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Database: PDB
Entry: 1I4L
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HEADER    SIGNALING PROTEIN                       22-FEB-01   1I4L              
TITLE     CRYSTAL STRUCTURE ANALYSIS OF RAC1-GDP IN COMPLEX WITH                
TITLE    2 ARFAPTIN (P41)                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ARFAPTIN 2;                                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 118-341;                                          
COMPND   5 SYNONYM: PARTNER OF RAC1;                                            
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1;                
COMPND   9 CHAIN: D;                                                            
COMPND  10 SYNONYM: P21-RAC1;                                                   
COMPND  11 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 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    COILED COIL, GTPASE, COMPLEX, SIGNALING PROTEIN                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.TARRICONE,B.XIAO,N.JUSTIN,S.J.GAMBLIN,S.J.SMERDON                   
REVDAT   2   24-FEB-09 1I4L    1       VERSN                                    
REVDAT   1   16-MAY-01 1I4L    0                                                
JRNL        AUTH   C.TARRICONE,B.XIAO,N.JUSTIN,P.A.WALKER,K.RITTINGER,          
JRNL        AUTH 2 S.J.GAMBLIN,S.J.SMERDON                                      
JRNL        TITL   THE STRUCTURAL BASIS OF ARFAPTIN-MEDIATED                    
JRNL        TITL 2 CROSS-TALK BETWEEN RAC AND ARF SIGNALLING PATHWAYS.          
JRNL        REF    NATURE                        V. 411   215 2001              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   11346801                                                     
JRNL        DOI    10.1038/35075620                                             
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 23325                          
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                          
REMARK   3   R VALUE            (WORKING SET) : 0.258                           
REMARK   3   FREE R VALUE                     : 0.301                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1146                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4294                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 126                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 75.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.49                            
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 1I4L COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB012896.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-MAR-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23325                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.08300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.78                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55000                            
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: MR / MAD                     
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS, PEG20K, PH 9.0, VAPOR              
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+1/4                                              
REMARK 290       4555   Y,-X,Z+3/4                                              
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       34.12100            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       17.06050            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       51.18150            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28060 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5610 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29250 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000      -17.06050            
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    22                                                      
REMARK 465     THR A   158                                                      
REMARK 465     ARG A   159                                                      
REMARK 465     GLY A   160                                                      
REMARK 465     ARG A   161                                                      
REMARK 465     LEU A   162                                                      
REMARK 465     GLU A   163                                                      
REMARK 465     SER A   164                                                      
REMARK 465     ALA A   165                                                      
REMARK 465     GLN A   166                                                      
REMARK 465     ALA A   167                                                      
REMARK 465     THR A   168                                                      
REMARK 465     PHE A   169                                                      
REMARK 465     GLN A   170                                                      
REMARK 465     ALA A   171                                                      
REMARK 465     HIS A   172                                                      
REMARK 465     ARG A   173                                                      
REMARK 465     LEU A   224                                                      
REMARK 465     GLN A   225                                                      
REMARK 465     GLN A   226                                                      
REMARK 465     PHE A   227                                                      
REMARK 465     ASN A   228                                                      
REMARK 465     ILE A   229                                                      
REMARK 465     LYS A   230                                                      
REMARK 465     LEU A   231                                                      
REMARK 465     ARG A   232                                                      
REMARK 465     PRO A   233                                                      
REMARK 465     PRO A   234                                                      
REMARK 465     GLY A   235                                                      
REMARK 465     ALA A   236                                                      
REMARK 465     GLU A   237                                                      
REMARK 465     LYS A   238                                                      
REMARK 465     PRO A   239                                                      
REMARK 465     SER A   240                                                      
REMARK 465     TRP A   241                                                      
REMARK 465     LEU A   242                                                      
REMARK 465     GLU A   243                                                      
REMARK 465     GLU A   244                                                      
REMARK 465     GLN A   245                                                      
REMARK 465     GLY B    22                                                      
REMARK 465     SER B    23                                                      
REMARK 465     ARG B    24                                                      
REMARK 465     THR B    25                                                      
REMARK 465     VAL B    26                                                      
REMARK 465     ARG B   154                                                      
REMARK 465     ASP B   155                                                      
REMARK 465     ALA B   156                                                      
REMARK 465     GLY B   157                                                      
REMARK 465     THR B   158                                                      
REMARK 465     ARG B   159                                                      
REMARK 465     GLY B   160                                                      
REMARK 465     ARG B   161                                                      
REMARK 465     LEU B   162                                                      
REMARK 465     GLU B   163                                                      
REMARK 465     SER B   164                                                      
REMARK 465     ALA B   165                                                      
REMARK 465     GLN B   166                                                      
REMARK 465     ALA B   167                                                      
REMARK 465     THR B   168                                                      
REMARK 465     PHE B   169                                                      
REMARK 465     GLN B   170                                                      
REMARK 465     ALA B   171                                                      
REMARK 465     HIS B   172                                                      
REMARK 465     LEU B   224                                                      
REMARK 465     GLN B   225                                                      
REMARK 465     GLN B   226                                                      
REMARK 465     PHE B   227                                                      
REMARK 465     ASN B   228                                                      
REMARK 465     ILE B   229                                                      
REMARK 465     LYS B   230                                                      
REMARK 465     LEU B   231                                                      
REMARK 465     ARG B   232                                                      
REMARK 465     PRO B   233                                                      
REMARK 465     PRO B   234                                                      
REMARK 465     GLY B   235                                                      
REMARK 465     ALA B   236                                                      
REMARK 465     GLU B   237                                                      
REMARK 465     LYS B   238                                                      
REMARK 465     PRO B   239                                                      
REMARK 465     SER B   240                                                      
REMARK 465     TRP B   241                                                      
REMARK 465     LEU B   242                                                      
REMARK 465     GLU B   243                                                      
REMARK 465     GLU B   244                                                      
REMARK 465     GLN B   245                                                      
REMARK 465     MET D     1                                                      
REMARK 465     PRO D   179                                                      
REMARK 465     PRO D   180                                                      
REMARK 465     PRO D   181                                                      
REMARK 465     VAL D   182                                                      
REMARK 465     LYS D   183                                                      
REMARK 465     LYS D   184                                                      
REMARK 465     ARG D   185                                                      
REMARK 465     LYS D   186                                                      
REMARK 465     ARG D   187                                                      
REMARK 465     LYS D   188                                                      
REMARK 465     CYS D   189                                                      
REMARK 465     LEU D   190                                                      
REMARK 465     LEU D   191                                                      
REMARK 465     LEU D   192                                                      
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     LEU A 220    CG   CD1  CD2                                       
REMARK 470     GLU A 221    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  29    CG   CD   OE1  OE2                                  
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   OE1  GLN D    61     O    HOH D   215              1.74            
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    ASP A  27       76.12   -108.22                                   
REMARK 500    LEU A  62      -71.29    -44.59                                   
REMARK 500    SER A  79       87.40   -156.05                                   
REMARK 500    LYS A 120      -69.63   -107.09                                   
REMARK 500    ARG A 154      140.56     76.50                                   
REMARK 500    ASP A 155       94.53    167.60                                   
REMARK 500    TYR A 212       30.50    -91.55                                   
REMARK 500    PHE A 213      -38.58   -148.61                                   
REMARK 500    GLN A 219       -3.80   -140.96                                   
REMARK 500    GLU A 221       27.48   -144.58                                   
REMARK 500    GLU B  29      -75.15    -34.92                                   
REMARK 500    LEU B  32      -25.19   -175.65                                   
REMARK 500    LEU B  50      -17.55    -47.00                                   
REMARK 500    SER B  79       76.47   -102.94                                   
REMARK 500    PHE B 110      -88.25    -57.03                                   
REMARK 500    LYS B 120      -78.22   -120.22                                   
REMARK 500    ASP B 124      -34.80    -38.35                                   
REMARK 500    ARG B 136      -60.42   -126.87                                   
REMARK 500    SER B 150      127.86    174.60                                   
REMARK 500    LEU B 151       90.81     60.80                                   
REMARK 500    ASP B 174       -5.39   -175.84                                   
REMARK 500    VAL B 183      -11.89   -177.23                                   
REMARK 500    LEU B 187      -95.00    -54.91                                   
REMARK 500    PHE B 189       -7.93   -151.98                                   
REMARK 500    LYS B 218      -72.28    -67.39                                   
REMARK 500    GLN B 222       43.74    -96.41                                   
REMARK 500    ASP D  11      138.65    -34.70                                   
REMARK 500    ALA D  13       -8.42     80.20                                   
REMARK 500    TYR D  32      -10.21     80.18                                   
REMARK 500    ILE D  33       81.86     54.66                                   
REMARK 500    THR D  35      112.79      5.26                                   
REMARK 500    ASP D  47       82.84     66.26                                   
REMARK 500    PRO D  69       -6.14    -57.56                                   
REMARK 500    VAL D  77      117.86   -163.08                                   
REMARK 500    LYS D  96      -56.77   -127.66                                   
REMARK 500    CYS D 105       77.69   -119.50                                   
REMARK 500    ASN D 107       -0.82    164.90                                   
REMARK 500    LYS D 116       69.19     72.27                                   
REMARK 500    LEU D 119       44.53    -74.92                                   
REMARK 500    ASP D 124      -70.48    170.50                                   
REMARK 500    LYS D 133       37.49     70.05                                   
REMARK 500    GLN D 141       71.69     51.54                                   
REMARK 500    ILE D 149      -71.08    -99.80                                   
REMARK 500    GLN D 162      -10.07     68.91                                   
REMARK 500    LEU D 165      -70.00    -63.63                                   
REMARK 500    VAL D 168      -39.35    -34.48                                   
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 252        DISTANCE = 10.99 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 D 201  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GDP D 200   O2B                                                    
REMARK 620 2 THR D  17   OG1  72.6                                              
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 D 201                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP D 200                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1I49   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ARFAPTIN                                        
REMARK 900 RELATED ID: 1I4D   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RAC1GDP IN COMPLEX WITH ARFAPTIN (P21)          
REMARK 900 RELATED ID: 1I4T   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF RAC1-GMPPNP IN COMPLEX WITH            
REMARK 900 ARFAPTIN                                                             
DBREF  1I4L A   22   245  UNP    P53365   ARFP2_HUMAN    118    341             
DBREF  1I4L B   22   245  UNP    P53365   ARFP2_HUMAN    118    341             
DBREF  1I4L D    1   192  UNP    P63000   RAC1_HUMAN       1    192             
SEQRES   1 A  224  GLY SER ARG THR VAL ASP LEU GLU LEU GLU LEU GLN ILE          
SEQRES   2 A  224  GLU LEU LEU ARG GLU THR LYS ARG LYS TYR GLU SER VAL          
SEQRES   3 A  224  LEU GLN LEU GLY ARG ALA LEU THR ALA HIS LEU TYR SER          
SEQRES   4 A  224  LEU LEU GLN THR GLN HIS ALA LEU GLY ASP ALA PHE ALA          
SEQRES   5 A  224  ASP LEU SER GLN LYS SER PRO GLU LEU GLN GLU GLU PHE          
SEQRES   6 A  224  GLY TYR ASN ALA GLU THR GLN LYS LEU LEU CYS LYS ASN          
SEQRES   7 A  224  GLY GLU THR LEU LEU GLY ALA VAL ASN PHE PHE VAL SER          
SEQRES   8 A  224  SER ILE ASN THR LEU VAL THR LYS THR MET GLU ASP THR          
SEQRES   9 A  224  LEU MET THR VAL LYS GLN TYR GLU ALA ALA ARG LEU GLU          
SEQRES  10 A  224  TYR ASP ALA TYR ARG THR ASP LEU GLU GLU LEU SER LEU          
SEQRES  11 A  224  GLY PRO ARG ASP ALA GLY THR ARG GLY ARG LEU GLU SER          
SEQRES  12 A  224  ALA GLN ALA THR PHE GLN ALA HIS ARG ASP LYS TYR GLU          
SEQRES  13 A  224  LYS LEU ARG GLY ASP VAL ALA ILE LYS LEU LYS PHE LEU          
SEQRES  14 A  224  GLU GLU ASN LYS ILE LYS VAL MET HIS LYS GLN LEU LEU          
SEQRES  15 A  224  LEU PHE HIS ASN ALA VAL SER ALA TYR PHE ALA GLY ASN          
SEQRES  16 A  224  GLN LYS GLN LEU GLU GLN THR LEU GLN GLN PHE ASN ILE          
SEQRES  17 A  224  LYS LEU ARG PRO PRO GLY ALA GLU LYS PRO SER TRP LEU          
SEQRES  18 A  224  GLU GLU GLN                                                  
SEQRES   1 B  224  GLY SER ARG THR VAL ASP LEU GLU LEU GLU LEU GLN ILE          
SEQRES   2 B  224  GLU LEU LEU ARG GLU THR LYS ARG LYS TYR GLU SER VAL          
SEQRES   3 B  224  LEU GLN LEU GLY ARG ALA LEU THR ALA HIS LEU TYR SER          
SEQRES   4 B  224  LEU LEU GLN THR GLN HIS ALA LEU GLY ASP ALA PHE ALA          
SEQRES   5 B  224  ASP LEU SER GLN LYS SER PRO GLU LEU GLN GLU GLU PHE          
SEQRES   6 B  224  GLY TYR ASN ALA GLU THR GLN LYS LEU LEU CYS LYS ASN          
SEQRES   7 B  224  GLY GLU THR LEU LEU GLY ALA VAL ASN PHE PHE VAL SER          
SEQRES   8 B  224  SER ILE ASN THR LEU VAL THR LYS THR MET GLU ASP THR          
SEQRES   9 B  224  LEU MET THR VAL LYS GLN TYR GLU ALA ALA ARG LEU GLU          
SEQRES  10 B  224  TYR ASP ALA TYR ARG THR ASP LEU GLU GLU LEU SER LEU          
SEQRES  11 B  224  GLY PRO ARG ASP ALA GLY THR ARG GLY ARG LEU GLU SER          
SEQRES  12 B  224  ALA GLN ALA THR PHE GLN ALA HIS ARG ASP LYS TYR GLU          
SEQRES  13 B  224  LYS LEU ARG GLY ASP VAL ALA ILE LYS LEU LYS PHE LEU          
SEQRES  14 B  224  GLU GLU ASN LYS ILE LYS VAL MET HIS LYS GLN LEU LEU          
SEQRES  15 B  224  LEU PHE HIS ASN ALA VAL SER ALA TYR PHE ALA GLY ASN          
SEQRES  16 B  224  GLN LYS GLN LEU GLU GLN THR LEU GLN GLN PHE ASN ILE          
SEQRES  17 B  224  LYS LEU ARG PRO PRO GLY ALA GLU LYS PRO SER TRP LEU          
SEQRES  18 B  224  GLU GLU GLN                                                  
SEQRES   1 D  192  MET GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA          
SEQRES   2 D  192  VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN          
SEQRES   3 D  192  ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN          
SEQRES   4 D  192  TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN          
SEQRES   5 D  192  LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP          
SEQRES   6 D  192  ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE          
SEQRES   7 D  192  LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU          
SEQRES   8 D  192  ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS          
SEQRES   9 D  192  CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU          
SEQRES  10 D  192  ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS          
SEQRES  11 D  192  GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU          
SEQRES  12 D  192  ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU          
SEQRES  13 D  192  CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE          
SEQRES  14 D  192  ASP GLU ALA ILE ARG ALA VAL LEU CYS PRO PRO PRO VAL          
SEQRES  15 D  192  LYS LYS ARG LYS ARG LYS CYS LEU LEU LEU                      
HET     MG  D 201       1                                                       
HET    GDP  D 200      28                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
FORMUL   4   MG    MG 2+                                                        
FORMUL   5  GDP    C10 H15 N5 O11 P2                                            
FORMUL   6  HOH   *126(H2 O)                                                    
HELIX    1   1 ASP A   27  LYS A   78  1                                  52    
HELIX    2   2 SER A   79  GLU A   81  5                                   3    
HELIX    3   3 LEU A   82  LYS A  120  1                                  39    
HELIX    4   4 LYS A  120  LEU A  151  1                                  32    
HELIX    5   5 ASP A  174  LYS A  218  1                                  45    
HELIX    6   6 GLU B   29  SER B   79  1                                  51    
HELIX    7   7 LEU B   82  LYS B  120  1                                  39    
HELIX    8   8 LYS B  120  ALA B  135  1                                  16    
HELIX    9   9 ARG B  136  LEU B  149  1                                  14    
HELIX   10  10 LYS B  175  ASP B  182  1                                   8    
HELIX   11  11 LYS B  186  PHE B  189  5                                   4    
HELIX   12  12 LEU B  190  LEU B  220  1                                  31    
HELIX   13  13 GLY D   15  ASN D   26  1                                  12    
HELIX   14  14 GLN D   61  ASP D   65  5                                   5    
HELIX   15  15 ARG D   68  TYR D   72  5                                   5    
HELIX   16  16 SER D   86  LYS D   96  1                                  11    
HELIX   17  17 LYS D   96  CYS D  105  1                                  10    
HELIX   18  18 ASP D  124  LYS D  132  1                                   9    
HELIX   19  19 GLY D  142  GLY D  150  1                                   9    
HELIX   20  20 GLY D  164  CYS D  178  1                                  15    
SHEET    1   A 6 TYR D  40  MET D  45  0                                        
SHEET    2   A 6 PRO D  50  TRP D  56 -1  N  VAL D  51   O  VAL D  44           
SHEET    3   A 6 ALA D   3  VAL D   9  1  O  ILE D   4   N  GLY D  54           
SHEET    4   A 6 VAL D  77  SER D  83  1  N  VAL D  77   O  LYS D   5           
SHEET    5   A 6 ILE D 111  THR D 115  1  N  ILE D 111   O  PHE D  78           
SHEET    6   A 6 LYS D 153  CYS D 157  1  O  LYS D 153   N  LEU D 112           
LINK        MG    MG D 201                 O2B GDP D 200     1555   1555  2.18  
LINK        MG    MG D 201                 OG1 THR D  17     1555   1555  2.13  
SITE     1 AC1  2 THR D  17  GDP D 200                                          
SITE     1 AC2 15 GLY D  12  ALA D  13  VAL D  14  GLY D  15                    
SITE     2 AC2 15 LYS D  16  THR D  17  CYS D  18  PHE D  28                    
SITE     3 AC2 15 LYS D 116  ASP D 118  LEU D 119  ALA D 159                    
SITE     4 AC2 15 LEU D 160   MG D 201  HOH D 214                               
CRYST1  112.379  112.379   68.242  90.00  90.00  90.00 P 41          8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008898  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008898  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014654        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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