JRNL        DOI    10.1016/J.STR.2005.03.007                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000.000                       
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 28465                          
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 SET) : 0.226                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1383                            
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            : 2268                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 349                                     
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) : -11.54000                                            
REMARK   3    B22 (A**2) : 6.79700                                              
REMARK   3    B33 (A**2) : 4.74300                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED 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) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
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) : 1.301 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.049 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.029 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.995 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 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 1YHW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JAN-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB031530.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 113                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 14-BM-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28485                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.4                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : 0.34400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.9000                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, NACL, PIPES, PH 6.5,           
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
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+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
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       61.31950            
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       61.31950            
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       25.88150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       51.52450            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       25.88150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       51.52450            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       61.31950            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       25.88150            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       51.52450            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       61.31950            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       25.88150            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       51.52450            
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     LYS A   542                                                      
REMARK 465     ASN A   543                                                      
REMARK 465     ASN A   544                                                      
REMARK 465     HIS A   545                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP A 250    CG   OD1  OD2                                       
REMARK 470     ARG A 272    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 278    CG   CD   OE1  NE2                                  
REMARK 470     SER A 281    OG                                                  
REMARK 470     ARG A 438    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 439    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A 271      -94.68   -119.47                                   
REMARK 500    ARG A 272       64.86    -56.48                                   
REMARK 500    ILE A 276     -105.17   -105.45                                   
REMARK 500    GLN A 278       41.38   -158.04                                   
REMARK 500    GLN A 304      -15.39    -47.68                                   
REMARK 500    LYS A 308       77.97   -100.47                                   
REMARK 500    ARG A 388       -0.61     71.12                                   
REMARK 500    ASP A 389       47.83   -143.80                                   
REMARK 500    ASP A 407       87.44     63.68                                   
REMARK 500    GLU A 417      -78.71    -51.35                                   
REMARK 500    GLN A 418       58.18    -92.18                                   
REMARK 500    ARG A 438      174.34     63.27                                   
REMARK 500    LYS A 439     -163.97   -117.85                                   
REMARK 500    ALA A 440       99.60     42.47                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1YHV   RELATED DB: PDB                                   
REMARK 900 PAK1 KINASE DOMAIN WITH TWO POINT MUTATIONS (K299R, T432E)           
DBREF  1YHW A  249   545  UNP    Q13153   PAK1_HUMAN     249    545             
SEQADV 1YHW ARG A  299  UNP  Q13153    LYS   299 ENGINEERED                     
SEQRES   1 A  297  SER ASP GLU GLU ILE LEU GLU LYS LEU ARG SER ILE VAL          
SEQRES   2 A  297  SER VAL GLY ASP PRO LYS LYS LYS TYR THR ARG PHE GLU          
SEQRES   3 A  297  LYS ILE GLY GLN GLY ALA SER GLY THR VAL TYR THR ALA          
SEQRES   4 A  297  MET ASP VAL ALA THR GLY GLN GLU VAL ALA ILE ARG GLN          
SEQRES   5 A  297  MET ASN LEU GLN GLN GLN PRO LYS LYS GLU LEU ILE ILE          
SEQRES   6 A  297  ASN GLU ILE LEU VAL MET ARG GLU ASN LYS ASN PRO ASN          
SEQRES   7 A  297  ILE VAL ASN TYR LEU ASP SER TYR LEU VAL GLY ASP GLU          
SEQRES   8 A  297  LEU TRP VAL VAL MET GLU TYR LEU ALA GLY GLY SER LEU          
SEQRES   9 A  297  THR ASP VAL VAL THR GLU THR CYS MET ASP GLU GLY GLN          
SEQRES  10 A  297  ILE ALA ALA VAL CYS ARG GLU CYS LEU GLN ALA LEU GLU          
SEQRES  11 A  297  PHE LEU HIS SER ASN GLN VAL ILE HIS ARG ASP ILE LYS          
SEQRES  12 A  297  SER ASP ASN ILE LEU LEU GLY MET ASP GLY SER VAL LYS          
SEQRES  13 A  297  LEU THR ASP PHE GLY PHE CYS ALA GLN ILE THR PRO GLU          
SEQRES  14 A  297  GLN SER LYS ARG SER THR MET VAL GLY THR PRO TYR TRP          
SEQRES  15 A  297  MET ALA PRO GLU VAL VAL THR ARG LYS ALA TYR GLY PRO          
SEQRES  16 A  297  LYS VAL ASP ILE TRP SER LEU GLY ILE MET ALA ILE GLU          
SEQRES  17 A  297  MET ILE GLU GLY GLU PRO PRO TYR LEU ASN GLU ASN PRO          
SEQRES  18 A  297  LEU ARG ALA LEU TYR LEU ILE ALA THR ASN GLY THR PRO          
SEQRES  19 A  297  GLU LEU GLN ASN PRO GLU LYS LEU SER ALA ILE PHE ARG          
SEQRES  20 A  297  ASP PHE LEU ASN ARG CYS LEU ASP MET ASP VAL GLU LYS          
SEQRES  21 A  297  ARG GLY SER ALA LYS GLU LEU LEU GLN HIS GLN PHE LEU          
SEQRES  22 A  297  LYS ILE ALA LYS PRO LEU SER SER LEU THR PRO LEU ILE          
SEQRES  23 A  297  ALA ALA ALA LYS GLU ALA THR LYS ASN ASN HIS                  
FORMUL   2  HOH   *349(H2 O)                                                    
HELIX    1   1 SER A  249  VAL A  261  1                                  13    
HELIX    2   2 GLN A  304  GLN A  306  5                                   3    
HELIX    3   3 LYS A  308  ASN A  322  1                                  15    
HELIX    4   4 SER A  351  THR A  359  1                                   9    
HELIX    5   5 ASP A  362  ASN A  383  1                                  22    
HELIX    6   6 LYS A  391  ASP A  393  5                                   3    
HELIX    7   7 THR A  427  MET A  431  5                                   5    
HELIX    8   8 ALA A  432  THR A  437  1                                   6    
HELIX    9   9 PRO A  443  GLY A  460  1                                  18    
HELIX   10  10 ASN A  468  GLY A  480  1                                  13    
HELIX   11  11 ASN A  486  LEU A  490  5                                   5    
HELIX   12  12 SER A  491  LEU A  502  1                                  12    
HELIX   13  13 SER A  511  LEU A  516  1                                   6    
HELIX   14  14 GLN A  517  ALA A  524  5                                   8    
HELIX   15  15 PRO A  526  SER A  529  5                                   4    
HELIX   16  16 LEU A  530  ALA A  540  1                                  11    
SHEET    1   A 5 GLU A 274  LYS A 275  0                                        
SHEET    2   A 5 THR A 283  MET A 288 -1  O  THR A 286   N  GLU A 274           
SHEET    3   A 5 GLU A 295  ASN A 302 -1  O  ILE A 298   N  TYR A 285           
SHEET    4   A 5 GLU A 339  GLU A 345 -1  O  LEU A 340   N  MET A 301           
SHEET    5   A 5 TYR A 330  VAL A 336 -1  N  VAL A 336   O  GLU A 339           
SHEET    1   B 2 VAL A 385  ILE A 386  0                                        
SHEET    2   B 2 ALA A 412  GLN A 413 -1  O  ALA A 412   N  ILE A 386           
SHEET    1   C 2 ILE A 395  LEU A 397  0                                        
SHEET    2   C 2 VAL A 403  LEU A 405 -1  O  LYS A 404   N  LEU A 396           
CRYST1   51.763  103.049  122.639  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019319  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009704  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008154        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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