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Database: PDB
Entry: 2G0N
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HEADER    SIGNALING PROTEIN                       13-FEB-06   2G0N              
TITLE     THE CRYSTAL STRUCTURE OF THE HUMAN RAC3 IN COMPLEX WITH GDP AND       
TITLE    2 CHLORIDE                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 3;                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RAC3;                                                      
COMPND   5 SYNONYM: P21-RAC3;                                                   
COMPND   6 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: RAC3;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3)-R3;                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    GTPASE RAC3A, SMALL GTP BINDING PROTEIN, P21 RAC, RAS-RELATED C3      
KEYWDS   2 BOTULINUM TOXIN SUBSTRATE 3, SIGNALLING PROTEIN, STRUCTURAL          
KEYWDS   3 GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, SIGNALING PROTEIN     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.UGOCHUKWU,X.YANG,Y.ZAO,J.ELKINS,C.GILEADI,N.BURGESS,S.COLEBROOK,    
AUTHOR   2 O.GILEADI,O.FEDOROV,G.BUNKOCZI,M.SUNDSTROM,C.ARROWSMITH,J.WEIGELT,   
AUTHOR   3 A.EDWARDS,F.VON DELFT,D.DOYLE,STRUCTURAL GENOMICS CONSORTIUM (SGC)   
REVDAT   3   13-JUL-11 2G0N    1       VERSN                                    
REVDAT   2   24-FEB-09 2G0N    1       VERSN                                    
REVDAT   1   30-MAY-06 2G0N    0                                                
JRNL        AUTH   E.UGOCHUKWU,X.YANG,Y.ZAO,J.ELKINS,C.GILEADI,N.BURGESS,       
JRNL        AUTH 2 S.COLEBROOK,O.GILEADI,O.FEDOROV,G.BUNKOCZI,M.SUNDSTROM,      
JRNL        AUTH 3 C.ARROWSMITH,J.WEIGELT,A.EDWARDS,F.VON DELFT,D.DOYLE         
JRNL        TITL   THE CRYSTAL STRUCTURE OF THE HUMAN RAC3 IN COMPLEX WITH GDP  
JRNL        TITL 2 AND CHLORIDE                                                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.43                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 28345                          
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) : 0.168                           
REMARK   3   R VALUE            (WORKING SET) : 0.165                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1515                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2064                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 115                          
REMARK   3   BIN FREE R VALUE                    : 0.3160                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2739                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 61                                      
REMARK   3   SOLVENT ATOMS            : 276                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.43                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.44000                                             
REMARK   3    B22 (A**2) : 1.38000                                              
REMARK   3    B33 (A**2) : -0.94000                                             
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): 0.141         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.141         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.104         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.526         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.938                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2888 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1907 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3959 ; 1.353 ; 2.001       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4667 ; 0.930 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   365 ; 5.682 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   115 ;33.827 ;23.565       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   456 ;12.813 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    19 ;18.197 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   459 ; 0.079 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3185 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   574 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   561 ; 0.204 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2022 ; 0.200 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1413 ; 0.177 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1409 ; 0.085 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   216 ; 0.171 ; 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):    12 ; 0.139 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    49 ; 0.195 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    21 ; 0.168 ; 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):  1944 ; 3.141 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   719 ; 0.880 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2923 ; 4.033 ; 5.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1218 ; 6.534 ; 7.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1031 ; 8.468 ;11.000       
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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 4                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      2       A      28      2                      
REMARK   3           1     B      2       B      28      2                      
REMARK   3           2     A     29       A      32      6                      
REMARK   3           2     B     29       B      32      6                      
REMARK   3           3     A     33       A      39      2                      
REMARK   3           3     B     33       B      39      2                      
REMARK   3           4     A     40       A      51      6                      
REMARK   3           4     B     40       B      51      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    200 ;  0.05 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    197 ;  0.39 ;  0.50           
REMARK   3   LOOSE POSITIONAL   1    A    (A):    160 ;  0.75 ;  5.00           
REMARK   3   TIGHT THERMAL      1    A (A**2):    200 ;  0.17 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    197 ;  1.09 ;  2.00           
REMARK   3   LOOSE THERMAL      1    A (A**2):    160 ;  3.12 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A   177                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.0450  14.7602  -7.3973              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1569 T22:  -0.1512                                     
REMARK   3      T33:  -0.1109 T12:   0.0055                                     
REMARK   3      T13:   0.0116 T23:  -0.0013                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1450 L22:   1.3485                                     
REMARK   3      L33:   1.5857 L12:   0.1470                                     
REMARK   3      L13:  -0.0309 L23:  -0.0007                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0066 S12:   0.0485 S13:   0.0505                       
REMARK   3      S21:  -0.0276 S22:   0.0185 S23:   0.0571                       
REMARK   3      S31:   0.0526 S32:   0.0541 S33:  -0.0119                       
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     2        B   177                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.2087 -13.8694 -12.6975              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0626 T22:  -0.1359                                     
REMARK   3      T33:  -0.1309 T12:   0.0328                                     
REMARK   3      T13:  -0.0086 T23:   0.0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7659 L22:   1.4889                                     
REMARK   3      L33:   2.0902 L12:   0.0327                                     
REMARK   3      L13:  -0.0157 L23:   0.8417                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0367 S12:  -0.1306 S13:  -0.0011                       
REMARK   3      S21:   0.1923 S22:   0.0191 S23:   0.0290                       
REMARK   3      S31:   0.3447 S32:   0.1576 S33:  -0.0558                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2G0N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-FEB-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB036539.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-OCT-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E                        
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54180                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS HTC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29868                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 22.430                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1MH1                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, 25% PEG 3350, PH 5.5,    
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       26.96600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.28150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.42050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       42.28150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.96600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.42050            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER B     0                                                      
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     TYR A  32    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP A  38    CG   OD1  OD2                                       
REMARK 470     LYS A  49    CD   CE   NZ                                        
REMARK 470     GLU A 127    CD   OE1  OE2                                       
REMARK 470     ARG A 130    CZ   NH1  NH2                                       
REMARK 470     LYS A 132    CD   CE   NZ                                        
REMARK 470     LYS A 133    CD   CE   NZ                                        
REMARK 470     LYS A 166    CD   CE   NZ                                        
REMARK 470     GLU B  31    CD   OE1  OE2                                       
REMARK 470     TYR B  32    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP B  47    CG   OD1  OD2                                       
REMARK 470     LYS B  49    CG   CD   CE   NZ                                   
REMARK 470     GLN B  74    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 123    NZ                                                  
REMARK 470     LYS B 132    CD   CE   NZ                                        
REMARK 470     LYS B 133    CE   NZ                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B   767     O    HOH B   827              1.75            
REMARK 500   O    HOH B   717     O    HOH B   819              1.92            
REMARK 500   O    HOH B   716     O    HOH B   819              2.08            
REMARK 500   O    HOH A   711     O    HOH A   835              2.12            
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    GLU A  31       58.55    -99.94                                   
REMARK 500    TYR A  32       93.99   -171.22                                   
REMARK 500    LYS A  96      -57.55   -125.42                                   
REMARK 500    LYS B  96      -54.89   -127.98                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 SER A    0     MET A    1                  144.93                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 602  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GDP A 501   O1B                                                    
REMARK 620 2 HOH A 748   O   168.0                                              
REMARK 620 3 HOH A 844   O    87.0  91.0                                        
REMARK 620 4 HOH A 847   O    86.6  81.7  94.2                                  
REMARK 620 5 THR A  17   OG1  94.7  88.3 175.4  90.2                            
REMARK 620 6 HOH A 788   O    90.0 101.8  87.1 176.3  88.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 737   O                                                      
REMARK 620 2 HOH B 742   O    97.1                                              
REMARK 620 3 HOH B 815   O    89.6  89.0                                        
REMARK 620 4 HOH B 818   O    84.1 178.7  90.8                                  
REMARK 620 5 GDP B 502   O1B 171.2  87.9  97.7  90.8                            
REMARK 620 6 THR B  17   OG1  83.0  88.7 171.9  91.6  90.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 502                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MH1   RELATED DB: PDB                                   
REMARK 900 SMALL G-PROTEIN                                                      
DBREF  2G0N A    1   177  UNP    P60763   RAC3_HUMAN       1    177             
DBREF  2G0N B    1   177  UNP    P60763   RAC3_HUMAN       1    177             
SEQADV 2G0N SER A    0  UNP  P60763              CLONING ARTIFACT               
SEQADV 2G0N GLY A  178  UNP  P60763              CLONING ARTIFACT               
SEQADV 2G0N SER B    0  UNP  P60763              CLONING ARTIFACT               
SEQADV 2G0N GLY B  178  UNP  P60763              CLONING ARTIFACT               
SEQRES   1 A  179  SER MET GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY          
SEQRES   2 A  179  ALA VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR          
SEQRES   3 A  179  ASN ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP          
SEQRES   4 A  179  ASN TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL          
SEQRES   5 A  179  ASN LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR          
SEQRES   6 A  179  ASP ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL          
SEQRES   7 A  179  PHE LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE          
SEQRES   8 A  179  GLU ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS          
SEQRES   9 A  179  HIS CYS PRO HIS THR PRO ILE LEU LEU VAL GLY THR LYS          
SEQRES  10 A  179  LEU ASP LEU ARG ASP ASP LYS ASP THR ILE GLU ARG LEU          
SEQRES  11 A  179  ARG ASP LYS LYS LEU ALA PRO ILE THR TYR PRO GLN GLY          
SEQRES  12 A  179  LEU ALA MET ALA ARG GLU ILE GLY SER VAL LYS TYR LEU          
SEQRES  13 A  179  GLU CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL          
SEQRES  14 A  179  PHE ASP GLU ALA ILE ARG ALA VAL LEU GLY                      
SEQRES   1 B  179  SER MET GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY          
SEQRES   2 B  179  ALA VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR          
SEQRES   3 B  179  ASN ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP          
SEQRES   4 B  179  ASN TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL          
SEQRES   5 B  179  ASN LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR          
SEQRES   6 B  179  ASP ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL          
SEQRES   7 B  179  PHE LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE          
SEQRES   8 B  179  GLU ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS          
SEQRES   9 B  179  HIS CYS PRO HIS THR PRO ILE LEU LEU VAL GLY THR LYS          
SEQRES  10 B  179  LEU ASP LEU ARG ASP ASP LYS ASP THR ILE GLU ARG LEU          
SEQRES  11 B  179  ARG ASP LYS LYS LEU ALA PRO ILE THR TYR PRO GLN GLY          
SEQRES  12 B  179  LEU ALA MET ALA ARG GLU ILE GLY SER VAL LYS TYR LEU          
SEQRES  13 B  179  GLU CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL          
SEQRES  14 B  179  PHE ASP GLU ALA ILE ARG ALA VAL LEU GLY                      
HET     MG  B 601       1                                                       
HET     MG  A 602       1                                                       
HET     CL  B 701       1                                                       
HET     CL  A 702       1                                                       
HET     CL  A 703       1                                                       
HET    GDP  A 501      28                                                       
HET    GDP  B 502      28                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   5   CL    3(CL 1-)                                                     
FORMUL   8  GDP    2(C10 H15 N5 O11 P2)                                         
FORMUL  10  HOH   *276(H2 O)                                                    
HELIX    1   1 GLY A   15  ASN A   26  1                                  12    
HELIX    2   2 GLN A   61  ASP A   65  5                                   5    
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  ASP A  131  1                                  10    
HELIX    8   8 THR A  138  ILE A  149  1                                  12    
HELIX    9   9 GLY A  164  GLY A  178  1                                  15    
HELIX   10  10 GLY B   15  ASN B   26  1                                  12    
HELIX   11  11 GLN B   61  ASP B   65  5                                   5    
HELIX   12  12 LEU B   67  TYR B   72  5                                   6    
HELIX   13  13 SER B   86  LYS B   96  1                                  11    
HELIX   14  14 LYS B   96  CYS B  105  1                                  10    
HELIX   15  15 LYS B  116  ARG B  120  5                                   5    
HELIX   16  16 ASP B  122  LYS B  132  1                                  11    
HELIX   17  17 THR B  138  ILE B  149  1                                  12    
HELIX   18  18 GLY B  164  GLY B  178  1                                  15    
SHEET    1   A 6 ASN A  39  VAL A  46  0                                        
SHEET    2   A 6 LYS A  49  TRP A  56 -1  O  LEU A  55   N  TYR A  40           
SHEET    3   A 6 GLN A   2  VAL A   9  1  N  GLN A   2   O  ASN A  52           
SHEET    4   A 6 VAL A  77  SER A  83  1  O  CYS A  81   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  LEU A 112           
SHEET    1   B 6 ASN B  39  VAL B  46  0                                        
SHEET    2   B 6 LYS B  49  TRP B  56 -1  O  LYS B  49   N  VAL B  46           
SHEET    3   B 6 GLN B   2  GLY B  10  1  N  CYS B   6   O  GLY B  54           
SHEET    4   B 6 VAL B  77  SER B  83  1  O  CYS B  81   N  VAL B   9           
SHEET    5   B 6 ILE B 110  THR B 115  1  O  VAL B 113   N  ILE B  80           
SHEET    6   B 6 LYS B 153  GLU B 156  1  O  LEU B 155   N  GLY B 114           
LINK        MG    MG A 602                 O1B GDP A 501     1555   1555  2.17  
LINK        MG    MG A 602                 O   HOH A 748     1555   1555  2.21  
LINK        MG    MG A 602                 O   HOH A 844     1555   1555  2.25  
LINK        MG    MG A 602                 O   HOH A 847     1555   1555  2.07  
LINK        MG    MG A 602                 OG1 THR A  17     1555   1555  2.06  
LINK        MG    MG A 602                 O   HOH A 788     1555   1555  2.25  
LINK        MG    MG B 601                 O   HOH B 737     1555   1555  2.33  
LINK        MG    MG B 601                 O   HOH B 742     1555   1555  2.25  
LINK        MG    MG B 601                 O   HOH B 815     1555   1555  2.10  
LINK        MG    MG B 601                 O   HOH B 818     1555   1555  2.11  
LINK        MG    MG B 601                 O1B GDP B 502     1555   1555  2.14  
LINK        MG    MG B 601                 OG1 THR B  17     1555   1555  2.10  
SITE     1 AC1  6 THR B  17  GDP B 502  HOH B 737  HOH B 742                    
SITE     2 AC1  6 HOH B 815  HOH B 818                                          
SITE     1 AC2  6 THR A  17  GDP A 501  HOH A 748  HOH A 788                    
SITE     2 AC2  6 HOH A 844  HOH A 847                                          
SITE     1 AC3  6 GLY B  12  LYS B  16  GLY B  60  GLN B  61                    
SITE     2 AC3  6 GDP B 502  HOH B 815                                          
SITE     1 AC4  6 GLY A  12  LYS A  16  GLY A  60  GLN A  61                    
SITE     2 AC4  6 GDP A 501  HOH A 844                                          
SITE     1 AC5  1 SER A 151                                                     
SITE     1 AC6 23 ALA A  13  VAL A  14  GLY A  15  LYS A  16                    
SITE     2 AC6 23 THR A  17  CYS A  18  PHE A  28  ILE A  33                    
SITE     3 AC6 23 LYS A 116  ASP A 118  LEU A 119  SER A 158                    
SITE     4 AC6 23 ALA A 159  LEU A 160   MG A 602   CL A 702                    
SITE     5 AC6 23 HOH A 718  HOH A 727  HOH A 796  HOH A 798                    
SITE     6 AC6 23 HOH A 844  HOH A 847  TYR B  64                               
SITE     1 AC7 22 TYR A  64  ALA B  13  VAL B  14  GLY B  15                    
SITE     2 AC7 22 LYS B  16  THR B  17  CYS B  18  PHE B  28                    
SITE     3 AC7 22 ILE B  33  LYS B 116  ASP B 118  LEU B 119                    
SITE     4 AC7 22 SER B 158  ALA B 159  LEU B 160   MG B 601                    
SITE     5 AC7 22  CL B 701  HOH B 706  HOH B 724  HOH B 742                    
SITE     6 AC7 22 HOH B 803  HOH B 818                                          
CRYST1   53.932   80.841   84.563  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018542  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012370  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011825        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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