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Database: PDB
Entry: 2NZ8
LinkDB: 2NZ8
Original site: 2NZ8 
HEADER    SIGNALING PROTEIN,CELL CYCLE            22-NOV-06   2NZ8              
TITLE     N-TERMINAL DHPH CASSETTE OF TRIO IN COMPLEX WITH NUCLEOTIDE-          
TITLE    2 FREE RAC1                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1                 
COMPND   3 ISOFORM RAC1;                                                        
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: SOLUBLE PART (RESIDUES 1-177);                             
COMPND   6 SYNONYM: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1; P21-            
COMPND   7 RAC1; RAS-LIKE PROTEIN TC25;                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: TRIPLE FUNCTIONAL DOMAIN PROTEIN;                          
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: N-TERMINAL DH/PH CASSETTE (RESIDUES 1226-1535);            
COMPND  13 SYNONYM: PTPRF-INTERACTING PROTEIN;                                  
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: RAC1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: TRIO;                                                          
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PPROEX-HTA                                
KEYWDS    TRIO; RAC1; DBL-FAMILY GEF; RHO-FAMILY GTPASE; DH/PH                  
KEYWDS   2 CASSETTE, SIGNALING PROTEIN,CELL CYCLE                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.K.CHHATRIWALA,L.BETTS,D.K.WORTHYLAKE,J.SONDEK                       
REVDAT   3   24-FEB-09 2NZ8    1       VERSN                                    
REVDAT   2   05-JUN-07 2NZ8    1       JRNL                                     
REVDAT   1   10-APR-07 2NZ8    0                                                
JRNL        AUTH   M.K.CHHATRIWALA,L.BETTS,D.K.WORTHYLAKE,J.SONDEK              
JRNL        TITL   THE DH AND PH DOMAINS OF TRIO COORDINATELY ENGAGE            
JRNL        TITL 2 RHO GTPASES FOR THEIR EFFICIENT ACTIVATION                   
JRNL        REF    J.MOL.BIOL.                   V. 368  1307 2007              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   17391702                                                     
JRNL        DOI    10.1016/J.JMB.2007.02.060                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2                                           
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.41                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 38900                          
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) : 0.225                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1968                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2718                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.89                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2610                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 129                          
REMARK   3   BIN FREE R VALUE                    : 0.3070                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3663                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 242                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.24                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.20000                                              
REMARK   3    B33 (A**2) : -0.21000                                             
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): 0.195         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.165         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.111         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.565         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.939                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.917                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3737 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5043 ; 1.138 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   451 ; 5.078 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   170 ;34.698 ;24.824       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   696 ;15.149 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;16.585 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   564 ; 0.083 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2767 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1729 ; 0.190 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2539 ; 0.300 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   251 ; 0.148 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    42 ; 0.200 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    14 ; 0.094 ; 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):  2359 ; 0.520 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3679 ; 0.848 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1584 ; 1.260 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1364 ; 1.913 ; 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  : 4                                          
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   177                          
REMARK   3    ORIGIN FOR THE GROUP (A):  48.0850  32.1290  -7.1214              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1328 T22:  -0.1902                                     
REMARK   3      T33:  -0.1971 T12:  -0.0171                                     
REMARK   3      T13:  -0.0041 T23:   0.0069                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7443 L22:   2.4427                                     
REMARK   3      L33:   4.6849 L12:   0.1444                                     
REMARK   3      L13:  -0.8049 L23:   0.2378                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0496 S12:   0.0714 S13:  -0.0816                       
REMARK   3      S21:  -0.3355 S22:   0.0723 S23:  -0.1213                       
REMARK   3      S31:   0.3195 S32:   0.0851 S33:  -0.0227                       
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  1231        B  1411                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.3108  41.1008  15.5037              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1602 T22:  -0.1770                                     
REMARK   3      T33:  -0.2421 T12:  -0.0394                                     
REMARK   3      T13:   0.0117 T23:   0.0000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5060 L22:   3.5037                                     
REMARK   3      L33:   1.8732 L12:  -0.0472                                     
REMARK   3      L13:  -0.2673 L23:  -0.2385                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0028 S12:  -0.1939 S13:   0.0513                       
REMARK   3      S21:   0.3334 S22:   0.0504 S23:  -0.0188                       
REMARK   3      S31:   0.0679 S32:   0.0635 S33:  -0.0531                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  1412        B  1417                          
REMARK   3    RESIDUE RANGE :   B  1423        B  1434                          
REMARK   3    RESIDUE RANGE :   B  1449        B  1497                          
REMARK   3    RESIDUE RANGE :   B  1505        B  1535                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.2525  11.8642  14.9497              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2877 T22:  -0.0272                                     
REMARK   3      T33:   1.2075 T12:  -0.2386                                     
REMARK   3      T13:  -0.6478 T23:   0.3116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  30.0993 L22:  12.5573                                     
REMARK   3      L33:  14.3880 L12:  -1.8593                                     
REMARK   3      L13:  13.3474 L23:  -1.6695                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   2.9268 S12:  -1.1897 S13:  -5.8947                       
REMARK   3      S21:   0.3162 S22:  -0.0338 S23:  -0.0182                       
REMARK   3      S31:   2.5485 S32:  -0.6843 S33:  -2.8930                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  2000        B  2241                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.9646  37.1742   4.9849              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0604 T22:  -0.0833                                     
REMARK   3      T33:  -0.0568 T12:  -0.0114                                     
REMARK   3      T13:  -0.0088 T23:   0.0335                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1617 L22:   2.3093                                     
REMARK   3      L33:   2.3013 L12:  -0.2572                                     
REMARK   3      L13:  -0.4692 L23:   0.5297                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0079 S12:  -0.0112 S13:   0.0247                       
REMARK   3      S21:  -0.0661 S22:   0.0337 S23:   0.1927                       
REMARK   3      S31:   0.0196 S32:  -0.0923 S33:  -0.0258                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2NZ8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-DEC-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB040486.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-OCT-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0712                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI (220)            
REMARK 200                                   CRYOGENICALLY COOLED               
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39416                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.52400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.530                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: RESIDUES 1231-1390 OF PDB ENTRY 1NTY AND             
REMARK 200  RESIDUES 1-177 OF PDB ENTRY 1FOE                                    
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CACODYLATE PH 5.5 TO       
REMARK 280  6.5, 14 TO 18% (W/V) PEG 8000, AND 300-500 MM CALCIUM ACETATE,      
REMARK 280  PH 6.0, VAPOR DIFFUSION, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       48.74600            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.27900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       48.74600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.27900            
REMARK 290   SMTRY3   4  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 300 REMARK: THERE IS ONE BIOLOGICAL UNIT IN EACH ASSYMETRIC UNIT         
REMARK 300 (COMPLEX BETWEEN RAC1 AND TRIO DH/PH)                                
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: 2590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A2175  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B2221  LIES ON A SPECIAL POSITION.                          
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 B  1223                                                      
REMARK 465     ALA B  1224                                                      
REMARK 465     MET B  1225                                                      
REMARK 465     GLU B  1226                                                      
REMARK 465     LYS B  1227                                                      
REMARK 465     ARG B  1228                                                      
REMARK 465     LYS B  1229                                                      
REMARK 465     SER B  1230                                                      
REMARK 465     ASP B  1418                                                      
REMARK 465     GLU B  1419                                                      
REMARK 465     ASN B  1420                                                      
REMARK 465     ILE B  1421                                                      
REMARK 465     GLU B  1422                                                      
REMARK 465     VAL B  1435                                                      
REMARK 465     TRP B  1436                                                      
REMARK 465     ASP B  1437                                                      
REMARK 465     PRO B  1438                                                      
REMARK 465     LYS B  1439                                                      
REMARK 465     THR B  1440                                                      
REMARK 465     LEU B  1441                                                      
REMARK 465     ILE B  1442                                                      
REMARK 465     ARG B  1443                                                      
REMARK 465     LYS B  1444                                                      
REMARK 465     GLY B  1445                                                      
REMARK 465     ARG B  1446                                                      
REMARK 465     GLU B  1447                                                      
REMARK 465     ARG B  1448                                                      
REMARK 465     LEU B  1498                                                      
REMARK 465     TRP B  1499                                                      
REMARK 465     VAL B  1500                                                      
REMARK 465     GLY B  1501                                                      
REMARK 465     ARG B  1502                                                      
REMARK 465     THR B  1503                                                      
REMARK 465     PRO B  1504                                                      
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   NH2  ARG A    68     O    HOH A  2133              2.04            
REMARK 500   OD2  ASP A    38     O    HOH A  2199              2.06            
REMARK 500   OD1  ASP B  1251     O    HOH B  2156              2.13            
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    GLN B1434   C     GLN B1434   O       0.132                       
REMARK 500    GLU B1482   CD    GLU B1482   OE1     0.144                       
REMARK 500    GLU B1482   CD    GLU B1482   OE2     0.144                       
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    PRO A  29       94.05    -66.72                                   
REMARK 500    LYS A  96      -58.66   -127.02                                   
REMARK 500    THR B1258      -80.44   -111.94                                   
REMARK 500    ASN B1284       35.50    -96.34                                   
REMARK 500    GLU B1390       -0.18     82.84                                   
REMARK 500    SER B1481      -69.90   -164.21                                   
REMARK 500    VAL B1489     -107.31   -117.93                                   
REMARK 500    PRO B1493      172.81    -56.48                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2NZ8 A    1   177  UNP    P63000   RAC1_HUMAN       1    177             
DBREF  2NZ8 B 1226  1535  UNP    O75962   TRIO_HUMAN    1226   1535             
SEQADV 2NZ8 GLY B 1223  UNP  O75962              CLONING ARTIFACT               
SEQADV 2NZ8 ALA B 1224  UNP  O75962              CLONING ARTIFACT               
SEQADV 2NZ8 MET B 1225  UNP  O75962              INITIATING METHIONINE          
SEQRES   1 A  177  MET GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA          
SEQRES   2 A  177  VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN          
SEQRES   3 A  177  ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN          
SEQRES   4 A  177  TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN          
SEQRES   5 A  177  LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP          
SEQRES   6 A  177  ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE          
SEQRES   7 A  177  LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU          
SEQRES   8 A  177  ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS          
SEQRES   9 A  177  CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU          
SEQRES  10 A  177  ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS          
SEQRES  11 A  177  GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU          
SEQRES  12 A  177  ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU          
SEQRES  13 A  177  CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE          
SEQRES  14 A  177  ASP GLU ALA ILE ARG ALA VAL LEU                              
SEQRES   1 B  313  GLY ALA MET GLU LYS ARG LYS SER ALA ARG ARG LYS GLU          
SEQRES   2 B  313  PHE ILE MET ALA GLU LEU ILE GLN THR GLU LYS ALA TYR          
SEQRES   3 B  313  VAL ARG ASP LEU ARG GLU CYS MET ASP THR TYR LEU TRP          
SEQRES   4 B  313  GLU MET THR SER GLY VAL GLU GLU ILE PRO PRO GLY ILE          
SEQRES   5 B  313  VAL ASN LYS GLU LEU ILE ILE PHE GLY ASN MET GLN GLU          
SEQRES   6 B  313  ILE TYR GLU PHE HIS ASN ASN ILE PHE LEU LYS GLU LEU          
SEQRES   7 B  313  GLU LYS TYR GLU GLN LEU PRO GLU ASP VAL GLY HIS CYS          
SEQRES   8 B  313  PHE VAL THR TRP ALA ASP LYS PHE GLN MET TYR VAL THR          
SEQRES   9 B  313  TYR CYS LYS ASN LYS PRO ASP SER THR GLN LEU ILE LEU          
SEQRES  10 B  313  GLU HIS ALA GLY SER TYR PHE ASP GLU ILE GLN GLN ARG          
SEQRES  11 B  313  HIS GLY LEU ALA ASN SER ILE SER SER TYR LEU ILE LYS          
SEQRES  12 B  313  PRO VAL GLN ARG ILE THR LYS TYR GLN LEU LEU LEU LYS          
SEQRES  13 B  313  GLU LEU LEU THR CYS CYS GLU GLU GLY LYS GLY GLU ILE          
SEQRES  14 B  313  LYS ASP GLY LEU GLU VAL MET LEU SER VAL PRO LYS ARG          
SEQRES  15 B  313  ALA ASN ASP ALA MET HIS LEU SER MET LEU GLU GLY PHE          
SEQRES  16 B  313  ASP GLU ASN ILE GLU SER GLN GLY GLU LEU ILE LEU GLN          
SEQRES  17 B  313  GLU SER PHE GLN VAL TRP ASP PRO LYS THR LEU ILE ARG          
SEQRES  18 B  313  LYS GLY ARG GLU ARG HIS LEU PHE LEU PHE GLU MET SER          
SEQRES  19 B  313  LEU VAL PHE SER LYS GLU VAL LYS ASP SER SER GLY ARG          
SEQRES  20 B  313  SER LYS TYR LEU TYR LYS SER LYS LEU PHE THR SER GLU          
SEQRES  21 B  313  LEU GLY VAL THR GLU HIS VAL GLU GLY ASP PRO CYS LYS          
SEQRES  22 B  313  PHE ALA LEU TRP VAL GLY ARG THR PRO THR SER ASP ASN          
SEQRES  23 B  313  LYS ILE VAL LEU LYS ALA SER SER ILE GLU ASN LYS GLN          
SEQRES  24 B  313  ASP TRP ILE LYS HIS ILE ARG GLU VAL ILE GLN GLU ARG          
SEQRES  25 B  313  THR                                                          
FORMUL   3  HOH   *242(H2 O)                                                    
HELIX    1   1 GLY A   12  VAL A   14  5                                   3    
HELIX    2   2 GLY A   15  THR A   25  1                                  11    
HELIX    3   3 LEU A   67  TYR A   72  5                                   6    
HELIX    4   4 SER A   86  LYS A   96  1                                  11    
HELIX    5   5 LYS A   96  CYS A  105  1                                  10    
HELIX    6   6 LYS A  116  ARG A  120  5                                   5    
HELIX    7   7 ASP A  122  GLU A  131  1                                  10    
HELIX    8   8 THR A  138  GLY A  150  1                                  13    
HELIX    9   9 GLY A  164  LEU A  177  1                                  14    
HELIX   10  10 ALA B 1231  THR B 1258  1                                  28    
HELIX   11  11 THR B 1258  GLY B 1266  1                                   9    
HELIX   12  12 LYS B 1277  GLY B 1283  1                                   7    
HELIX   13  13 ASN B 1284  ILE B 1295  1                                  12    
HELIX   14  14 ILE B 1295  TYR B 1303  1                                   9    
HELIX   15  15 LEU B 1306  ASP B 1309  5                                   4    
HELIX   16  16 VAL B 1310  TRP B 1317  1                                   8    
HELIX   17  17 ALA B 1318  PHE B 1321  5                                   4    
HELIX   18  18 GLN B 1322  ALA B 1342  1                                  21    
HELIX   19  19 SER B 1344  GLY B 1354  1                                  11    
HELIX   20  20 SER B 1358  CYS B 1383  1                                  26    
HELIX   21  21 GLU B 1390  SER B 1412  1                                  23    
HELIX   22  22 SER B 1516  GLU B 1533  1                                  18    
SHEET    1   A 6 TYR A  40  VAL A  46  0                                        
SHEET    2   A 6 LYS A  49  TRP A  56 -1  O  VAL A  51   N  VAL A  44           
SHEET    3   A 6 ALA A   3  GLY A  10  1  N  ILE A   4   O  ASN A  52           
SHEET    4   A 6 VAL A  77  SER A  83  1  O  LEU A  79   N  VAL A   9           
SHEET    5   A 6 ILE A 110  THR A 115  1  O  THR A 115   N  PHE A  82           
SHEET    6   A 6 LYS A 153  GLU A 156  1  O  LEU A 155   N  GLY A 114           
SHEET    1   B 5 LEU B1414  GLU B1415  0                                        
SHEET    2   B 5 SER B1470  LEU B1478  1  O  TYR B1472   N  GLU B1415           
SHEET    3   B 5 LEU B1457  LYS B1464 -1  N  LYS B1461   O  LEU B1473           
SHEET    4   B 5 LEU B1450  PHE B1453 -1  N  PHE B1451   O  VAL B1458           
SHEET    5   B 5 LEU B1427  GLU B1431 -1  N  GLU B1431   O  LEU B1450           
SHEET    1   C 2 LYS B1495  PHE B1496  0                                        
SHEET    2   C 2 LEU B1512  LYS B1513 -1  O  LEU B1512   N  PHE B1496           
CISPEP   1 SER B 1423    GLN B 1424          0         0.68                     
CRYST1   97.492  108.558   53.416  90.00  90.00  90.00 P 21 21 2     4          
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      0.010257  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009212  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018721        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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