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Database: PDB
Entry: 1RYF
LinkDB: 1RYF
Original site: 1RYF 
HEADER    HYDROLASE                               22-DEC-03   1RYF              
TITLE     ALTERNATIVE SPLICING OF RAC1 GENERATES RAC1B, A SELF-ACTIVATING GTPASE
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1 ISOFORM RAC1B;  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 1-201;                                            
COMPND   5 SYNONYM: RAC1B;                                                      
COMPND   6 EC: 3.6.5.2;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PGEX4T1                                   
KEYWDS    GTP BINDING, HYDROLASE                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.R.AHMADIAN,D.FIEGEN                                                 
REVDAT   4   13-JUL-11 1RYF    1       VERSN                                    
REVDAT   3   24-FEB-09 1RYF    1       VERSN                                    
REVDAT   2   10-FEB-04 1RYF    1       JRNL                                     
REVDAT   1   27-JAN-04 1RYF    0                                                
JRNL        AUTH   D.FIEGEN,L.C.HAEUSLER,L.BLUMENSTEIN,U.HERBRAND,R.DVORSKY,    
JRNL        AUTH 2 I.R.VETTER,M.R.AHMADIAN                                      
JRNL        TITL   ALTERNATIVE SPLICING OF RAC1 GENERATES RAC1B, A              
JRNL        TITL 2 SELF-ACTIVATING GTPASE                                       
JRNL        REF    J.BIOL.CHEM.                  V. 279  4743 2004              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   14625275                                                     
JRNL        DOI    10.1074/JBC.M310281200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.19                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.92                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 37724                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1958                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.75                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.79                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2657                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2360                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 139                          
REMARK   3   BIN FREE R VALUE                    : 0.3400                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2580                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 273                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.38                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.24000                                              
REMARK   3    B22 (A**2) : 0.24000                                              
REMARK   3    B33 (A**2) : -0.48000                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.113         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.111         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.076         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.456         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.951                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2701 ; 0.021 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2473 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3688 ; 1.873 ; 2.000       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5786 ; 0.966 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   333 ; 6.774 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   434 ; 0.137 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2884 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   486 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   507 ; 0.211 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2815 ; 0.249 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1562 ; 0.088 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   190 ; 0.173 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     1 ; 0.033 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    13 ; 0.208 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    52 ; 0.356 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    27 ; 0.186 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1684 ; 1.164 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2739 ; 1.974 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1017 ; 2.881 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   949 ; 4.429 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   201                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.7810  62.6790  41.1640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0546 T22:   0.0536                                     
REMARK   3      T33:   0.0701 T12:  -0.0103                                     
REMARK   3      T13:  -0.0236 T23:   0.0298                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6853 L22:   1.9991                                     
REMARK   3      L33:   2.5305 L12:   0.7860                                     
REMARK   3      L13:  -1.2975 L23:  -0.2259                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1242 S12:   0.2702 S13:   0.1571                       
REMARK   3      S21:  -0.1221 S22:   0.1368 S23:   0.0012                       
REMARK   3      S31:  -0.0013 S32:  -0.1219 S33:  -0.0126                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   199                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.1320  62.7900   7.2190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0064 T22:   0.0554                                     
REMARK   3      T33:   0.0822 T12:  -0.0110                                     
REMARK   3      T13:  -0.0095 T23:  -0.0333                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9507 L22:   1.7649                                     
REMARK   3      L33:   2.1915 L12:  -0.2766                                     
REMARK   3      L13:  -0.9545 L23:  -0.0428                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0145 S12:  -0.2814 S13:   0.2241                       
REMARK   3      S21:   0.1290 S22:   0.0542 S23:   0.0070                       
REMARK   3      S31:   0.0049 S32:   0.0557 S33:  -0.0397                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1RYF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-DEC-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB021147.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39688                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.922                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
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: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1MH1                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   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       25.82000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       48.39500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.34500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       48.39500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.82000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.34500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    60                                                      
REMARK 465     GLN A    61                                                      
REMARK 465     GLU A    62                                                      
REMARK 465     ASP A    63                                                      
REMARK 465     TYR A    64                                                      
REMARK 465     ASP A    65                                                      
REMARK 465     ARG A    66                                                      
REMARK 465     LEU A    67                                                      
REMARK 465     ARG A    68                                                      
REMARK 465     PRO A    69                                                      
REMARK 465     LEU A    70                                                      
REMARK 465     SER A    71                                                      
REMARK 465     TYR A    72                                                      
REMARK 465     PRO A    73                                                      
REMARK 465     GLN A    74                                                      
REMARK 465     THR A    75                                                      
REMARK 465     VAL A    76                                                      
REMARK 465     GLY A    77                                                      
REMARK 465     GLU A    78                                                      
REMARK 465     THR A    79                                                      
REMARK 465     TYR A    80                                                      
REMARK 465     GLY A    81                                                      
REMARK 465     LYS A    82                                                      
REMARK 465     ASP A    83                                                      
REMARK 465     ILE A    84                                                      
REMARK 465     THR A    85                                                      
REMARK 465     SER A    86                                                      
REMARK 465     ARG A    87                                                      
REMARK 465     GLY A    88                                                      
REMARK 465     LYS A    89                                                      
REMARK 465     ASP A    90                                                      
REMARK 465     LYS A    91                                                      
REMARK 465     PRO A    92                                                      
REMARK 465     ALA B    59                                                      
REMARK 465     GLY B    60                                                      
REMARK 465     GLN B    61                                                      
REMARK 465     GLU B    62                                                      
REMARK 465     ASP B    63                                                      
REMARK 465     TYR B    64                                                      
REMARK 465     ASP B    65                                                      
REMARK 465     ARG B    66                                                      
REMARK 465     LEU B    67                                                      
REMARK 465     ARG B    68                                                      
REMARK 465     PRO B    69                                                      
REMARK 465     LEU B    70                                                      
REMARK 465     SER B    71                                                      
REMARK 465     TYR B    72                                                      
REMARK 465     PRO B    73                                                      
REMARK 465     GLN B    74                                                      
REMARK 465     THR B    75                                                      
REMARK 465     VAL B    76                                                      
REMARK 465     GLY B    77                                                      
REMARK 465     GLU B    78                                                      
REMARK 465     THR B    79                                                      
REMARK 465     TYR B    80                                                      
REMARK 465     GLY B    81                                                      
REMARK 465     LYS B    82                                                      
REMARK 465     ASP B    83                                                      
REMARK 465     ILE B    84                                                      
REMARK 465     THR B    85                                                      
REMARK 465     SER B    86                                                      
REMARK 465     ARG B    87                                                      
REMARK 465     GLY B    88                                                      
REMARK 465     LYS B    89                                                      
REMARK 465     ASP B    90                                                      
REMARK 465     LYS B    91                                                      
REMARK 465     PRO B    92                                                      
REMARK 465     PRO B   200                                                      
REMARK 465     VAL B   201                                                      
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     VAL A  36    CG1  CG2                                            
REMARK 470     ILE A  93    CG1  CG2  CD1                                       
REMARK 470     VAL A 201    CG1  CG2                                            
REMARK 470     VAL B  36    CG1  CG2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B  1553     O    HOH B  1651              1.92            
REMARK 500   O    HOH A   623     O    HOH A   643              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG A 139   CG    ARG A 139   CD     -0.152                       
REMARK 500    VAL A 171   CB    VAL A 171   CG2    -0.130                       
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    ASP A  47   CB  -  CG  -  OD2 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ASP A  95   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP A 140   CB  -  CG  -  OD2 ANGL. DEV. =   7.7 DEGREES          
REMARK 500    ASP A 141   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP B  38   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP B  47   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP B  95   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP B 143   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG B 182   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 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    SER A   2A      97.48     63.08                                   
REMARK 500    LYS A 115      -52.96   -124.55                                   
REMARK 500    LYS B 115      -51.83   -127.26                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR B 127        24.8      L          L   OUTSIDE RANGE           
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 A 661        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH A 663        DISTANCE =  5.51 ANGSTROMS                       
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                              MG A 539  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GDP A 538   O2B                                                    
REMARK 620 2 HOH A 541   O    93.4                                              
REMARK 620 3 HOH A 605   O    96.8  88.6                                        
REMARK 620 4 THR A  17   OG1  93.0 172.9  87.5                                  
REMARK 620 5 HOH A 606   O    86.2  91.5 176.9  92.1                            
REMARK 620 6 HOH A 540   O   175.0  84.9  87.8  89.1  89.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1539  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GDP B1538   O2B                                                    
REMARK 620 2 HOH B1585   O   102.5                                              
REMARK 620 3 HOH B1587   O    95.5  92.0                                        
REMARK 620 4 HOH B1586   O    87.8 167.6  93.9                                  
REMARK 620 5 HOH B1584   O   172.5  84.5  87.1  85.0                            
REMARK 620 6 THR B  17   OG1  93.2  85.3 171.3  87.3  84.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 539                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1539                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 538                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 1538                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1RYH   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH 5'-GUANOSYL-IMIDO-                   
REMARK 900 TRIPHOSPHATE                                                         
DBREF  1RYF A    1   201  UNP    P63000   RAC1_HUMAN       1    201             
DBREF  1RYF B    1   201  UNP    P63000   RAC1_HUMAN       1    201             
SEQADV 1RYF GLY A    1A UNP  P63000              CLONING ARTIFACT               
SEQADV 1RYF SER A    2A UNP  P63000              CLONING ARTIFACT               
SEQADV 1RYF GLY B    1A UNP  P63000              CLONING ARTIFACT               
SEQADV 1RYF SER B    2A UNP  P63000              CLONING ARTIFACT               
SEQRES   1 A  203  GLY SER MET GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP          
SEQRES   2 A  203  GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR          
SEQRES   3 A  203  THR ASN ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE          
SEQRES   4 A  203  ASP ASN TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO          
SEQRES   5 A  203  VAL ASN LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP          
SEQRES   6 A  203  TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN THR VAL          
SEQRES   7 A  203  GLY GLU THR TYR GLY LYS ASP ILE THR SER ARG GLY LYS          
SEQRES   8 A  203  ASP LYS PRO ILE ALA ASP VAL PHE LEU ILE CYS PHE SER          
SEQRES   9 A  203  LEU VAL SER PRO ALA SER PHE GLU ASN VAL ARG ALA LYS          
SEQRES  10 A  203  TRP TYR PRO GLU VAL ARG HIS HIS CYS PRO ASN THR PRO          
SEQRES  11 A  203  ILE ILE LEU VAL GLY THR LYS LEU ASP LEU ARG ASP ASP          
SEQRES  12 A  203  LYS ASP THR ILE GLU LYS LEU LYS GLU LYS LYS LEU THR          
SEQRES  13 A  203  PRO ILE THR TYR PRO GLN GLY LEU ALA MET ALA LYS GLU          
SEQRES  14 A  203  ILE GLY ALA VAL LYS TYR LEU GLU CYS SER ALA LEU THR          
SEQRES  15 A  203  GLN ARG GLY LEU LYS THR VAL PHE ASP GLU ALA ILE ARG          
SEQRES  16 A  203  ALA VAL LEU CYS PRO PRO PRO VAL                              
SEQRES   1 B  203  GLY SER MET GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP          
SEQRES   2 B  203  GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR          
SEQRES   3 B  203  THR ASN ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE          
SEQRES   4 B  203  ASP ASN TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO          
SEQRES   5 B  203  VAL ASN LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP          
SEQRES   6 B  203  TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN THR VAL          
SEQRES   7 B  203  GLY GLU THR TYR GLY LYS ASP ILE THR SER ARG GLY LYS          
SEQRES   8 B  203  ASP LYS PRO ILE ALA ASP VAL PHE LEU ILE CYS PHE SER          
SEQRES   9 B  203  LEU VAL SER PRO ALA SER PHE GLU ASN VAL ARG ALA LYS          
SEQRES  10 B  203  TRP TYR PRO GLU VAL ARG HIS HIS CYS PRO ASN THR PRO          
SEQRES  11 B  203  ILE ILE LEU VAL GLY THR LYS LEU ASP LEU ARG ASP ASP          
SEQRES  12 B  203  LYS ASP THR ILE GLU LYS LEU LYS GLU LYS LYS LEU THR          
SEQRES  13 B  203  PRO ILE THR TYR PRO GLN GLY LEU ALA MET ALA LYS GLU          
SEQRES  14 B  203  ILE GLY ALA VAL LYS TYR LEU GLU CYS SER ALA LEU THR          
SEQRES  15 B  203  GLN ARG GLY LEU LYS THR VAL PHE ASP GLU ALA ILE ARG          
SEQRES  16 B  203  ALA VAL LEU CYS PRO PRO PRO VAL                              
HET     MG  A 539       1                                                       
HET     MG  B1539       1                                                       
HET    GDP  A 538      28                                                       
HET    GDP  B1538      28                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   5  GDP    2(C10 H15 N5 O11 P2)                                         
FORMUL   7  HOH   *273(H2 O)                                                    
HELIX    1   1 GLY A   15  ASN A   26  1                                  12    
HELIX    2   2 SER A  105  LYS A  115  1                                  11    
HELIX    3   3 LYS A  115  CYS A  124  1                                  10    
HELIX    4   4 LYS A  135  ASP A  140  1                                   6    
HELIX    5   5 ASP A  141  GLU A  150  1                                  10    
HELIX    6   6 THR A  157  GLY A  169  1                                  13    
HELIX    7   7 GLY A  183  CYS A  197  1                                  15    
HELIX    8   8 GLY B   15  ASN B   26  1                                  12    
HELIX    9   9 SER B  105  LYS B  115  1                                  11    
HELIX   10  10 LYS B  115  CYS B  124  1                                  10    
HELIX   11  11 LYS B  135  ASP B  140  1                                   6    
HELIX   12  12 ASP B  141  LYS B  151  1                                  11    
HELIX   13  13 THR B  157  GLY B  169  1                                  13    
HELIX   14  14 GLY B  183  CYS B  197  1                                  15    
SHEET    1   A 6 ASN A  39  VAL A  46  0                                        
SHEET    2   A 6 LYS A  49  ASP A  57 -1  O  LEU A  55   N  TYR A  40           
SHEET    3   A 6 SER A   2A GLY A  10  1  N  CYS A   6   O  GLY A  54           
SHEET    4   A 6 SER B   2A GLY B  10 -1  O  MET B   1   N  MET A   1           
SHEET    5   A 6 LYS B  49  ASP B  57  1  O  GLY B  54   N  CYS B   6           
SHEET    6   A 6 ASN B  39  VAL B  46 -1  N  TYR B  40   O  LEU B  55           
SHEET    1   B 8 LYS A 172  GLU A 175  0                                        
SHEET    2   B 8 ILE A 129  THR A 134  1  N  LEU A 131   O  LYS A 172           
SHEET    3   B 8 VAL A  96  SER A 102  1  N  PHE A  97   O  ILE A 130           
SHEET    4   B 8 SER A   2A GLY A  10  1  N  VAL A   9   O  CYS A 100           
SHEET    5   B 8 SER B   2A GLY B  10 -1  O  MET B   1   N  MET A   1           
SHEET    6   B 8 VAL B  96  SER B 102  1  O  CYS B 100   N  VAL B   9           
SHEET    7   B 8 ILE B 129  THR B 134  1  O  ILE B 130   N  PHE B  97           
SHEET    8   B 8 LYS B 172  GLU B 175  1  O  LEU B 174   N  GLY B 133           
LINK         O2B GDP A 538                MG    MG A 539     1555   1555  2.00  
LINK        MG    MG A 539                 O   HOH A 541     1555   1555  2.10  
LINK        MG    MG A 539                 O   HOH A 605     1555   1555  2.05  
LINK        MG    MG A 539                 OG1 THR A  17     1555   1555  2.09  
LINK        MG    MG A 539                 O   HOH A 606     1555   1555  2.08  
LINK        MG    MG A 539                 O   HOH A 540     1555   1555  2.20  
LINK         O2B GDP B1538                MG    MG B1539     1555   1555  1.96  
LINK        MG    MG B1539                 O   HOH B1585     1555   1555  2.08  
LINK        MG    MG B1539                 O   HOH B1587     1555   1555  2.07  
LINK        MG    MG B1539                 O   HOH B1586     1555   1555  2.06  
LINK        MG    MG B1539                 O   HOH B1584     1555   1555  2.36  
LINK        MG    MG B1539                 OG1 THR B  17     1555   1555  2.09  
CISPEP   1 GLY A    1A   SER A    2A         0        26.66                     
SITE     1 AC1  6 THR A  17  GDP A 538  HOH A 540  HOH A 541                    
SITE     2 AC1  6 HOH A 605  HOH A 606                                          
SITE     1 AC2  6 THR B  17  GDP B1538  HOH B1584  HOH B1585                    
SITE     2 AC2  6 HOH B1586  HOH B1587                                          
SITE     1 AC3 23 ALA A  13  VAL A  14  GLY A  15  LYS A  16                    
SITE     2 AC3 23 THR A  17  CYS A  18  PHE A  28  LYS A 135                    
SITE     3 AC3 23 ASP A 137  LEU A 138  SER A 177  ALA A 178                    
SITE     4 AC3 23 LEU A 179   MG A 539  HOH A 541  HOH A 542                    
SITE     5 AC3 23 HOH A 575  HOH A 585  HOH A 605  HOH A 606                    
SITE     6 AC3 23 HOH A 623  HOH A 641  HOH A 645                               
SITE     1 AC4 21 ALA B  13  VAL B  14  GLY B  15  LYS B  16                    
SITE     2 AC4 21 THR B  17  CYS B  18  PHE B  28  LYS B 135                    
SITE     3 AC4 21 ASP B 137  LEU B 138  SER B 177  ALA B 178                    
SITE     4 AC4 21 LEU B 179   MG B1539  HOH B1558  HOH B1575                    
SITE     5 AC4 21 HOH B1586  HOH B1587  HOH B1598  HOH B1642                    
SITE     6 AC4 21 HOH B1663                                                     
CRYST1   51.640   78.690   96.790  90.00  90.00  90.00 P 21 21 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      0.019365  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012708  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010332        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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