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Database: PDB
Entry: 1G4U
LinkDB: 1G4U
Original site: 1G4U 
HEADER    SIGNALING PROTEIN                       28-OCT-00   1G4U              
TITLE     CRYSTAL STRUCTURE OF THE SALMONELLA TYROSINE PHOSPHATASE              
TITLE    2 AND GTPASE ACTIVATING PROTEIN SPTP BOUND TO RAC1                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN TYROSINE PHOSPHATASE SPTP;                         
COMPND   3 CHAIN: S;                                                            
COMPND   4 FRAGMENT: SPTP RESIDUES 161-543;                                     
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1;                
COMPND   8 CHAIN: R;                                                            
COMPND   9 FRAGMENT: RAC1 RESIDUES 1-184;                                       
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;                         
SOURCE   3 ORGANISM_TAXID: 602;                                                 
SOURCE   4 GENE: SPTP;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-3;                                
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: RAC1;                                                          
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-3                                 
KEYWDS    VIRULENCE FACTOR, GAP, TYROSINE PHOSPHATASE, 4-HELIX BUNDLE,          
KEYWDS   2 GTPASE, SIGNALING PROTEIN                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.E.STEBBINS,J.E.GALAN                                                
REVDAT   2   24-FEB-09 1G4U    1       VERSN                                    
REVDAT   1   24-JAN-01 1G4U    0                                                
JRNL        AUTH   C.E.STEBBINS,J.E.GALAN                                       
JRNL        TITL   MODULATION OF HOST SIGNALING BY A BACTERIAL MIMIC:           
JRNL        TITL 2 STRUCTURE OF THE SALMONELLA EFFECTOR SPTP BOUND TO           
JRNL        TITL 3 RAC1.                                                        
JRNL        REF    MOL.CELL                      V.   6  1449 2000              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   11163217                                                     
JRNL        DOI    10.1016/S1097-2765(00)00141-6                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 26361                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM 7% CNS                   
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2009                            
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) : 2.33                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.30                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2850                       
REMARK   3   BIN FREE R VALUE                    : 0.3600                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 51                           
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            : 4188                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 334                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.13                          
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) : 0.27                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.23                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.35                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.35                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
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 1G4U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-OCT-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB012234.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-APR-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 113                                
REMARK 200  PH                             : 5.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200HB                     
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : YALE MIRRORS                       
REMARK 200  OPTICS                         : YALE MIRRORS                       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27264                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.10600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.0000                            
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) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18 %PEG 400, 0.1M MES, 15MM SODIUM       
REMARK 280  FLOURIDE, 0.1MM ALUMINUM CHLORIDE, 2MM DTT, 2MM MAGNESIUM           
REMARK 280  CHLORIDE, PH 5.7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE        
REMARK 280  323K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3190 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, R                                  
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     ASN S   161                                                      
REMARK 465     ASP S   162                                                      
REMARK 465     VAL S   163                                                      
REMARK 465     GLY S   164                                                      
REMARK 465     ALA S   165                                                      
REMARK 465     GLU S   166                                                      
REMARK 465     SER S   461                                                      
REMARK 465     ASN S   462                                                      
REMARK 465     GLN S   463                                                      
REMARK 465     ASN S   464                                                      
REMARK 465     GLY S   465                                                      
REMARK 465     ALA S   466                                                      
REMARK 465     PRO S   467                                                      
REMARK 465     GLY S   468                                                      
REMARK 465     ARG S   469                                                      
REMARK 465     SER S   470                                                      
REMARK 465     SER S   471                                                      
REMARK 465     SER S   472                                                      
REMARK 465     ASP S   473                                                      
REMARK 465     THR S   540                                                      
REMARK 465     THR S   541                                                      
REMARK 465     ALA S   542                                                      
REMARK 465     SER S   543                                                      
REMARK 465     PRO R   181                                                      
REMARK 465     VAL R   182                                                      
REMARK 465     LYS R   183                                                      
REMARK 465     LYS R   184                                                      
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 S   545     O    HOH S   640              2.10            
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    ALA S 292     -122.11   -103.16                                   
REMARK 500    ALA S 294       45.69    -90.77                                   
REMARK 500    LEU S 305       40.32     38.27                                   
REMARK 500    ALA S 344      170.41    178.49                                   
REMARK 500    ARG S 391      -91.30   -105.06                                   
REMARK 500    ALA S 409     -112.12    -22.72                                   
REMARK 500    SER S 410      -75.93   -128.94                                   
REMARK 500    CYS S 481     -115.00   -106.23                                   
REMARK 500    PRO S 501      -16.59    -48.53                                   
REMARK 500    ARG S 516      -68.83   -137.11                                   
REMARK 500    ALA R  13        8.20     81.79                                   
REMARK 500    PHE R  37      149.86   -174.61                                   
REMARK 500    LYS R  96      -59.39   -139.86                                   
REMARK 500    PRO R 106      -76.01    -28.28                                   
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 S 577        DISTANCE =  5.40 ANGSTROMS                       
REMARK 525    HOH R1108        DISTANCE =  5.61 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 R1001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR R  17   OG1                                                    
REMARK 620 2 HOH R1073   O    80.2                                              
REMARK 620 3 GDP R1000   O2B  79.5  83.9                                        
REMARK 620 4 HOH R1072   O    86.0 162.3  82.8                                  
REMARK 620 5 THR R  35   OG1  73.1  91.2 152.7  95.3                            
REMARK 620 6 AF3 R1002   F1  172.3 103.8  94.2  88.7 113.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             AF3 R1002  AL                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH R1071   O                                                      
REMARK 620 2 GDP R1000   O3B 138.8                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG R 1001                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP R 1000                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 R 1002                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1G4W   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE SALMONELLA TYROSINE PHOSPHATASE             
REMARK 900 AND GTPASE ACTIVATING PROTEIN SPTP                                   
DBREF  1G4U S  161   543  UNP    P74873   SPTP_SALTY     161    543             
DBREF  1G4U R    1   184  UNP    P63000   RAC1_HUMAN       1    184             
SEQADV 1G4U SER R   78  UNP  P63000    PHE    78 ENGINEERED                     
SEQRES   1 S  383  ASN ASP VAL GLY ALA GLU SER LYS GLN PRO LEU LEU ASP          
SEQRES   2 S  383  ILE ALA LEU LYS GLY LEU LYS ARG THR LEU PRO GLN LEU          
SEQRES   3 S  383  GLU GLN MET ASP GLY ASN SER LEU ARG GLU ASN PHE GLN          
SEQRES   4 S  383  GLU MET ALA SER GLY ASN GLY PRO LEU ARG SER LEU MET          
SEQRES   5 S  383  THR ASN LEU GLN ASN LEU ASN LYS ILE PRO GLU ALA LYS          
SEQRES   6 S  383  GLN LEU ASN ASP TYR VAL THR THR LEU THR ASN ILE GLN          
SEQRES   7 S  383  VAL GLY VAL ALA ARG PHE SER GLN TRP GLY THR CYS GLY          
SEQRES   8 S  383  GLY GLU VAL GLU ARG TRP VAL ASP LYS ALA SER THR HIS          
SEQRES   9 S  383  GLU LEU THR GLN ALA VAL LYS LYS ILE HIS VAL ILE ALA          
SEQRES  10 S  383  LYS GLU LEU LYS ASN VAL THR ALA GLU LEU GLU LYS ILE          
SEQRES  11 S  383  GLU ALA GLY ALA PRO MET PRO GLN THR MET SER GLY PRO          
SEQRES  12 S  383  THR LEU GLY LEU ALA ARG PHE ALA VAL SER SER ILE PRO          
SEQRES  13 S  383  ILE ASN GLN GLN THR GLN VAL LYS LEU SER ASP GLY MET          
SEQRES  14 S  383  PRO VAL PRO VAL ASN THR LEU THR PHE ASP GLY LYS PRO          
SEQRES  15 S  383  VAL ALA LEU ALA GLY SER TYR PRO LYS ASN THR PRO ASP          
SEQRES  16 S  383  ALA LEU GLU ALA HIS MET LYS MET LEU LEU GLU LYS GLU          
SEQRES  17 S  383  CYS SER CYS LEU VAL VAL LEU THR SER GLU ASP GLN MET          
SEQRES  18 S  383  GLN ALA LYS GLN LEU PRO PRO TYR PHE ARG GLY SER TYR          
SEQRES  19 S  383  THR PHE GLY GLU VAL HIS THR ASN SER GLN LYS VAL SER          
SEQRES  20 S  383  SER ALA SER GLN GLY GLU ALA ILE ASP GLN TYR ASN MET          
SEQRES  21 S  383  GLN LEU SER CYS GLY GLU LYS ARG TYR THR ILE PRO VAL          
SEQRES  22 S  383  LEU HIS VAL LYS ASN TRP PRO ASP HIS GLN PRO LEU PRO          
SEQRES  23 S  383  SER THR ASP GLN LEU GLU TYR LEU ALA ASP ARG VAL LYS          
SEQRES  24 S  383  ASN SER ASN GLN ASN GLY ALA PRO GLY ARG SER SER SER          
SEQRES  25 S  383  ASP LYS HIS LEU PRO MET ILE HIS CYS LEU GLY GLY VAL          
SEQRES  26 S  383  GLY ARG THR GLY THR MET ALA ALA ALA LEU VAL LEU LYS          
SEQRES  27 S  383  ASP ASN PRO HIS SER ASN LEU GLU GLN VAL ARG ALA ASP          
SEQRES  28 S  383  PHE ARG ASP SER ARG ASN ASN ARG MET LEU GLU ASP ALA          
SEQRES  29 S  383  SER GLN PHE VAL GLN LEU LYS ALA MET GLN ALA GLN LEU          
SEQRES  30 S  383  LEU MET THR THR ALA SER                                      
SEQRES   1 R  184  MET GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA          
SEQRES   2 R  184  VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN          
SEQRES   3 R  184  ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN          
SEQRES   4 R  184  TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN          
SEQRES   5 R  184  LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP          
SEQRES   6 R  184  ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL SER          
SEQRES   7 R  184  LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU          
SEQRES   8 R  184  ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS          
SEQRES   9 R  184  CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU          
SEQRES  10 R  184  ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS          
SEQRES  11 R  184  GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU          
SEQRES  12 R  184  ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU          
SEQRES  13 R  184  CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE          
SEQRES  14 R  184  ASP GLU ALA ILE ARG ALA VAL LEU CYS PRO PRO PRO VAL          
SEQRES  15 R  184  LYS LYS                                                      
HET     MG  R1001       1                                                       
HET    GDP  R1000      28                                                       
HET    AF3  R1002       4                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM     AF3 ALUMINUM FLUORIDE                                                
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  GDP    C10 H15 N5 O11 P2                                            
FORMUL   5  AF3    AL F3                                                        
FORMUL   6  HOH   *334(H2 O)                                                    
HELIX    1   1 SER S  167  GLN S  188  1                                  22    
HELIX    2   2 ASP S  190  GLU S  196  1                                   7    
HELIX    3   3 ASN S  197  ALA S  202  1                                   6    
HELIX    4   4 GLY S  206  ASN S  217  1                                  12    
HELIX    5   5 LEU S  218  GLU S  223  5                                   6    
HELIX    6   6 ALA S  224  ASN S  236  1                                  13    
HELIX    7   7 PHE S  244  THR S  249  5                                   6    
HELIX    8   8 GLY S  252  ALA S  261  1                                  10    
HELIX    9   9 SER S  262  LEU S  280  1                                  19    
HELIX   10  10 LEU S  280  ALA S  292  1                                  13    
HELIX   11  11 THR S  353  GLU S  368  1                                  16    
HELIX   12  12 SER S  377  LYS S  384  1                                   8    
HELIX   13  13 SER S  447  ASN S  460  1                                  14    
HELIX   14  14 GLY S  486  ASN S  500  1                                  15    
HELIX   15  15 ASN S  504  ASP S  514  1                                  11    
HELIX   16  16 ASP S  523  MET S  539  1                                  17    
HELIX   17  17 GLY R   15  ASN R   26  1                                  12    
HELIX   18  18 GLN R   61  ASP R   65  5                                   5    
HELIX   19  19 LEU R   67  TYR R   72  5                                   6    
HELIX   20  20 SER R   86  LYS R   96  1                                  11    
HELIX   21  21 LYS R   96  CYS R  105  1                                  10    
HELIX   22  22 LYS R  116  ARG R  120  5                                   5    
HELIX   23  23 ASP R  122  LYS R  132  1                                  11    
HELIX   24  24 THR R  138  GLY R  150  1                                  13    
HELIX   25  25 GLY R  164  LEU R  177  1                                  14    
SHEET    1   A 9 GLN S 322  LYS S 324  0                                        
SHEET    2   A 9 PRO S 330  PHE S 338 -1  N  VAL S 331   O  VAL S 323           
SHEET    3   A 9 LYS S 341  GLY S 347 -1  O  LYS S 341   N  PHE S 338           
SHEET    4   A 9 PRO S 477  HIS S 480  1  O  PRO S 477   N  LEU S 345           
SHEET    5   A 9 CYS S 371  VAL S 374  1  O  CYS S 371   N  MET S 478           
SHEET    6   A 9 LYS S 427  VAL S 436  1  O  PRO S 432   N  LEU S 372           
SHEET    7   A 9 ILE S 415  CYS S 424 -1  O  ASP S 416   N  HIS S 435           
SHEET    8   A 9 VAL S 399  LYS S 405 -1  N  HIS S 400   O  SER S 423           
SHEET    9   A 9 SER S 393  PHE S 396 -1  O  TYR S 394   N  THR S 401           
SHEET    1   B 6 ASP R  38  VAL R  46  0                                        
SHEET    2   B 6 LYS R  49  ASP R  57 -1  O  LYS R  49   N  VAL R  46           
SHEET    3   B 6 GLN R   2  GLY R  10  1  O  GLN R   2   N  ASN R  52           
SHEET    4   B 6 VAL R  77  SER R  83  1  O  VAL R  77   N  VAL R   7           
SHEET    5   B 6 ILE R 110  THR R 115  1  O  ILE R 111   N  ILE R  80           
SHEET    6   B 6 LYS R 153  GLU R 156  1  O  LYS R 153   N  LEU R 112           
LINK        MG    MG R1001                 OG1 THR R  17     1555   1555  2.43  
LINK        MG    MG R1001                 O   HOH R1073     1555   1555  2.53  
LINK        MG    MG R1001                 O2B GDP R1000     1555   1555  2.36  
LINK        MG    MG R1001                 O   HOH R1072     1555   1555  2.23  
LINK        MG    MG R1001                 OG1 THR R  35     1555   1555  2.46  
LINK        MG    MG R1001                 F1  AF3 R1002     1555   1555  2.43  
LINK        AL   AF3 R1002                 O   HOH R1071     1555   1555  2.96  
LINK        AL   AF3 R1002                 O3B GDP R1000     1555   1555  2.79  
SITE     1 AC1  6 THR R  17  THR R  35  GDP R1000  AF3 R1002                    
SITE     2 AC1  6 HOH R1072  HOH R1073                                          
SITE     1 AC2 22 ALA R  13  VAL R  14  GLY R  15  LYS R  16                    
SITE     2 AC2 22 THR R  17  CYS R  18  LYS R 116  ASP R 118                    
SITE     3 AC2 22 SER R 158  ALA R 159  LEU R 160   MG R1001                    
SITE     4 AC2 22 AF3 R1002  HOH R1004  HOH R1010  HOH R1042                    
SITE     5 AC2 22 HOH R1072  HOH R1073  ARG S 209  THR S 249                    
SITE     6 AC2 22 CYS S 250  HOH S 680                                          
SITE     1 AC3 10 GLY R  12  ALA R  13  LYS R  16  THR R  35                    
SITE     2 AC3 10 GLY R  60  GLN R  61  GDP R1000   MG R1001                    
SITE     3 AC3 10 HOH R1071  ARG S 209                                          
CRYST1   56.722   58.260   60.324  70.03  69.51  65.03 P 1           1          
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      0.017630 -0.008210 -0.004843        0.00000                         
SCALE2      0.000000  0.018934 -0.004437        0.00000                         
SCALE3      0.000000  0.000000  0.018176        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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