GenomeNet

Database: PDB
Entry: 1F3M
LinkDB: 1F3M
Original site: 1F3M 
HEADER    TRANSFERASE                             05-JUN-00   1F3M              
TITLE     CRYSTAL STRUCTURE OF HUMAN SERINE/THREONINE KINASE PAK1               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PAK-ALPHA;                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: PAK1 AUTOREGULATORY DOMAIN (70-149);                       
COMPND   5 EC: 2.7.1.-;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PAK-ALPHA;                 
COMPND   9 CHAIN: C, D;                                                         
COMPND  10 FRAGMENT: KINASE DOMAIN (249-545);                                   
COMPND  11 EC: 2.7.1.-;                                                         
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PGEX2N;                                   
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PGEX2N                                    
KEYWDS    KINASE DOMAIN, AUTOINHIBITORY FRAGMENT, HOMODIMER,                    
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.LEI,W.LU,W.MENG,M-C.PARRINI,M.J.ECK,B.J.MAYER,S.C.HARRISON          
REVDAT   4   24-FEB-09 1F3M    1       VERSN                                    
REVDAT   3   01-APR-03 1F3M    1       JRNL                                     
REVDAT   2   29-NOV-00 1F3M    1       JRNL                                     
REVDAT   1   29-JUN-00 1F3M    0                                                
JRNL        AUTH   M.LEI,W.LU,W.MENG,M.C.PARRINI,M.J.ECK,B.J.MAYER,             
JRNL        AUTH 2 S.C.HARRISON                                                 
JRNL        TITL   STRUCTURE OF PAK1 IN AN AUTOINHIBITED CONFORMATION           
JRNL        TITL 2 REVEALS A MULTISTAGE ACTIVATION SWITCH.                      
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 102   387 2000              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   10975528                                                     
JRNL        DOI    10.1016/S0092-8674(00)00043-X                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.9                                              
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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.08                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 56156                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.237                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2848                            
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            : 5577                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 582                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.60                          
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) : 0.006                           
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  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 1F3M COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUN-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB011201.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-AUG-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 113.0                              
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) : 1.0                                
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   : 56156                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.080                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.06900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34900                            
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: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PH 6.5, VAPOR          
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 285K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41                             
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   -Y,X,Z+1/4                                              
REMARK 290       4555   Y,-X,Z+3/4                                              
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       73.74850            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       36.87425            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      110.62275            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11470 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 33850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D                            
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    70                                                      
REMARK 465     GLU A    71                                                      
REMARK 465     ARG A    72                                                      
REMARK 465     PRO A    73                                                      
REMARK 465     GLU A    74                                                      
REMARK 465     ILE A    75                                                      
REMARK 465     SER A    76                                                      
REMARK 465     LEU A    77                                                      
REMARK 465     LYS A   148                                                      
REMARK 465     SER A   149                                                      
REMARK 465     PRO C   416                                                      
REMARK 465     GLU C   417                                                      
REMARK 465     GLN C   418                                                      
REMARK 465     SER C   419                                                      
REMARK 465     LYS C   420                                                      
REMARK 465     ARG C   421                                                      
REMARK 465     SER C   422                                                      
REMARK 465     ASN C   543                                                      
REMARK 465     ASN C   544                                                      
REMARK 465     HIS C   545                                                      
REMARK 465     LYS B    70                                                      
REMARK 465     GLU B    71                                                      
REMARK 465     ARG B    72                                                      
REMARK 465     PRO B    73                                                      
REMARK 465     GLU B    74                                                      
REMARK 465     ILE B    75                                                      
REMARK 465     SER B    76                                                      
REMARK 465     LEU B    77                                                      
REMARK 465     LYS B   148                                                      
REMARK 465     SER B   149                                                      
REMARK 465     GLU D   417                                                      
REMARK 465     GLN D   418                                                      
REMARK 465     SER D   419                                                      
REMARK 465     LYS D   420                                                      
REMARK 465     ARG D   421                                                      
REMARK 465     SER D   422                                                      
REMARK 465     THR D   423                                                      
REMARK 465     MET D   424                                                      
REMARK 465     VAL D   425                                                      
REMARK 465     ASN D   543                                                      
REMARK 465     ASN D   544                                                      
REMARK 465     HIS D   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     SER C 249    OG                                                  
REMARK 470     ASP C 250    CG   OD1  OD2                                       
REMARK 470     LYS C 542    CG   CD   CE   NZ                                   
REMARK 470     SER D 249    OG                                                  
REMARK 470     ASP D 250    CG   OD1  OD2                                       
REMARK 470     GLU D 539    CG   CD   OE1  OE2                                  
REMARK 470     THR D 541    OG1  CG2                                            
REMARK 470     LYS D 542    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    SER A  79      102.21    -10.53                                   
REMARK 500    ASN A 138       38.67    -99.51                                   
REMARK 500    ASP C 250       14.00    -69.61                                   
REMARK 500    ARG C 258       -5.77    -53.14                                   
REMARK 500    ILE C 260      -17.77   -140.61                                   
REMARK 500    ILE C 276      -81.97   -107.07                                   
REMARK 500    LEU C 303      -90.21    -51.97                                   
REMARK 500    PRO C 307     -107.26    -31.10                                   
REMARK 500    LEU C 331      -65.04    -97.38                                   
REMARK 500    ARG C 388      -18.68     81.14                                   
REMARK 500    ALA C 412       27.92    170.42                                   
REMARK 500    GLN C 413     -169.51    -75.62                                   
REMARK 500    ILE C 414       92.39    -56.16                                   
REMARK 500    TYR C 429       -8.66    -48.92                                   
REMARK 500    THR C 541      119.25     58.83                                   
REMARK 500    SER B  79      -86.57   -110.26                                   
REMARK 500    ASP B  80     -102.59    -11.56                                   
REMARK 500    ASN B 120       70.70   -153.39                                   
REMARK 500    LYS B 134       45.28    -77.86                                   
REMARK 500    LYS B 135      -13.56   -146.95                                   
REMARK 500    THR B 136      -63.61    -99.80                                   
REMARK 500    SER B 137      151.19    -48.84                                   
REMARK 500    GLN B 140       96.85    -51.72                                   
REMARK 500    LEU D 303     -133.14     59.23                                   
REMARK 500    GLN D 304      -47.65    -18.65                                   
REMARK 500    GLN D 305       47.43    -93.13                                   
REMARK 500    PRO D 307     -178.20    -41.36                                   
REMARK 500    LYS D 308      127.12    -17.20                                   
REMARK 500    LEU D 331      -61.41   -101.06                                   
REMARK 500    ARG D 388      -14.09     76.49                                   
REMARK 500    ALA D 412       41.43   -101.32                                   
REMARK 500    ILE D 414      104.01    -49.03                                   
REMARK 500    PRO D 428       29.76    -59.28                                   
REMARK 500    TYR D 429      -25.56    -36.41                                   
REMARK 500    GLU D 461      140.99   -176.94                                   
REMARK 500    PRO D 462      152.89    -49.55                                   
REMARK 500    ASN D 466       34.55    -93.10                                   
REMARK 500    ASN D 486       71.88   -150.26                                   
REMARK 500    LEU D 502       41.57    -98.53                                   
REMARK 500    ALA D 540      -90.75    -60.30                                   
REMARK 500    THR D 541      159.34    -42.26                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 661        DISTANCE =  8.00 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 601                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C 602                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 603                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 604                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 605                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 607                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 608                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C 609                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C 610                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C 611                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C 613                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 614                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 615                 
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C 616                 
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 617                 
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 619                 
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 620                 
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 621                 
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 622                 
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C 623                 
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 624                 
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 625                 
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C 627                 
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 628                 
DBREF  1F3M A   70   149  UNP    Q13153   PAK1_HUMAN      70    149             
DBREF  1F3M B   70   149  UNP    Q13153   PAK1_HUMAN      70    149             
DBREF  1F3M C  249   545  UNP    Q13153   PAK1_HUMAN     249    545             
DBREF  1F3M D  249   545  UNP    Q13153   PAK1_HUMAN     249    545             
SEQRES   1 A   80  LYS GLU ARG PRO GLU ILE SER LEU PRO SER ASP PHE GLU          
SEQRES   2 A   80  HIS THR ILE HIS VAL GLY PHE ASP ALA VAL THR GLY GLU          
SEQRES   3 A   80  PHE THR GLY MET PRO GLU GLN TRP ALA ARG LEU LEU GLN          
SEQRES   4 A   80  THR SER ASN ILE THR LYS SER GLU GLN LYS LYS ASN PRO          
SEQRES   5 A   80  GLN ALA VAL LEU ASP VAL LEU GLU PHE TYR ASN SER LYS          
SEQRES   6 A   80  LYS THR SER ASN SER GLN LYS TYR MET SER PHE THR ASP          
SEQRES   7 A   80  LYS SER                                                      
SEQRES   1 C  297  SER ASP GLU GLU ILE LEU GLU LYS LEU ARG SER ILE VAL          
SEQRES   2 C  297  SER VAL GLY ASP PRO LYS LYS LYS TYR THR ARG PHE GLU          
SEQRES   3 C  297  LYS ILE GLY GLN GLY ALA SER GLY THR VAL TYR THR ALA          
SEQRES   4 C  297  MET ASP VAL ALA THR GLY GLN GLU VAL ALA ILE ARG GLN          
SEQRES   5 C  297  MET ASN LEU GLN GLN GLN PRO LYS LYS GLU LEU ILE ILE          
SEQRES   6 C  297  ASN GLU ILE LEU VAL MET ARG GLU ASN LYS ASN PRO ASN          
SEQRES   7 C  297  ILE VAL ASN TYR LEU ASP SER TYR LEU VAL GLY ASP GLU          
SEQRES   8 C  297  LEU TRP VAL VAL MET GLU TYR LEU ALA GLY GLY SER LEU          
SEQRES   9 C  297  THR ASP VAL VAL THR GLU THR CYS MET ASP GLU GLY GLN          
SEQRES  10 C  297  ILE ALA ALA VAL CYS ARG GLU CYS LEU GLN ALA LEU GLU          
SEQRES  11 C  297  PHE LEU HIS SER ASN GLN VAL ILE HIS ARG ASP ILE LYS          
SEQRES  12 C  297  SER ASP ASN ILE LEU LEU GLY MET ASP GLY SER VAL LYS          
SEQRES  13 C  297  LEU THR ASP PHE GLY PHE CYS ALA GLN ILE THR PRO GLU          
SEQRES  14 C  297  GLN SER LYS ARG SER THR MET VAL GLY THR PRO TYR TRP          
SEQRES  15 C  297  MET ALA PRO GLU VAL VAL THR ARG LYS ALA TYR GLY PRO          
SEQRES  16 C  297  LYS VAL ASP ILE TRP SER LEU GLY ILE MET ALA ILE GLU          
SEQRES  17 C  297  MET ILE GLU GLY GLU PRO PRO TYR LEU ASN GLU ASN PRO          
SEQRES  18 C  297  LEU ARG ALA LEU TYR LEU ILE ALA THR ASN GLY THR PRO          
SEQRES  19 C  297  GLU LEU GLN ASN PRO GLU LYS LEU SER ALA ILE PHE ARG          
SEQRES  20 C  297  ASP PHE LEU ASN ARG CYS LEU ASP MET ASP VAL GLU LYS          
SEQRES  21 C  297  ARG GLY SER ALA LYS GLU LEU LEU GLN HIS GLN PHE LEU          
SEQRES  22 C  297  LYS ILE ALA LYS PRO LEU SER SER LEU THR PRO LEU ILE          
SEQRES  23 C  297  ALA ALA ALA LYS GLU ALA THR LYS ASN ASN HIS                  
SEQRES   1 B   80  LYS GLU ARG PRO GLU ILE SER LEU PRO SER ASP PHE GLU          
SEQRES   2 B   80  HIS THR ILE HIS VAL GLY PHE ASP ALA VAL THR GLY GLU          
SEQRES   3 B   80  PHE THR GLY MET PRO GLU GLN TRP ALA ARG LEU LEU GLN          
SEQRES   4 B   80  THR SER ASN ILE THR LYS SER GLU GLN LYS LYS ASN PRO          
SEQRES   5 B   80  GLN ALA VAL LEU ASP VAL LEU GLU PHE TYR ASN SER LYS          
SEQRES   6 B   80  LYS THR SER ASN SER GLN LYS TYR MET SER PHE THR ASP          
SEQRES   7 B   80  LYS SER                                                      
SEQRES   1 D  297  SER ASP GLU GLU ILE LEU GLU LYS LEU ARG SER ILE VAL          
SEQRES   2 D  297  SER VAL GLY ASP PRO LYS LYS LYS TYR THR ARG PHE GLU          
SEQRES   3 D  297  LYS ILE GLY GLN GLY ALA SER GLY THR VAL TYR THR ALA          
SEQRES   4 D  297  MET ASP VAL ALA THR GLY GLN GLU VAL ALA ILE ARG GLN          
SEQRES   5 D  297  MET ASN LEU GLN GLN GLN PRO LYS LYS GLU LEU ILE ILE          
SEQRES   6 D  297  ASN GLU ILE LEU VAL MET ARG GLU ASN LYS ASN PRO ASN          
SEQRES   7 D  297  ILE VAL ASN TYR LEU ASP SER TYR LEU VAL GLY ASP GLU          
SEQRES   8 D  297  LEU TRP VAL VAL MET GLU TYR LEU ALA GLY GLY SER LEU          
SEQRES   9 D  297  THR ASP VAL VAL THR GLU THR CYS MET ASP GLU GLY GLN          
SEQRES  10 D  297  ILE ALA ALA VAL CYS ARG GLU CYS LEU GLN ALA LEU GLU          
SEQRES  11 D  297  PHE LEU HIS SER ASN GLN VAL ILE HIS ARG ASP ILE LYS          
SEQRES  12 D  297  SER ASP ASN ILE LEU LEU GLY MET ASP GLY SER VAL LYS          
SEQRES  13 D  297  LEU THR ASP PHE GLY PHE CYS ALA GLN ILE THR PRO GLU          
SEQRES  14 D  297  GLN SER LYS ARG SER THR MET VAL GLY THR PRO TYR TRP          
SEQRES  15 D  297  MET ALA PRO GLU VAL VAL THR ARG LYS ALA TYR GLY PRO          
SEQRES  16 D  297  LYS VAL ASP ILE TRP SER LEU GLY ILE MET ALA ILE GLU          
SEQRES  17 D  297  MET ILE GLU GLY GLU PRO PRO TYR LEU ASN GLU ASN PRO          
SEQRES  18 D  297  LEU ARG ALA LEU TYR LEU ILE ALA THR ASN GLY THR PRO          
SEQRES  19 D  297  GLU LEU GLN ASN PRO GLU LYS LEU SER ALA ILE PHE ARG          
SEQRES  20 D  297  ASP PHE LEU ASN ARG CYS LEU ASP MET ASP VAL GLU LYS          
SEQRES  21 D  297  ARG GLY SER ALA LYS GLU LEU LEU GLN HIS GLN PHE LEU          
SEQRES  22 D  297  LYS ILE ALA LYS PRO LEU SER SER LEU THR PRO LEU ILE          
SEQRES  23 D  297  ALA ALA ALA LYS GLU ALA THR LYS ASN ASN HIS                  
HET    IOD  A 601       1                                                       
HET    IOD  C 602       1                                                       
HET    IOD  D 603       1                                                       
HET    IOD  D 604       1                                                       
HET    IOD  A 605       1                                                       
HET    IOD  B 606       1                                                       
HET    IOD  A 607       1                                                       
HET    IOD  B 608       1                                                       
HET    IOD  C 609       1                                                       
HET    IOD  C 610       1                                                       
HET    IOD  C 611       1                                                       
HET    IOD  B 612       1                                                       
HET    IOD  C 613       1                                                       
HET    IOD  A 614       1                                                       
HET    IOD  B 615       1                                                       
HET    IOD  C 616       1                                                       
HET    IOD  B 617       1                                                       
HET    IOD  C 618       1                                                       
HET    IOD  D 619       1                                                       
HET    IOD  A 620       1                                                       
HET    IOD  D 621       1                                                       
HET    IOD  D 622       1                                                       
HET    IOD  C 623       1                                                       
HET    IOD  B 624       1                                                       
HET    IOD  D 625       1                                                       
HET    IOD  A 626       1                                                       
HET    IOD  C 627       1                                                       
HET    IOD  D 628       1                                                       
HETNAM     IOD IODIDE ION                                                       
FORMUL   5  IOD    28(I 1-)                                                     
FORMUL  33  HOH   *582(H2 O)                                                    
HELIX    1   1 PRO A  100  THR A  109  1                                  10    
HELIX    2   2 THR A  113  ASN A  120  1                                   8    
HELIX    3   3 ASN A  120  THR A  136  1                                  17    
HELIX    4   4 GLU C  251  ARG C  258  1                                   8    
HELIX    5   5 ASP C  265  LYS C  269  1                                   5    
HELIX    6   6 LYS C  308  ARG C  320  1                                  13    
HELIX    7   7 LEU C  352  THR C  359  1                                   8    
HELIX    8   8 ASP C  362  ASN C  383  1                                  22    
HELIX    9   9 LYS C  391  ASP C  393  5                                   3    
HELIX   10  10 ALA C  432  THR C  437  1                                   6    
HELIX   11  11 PRO C  443  GLY C  460  1                                  18    
HELIX   12  12 ASN C  468  ASN C  479  1                                  12    
HELIX   13  13 ASN C  486  LEU C  490  5                                   5    
HELIX   14  14 SER C  491  LEU C  502  1                                  12    
HELIX   15  15 SER C  511  LEU C  516  1                                   6    
HELIX   16  16 GLN C  517  ALA C  524  5                                   8    
HELIX   17  17 PRO C  526  SER C  529  5                                   4    
HELIX   18  18 LEU C  530  ALA C  540  1                                  11    
HELIX   19  19 PRO B  100  SER B  110  1                                  11    
HELIX   20  20 THR B  113  ASN B  120  1                                   8    
HELIX   21  21 ASN B  120  LYS B  134  1                                  15    
HELIX   22  22 GLU D  252  SER D  259  1                                   8    
HELIX   23  23 ASP D  265  LYS D  269  1                                   5    
HELIX   24  24 ASN D  302  GLN D  306  5                                   5    
HELIX   25  25 LEU D  311  ARG D  320  1                                  10    
HELIX   26  26 LEU D  352  THR D  359  1                                   8    
HELIX   27  27 ASP D  362  SER D  382  1                                  21    
HELIX   28  28 ALA D  432  THR D  437  1                                   6    
HELIX   29  29 LYS D  444  GLY D  460  1                                  17    
HELIX   30  30 ASN D  468  ASN D  479  1                                  12    
HELIX   31  31 SER D  491  LEU D  502  1                                  12    
HELIX   32  32 SER D  511  GLN D  517  1                                   7    
HELIX   33  33 PHE D  520  ALA D  524  5                                   5    
HELIX   34  34 PRO D  526  SER D  529  5                                   4    
HELIX   35  35 LEU D  530  THR D  541  1                                  12    
SHEET    1   A 3 GLU A  95  THR A  97  0                                        
SHEET    2   A 3 GLU A  82  ASP A  90 -1  O  GLY A  88   N  THR A  97           
SHEET    3   A 3 PHE B  81  HIS B  86 -1  O  PHE B  81   N  VAL A  87           
SHEET    1   B 2 SER A 144  PHE A 145  0                                        
SHEET    2   B 2 VAL C 385  ILE C 386 -1  N  ILE C 386   O  SER A 144           
SHEET    1   C 5 TYR C 330  TYR C 334  0                                        
SHEET    2   C 5 TRP C 341  GLU C 345 -1  O  TRP C 341   N  TYR C 334           
SHEET    3   C 5 GLU C 295  GLN C 300 -1  N  ALA C 297   O  MET C 344           
SHEET    4   C 5 GLY C 282  ASP C 289 -1  O  THR C 283   N  GLN C 300           
SHEET    5   C 5 TYR C 270  THR C 271 -1  N  THR C 271   O  MET C 288           
SHEET    1   D 5 TYR C 330  TYR C 334  0                                        
SHEET    2   D 5 TRP C 341  GLU C 345 -1  O  TRP C 341   N  TYR C 334           
SHEET    3   D 5 GLU C 295  GLN C 300 -1  N  ALA C 297   O  MET C 344           
SHEET    4   D 5 GLY C 282  ASP C 289 -1  O  THR C 283   N  GLN C 300           
SHEET    5   D 5 LYS C 275  GLY C 279 -1  N  ILE C 276   O  VAL C 284           
SHEET    1   E 3 GLY C 350  SER C 351  0                                        
SHEET    2   E 3 ILE C 395  LEU C 397 -1  N  LEU C 397   O  GLY C 350           
SHEET    3   E 3 VAL C 403  LEU C 405 -1  O  LYS C 404   N  LEU C 396           
SHEET    1   F 2 GLY B  88  ASP B  90  0                                        
SHEET    2   F 2 GLU B  95  THR B  97 -1  O  GLU B  95   N  ASP B  90           
SHEET    1   G 2 SER B 144  PHE B 145  0                                        
SHEET    2   G 2 VAL D 385  ILE D 386 -1  N  ILE D 386   O  SER B 144           
SHEET    1   H 5 TYR D 270  GLY D 279  0                                        
SHEET    2   H 5 GLY D 282  ASP D 289 -1  O  GLY D 282   N  GLY D 279           
SHEET    3   H 5 GLU D 295  MET D 301 -1  N  VAL D 296   O  ALA D 287           
SHEET    4   H 5 GLU D 339  GLU D 345 -1  O  LEU D 340   N  MET D 301           
SHEET    5   H 5 TYR D 330  VAL D 336 -1  N  LEU D 331   O  VAL D 343           
SHEET    1   I 3 GLY D 350  SER D 351  0                                        
SHEET    2   I 3 ILE D 395  LEU D 397 -1  N  LEU D 397   O  GLY D 350           
SHEET    3   I 3 VAL D 403  LEU D 405 -1  O  LYS D 404   N  LEU D 396           
SITE     1 AC1  1 ASN A 132                                                     
SITE     1 AC2  3 ASN C 468  LEU C 470  IOD C 616                               
SITE     1 AC3  1 HOH D 631                                                     
SITE     1 AC4  2 PRO D 325  IOD D 628                                          
SITE     1 AC5  1 HOH C 653                                                     
SITE     1 AC6  1 LYS A 114                                                     
SITE     1 AC7  3 GLN A 102  HOH A 667  GLY B  98                               
SITE     1 AC8  1 HOH C 628                                                     
SITE     1 AC9  2 ASN C 466  LYS D 268                                          
SITE     1 BC1  1 GLY C 364                                                     
SITE     1 BC2  1 PRO C 325                                                     
SITE     1 BC3  3 LYS A 119  IOD B 615  HOH B 652                               
SITE     1 BC4  4 ASN A 120  IOD A 614  LYS B 119  HOH C 695                    
SITE     1 BC5  3 HOH A 640  IOD C 602  HOH C 629                               
SITE     1 BC6  1 HOH B 660                                                     
SITE     1 BC7  1 MET D 399                                                     
SITE     1 BC8  1 LYS A 134                                                     
SITE     1 BC9  1 GLY D 364                                                     
SITE     1 CC1  1 ASP D 265                                                     
SITE     1 CC2  1 LYS C 444                                                     
SITE     1 CC3  1 HOH B 631                                                     
SITE     1 CC4  2 LEU C 347  ASP D 400                                          
SITE     1 CC5  2 GLU C 514  HOH C 701                                          
SITE     1 CC6  3 LYS D 323  ASN D 324  IOD D 604                               
CRYST1   94.583   94.583  147.497  90.00  90.00  90.00 P 41          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      0.010573  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010573  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006780        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system