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Database: PDB
Entry: 3SBD
LinkDB: 3SBD
Original site: 3SBD 
HEADER    HYDROLASE                               03-JUN-11   3SBD              
TITLE     CRYSTAL STRUCTURE OF RAC1 P29S MUTANT                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1;                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: CELL MIGRATION-INDUCING GENE 5 PROTEIN, RAS-LIKE PROTEIN    
COMPND   5 TC25, P21-RAC1;                                                      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: 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, TC25, MIG5;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: MODIFIED PET-28                       
KEYWDS    ROSSMANN FOLD, GTPASE, GTP BINDING, HYDROLASE                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.H.HA,T.J.BOGGON                                                     
REVDAT   4   12-DEC-12 3SBD    1       REMARK                                   
REVDAT   3   19-SEP-12 3SBD    1       JRNL                                     
REVDAT   2   29-AUG-12 3SBD    1       JRNL                                     
REVDAT   1   18-JUL-12 3SBD    0                                                
JRNL        AUTH   M.KRAUTHAMMER,Y.KONG,B.H.HA,P.EVANS,A.BACCHIOCCHI,           
JRNL        AUTH 2 J.P.MCCUSKER,E.CHENG,M.J.DAVIS,G.GOH,M.CHOI,S.ARIYAN,        
JRNL        AUTH 3 D.NARAYAN,K.DUTTON-REGESTER,A.CAPATANA,E.C.HOLMAN,           
JRNL        AUTH 4 M.BOSENBERG,M.SZNOL,H.M.KLUGER,D.E.BRASH,D.F.STERN,          
JRNL        AUTH 5 M.A.MATERIN,R.S.LO,S.MANE,S.MA,K.K.KIDD,N.K.HAYWARD,         
JRNL        AUTH 6 R.P.LIFTON,J.SCHLESSINGER,T.J.BOGGON,R.HALABAN               
JRNL        TITL   EXOME SEQUENCING IDENTIFIES RECURRENT SOMATIC RAC1 MUTATIONS 
JRNL        TITL 2 IN MELANOMA.                                                 
JRNL        REF    NAT.GENET.                    V.  44  1006 2012              
JRNL        REFN                   ISSN 1061-4036                               
JRNL        PMID   22842228                                                     
JRNL        DOI    10.1038/NG.2359                                              
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.68                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 21265                          
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) : 0.240                           
REMARK   3   R VALUE            (WORKING SET) : 0.238                           
REMARK   3   FREE R VALUE                     : 0.285                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1158                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1295                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 83.78                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2910                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 63                           
REMARK   3   BIN FREE R VALUE                    : 0.3930                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2752                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 66                                      
REMARK   3   SOLVENT ATOMS            : 146                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.61                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.50000                                             
REMARK   3    B22 (A**2) : 0.78000                                              
REMARK   3    B33 (A**2) : -0.28000                                             
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.230         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.174         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.584        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2918 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3990 ; 1.576 ; 2.003       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   359 ; 5.699 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   117 ;38.500 ;24.359       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   486 ;15.808 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;19.300 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   456 ; 0.091 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2158 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  1784 ; 0.581 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2905 ; 1.063 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1134 ; 1.738 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1085 ; 2.671 ; 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      2       A     177      4                      
REMARK   3           1     B      2       B     177      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1370 ;  0.44 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1370 ;  0.61 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A    76                          
REMARK   3    RESIDUE RANGE :   A    77        A   177                          
REMARK   3    RESIDUE RANGE :   B     2        B    76                          
REMARK   3    RESIDUE RANGE :   B    77        B   177                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.2460  64.3560  23.7440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1617 T22:   0.0114                                     
REMARK   3      T33:   0.1530 T12:  -0.0011                                     
REMARK   3      T13:   0.0169 T23:  -0.0003                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5830 L22:   0.0137                                     
REMARK   3      L33:   1.2097 L12:   0.0042                                     
REMARK   3      L13:   0.8321 L23:   0.0624                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0194 S12:   0.0128 S13:   0.0270                       
REMARK   3      S21:   0.0114 S22:  -0.0005 S23:   0.0037                       
REMARK   3      S31:  -0.0217 S32:   0.0061 S33:   0.0199                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3SBD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB065996.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-MAY-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
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 MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944+                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23040                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.12900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.17                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.64700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
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: PDB ENTRY 1MH1                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG4000, 7% ISOPROPANOL, 0.1M        
REMARK 280  HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       25.13300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       47.45500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.01050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       47.45500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.13300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.01050            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     MET A    -6                                                      
REMARK 465     GLU A    -5                                                      
REMARK 465     ASN A    -4                                                      
REMARK 465     LEU A    -3                                                      
REMARK 465     TYR A    -2                                                      
REMARK 465     PHE A    -1                                                      
REMARK 465     GLN A     0                                                      
REMARK 465     GLY B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     HIS B    -7                                                      
REMARK 465     MET B    -6                                                      
REMARK 465     GLU B    -5                                                      
REMARK 465     ASN B    -4                                                      
REMARK 465     LEU B    -3                                                      
REMARK 465     TYR B    -2                                                      
REMARK 465     PHE B    -1                                                      
REMARK 465     GLN B     0                                                      
REMARK 465     GLY B     1                                                      
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   120     OE2  GLU A   156              2.07            
REMARK 500   O    GLU A    31     O    HOH A   235              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 102   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A 102   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG A 120   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG B 120   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A  74       -0.62     74.87                                   
REMARK 500    LYS A  96      -52.76   -130.91                                   
REMARK 500    PHE B  37      133.83   -172.18                                   
REMARK 500    GLN B  74       14.34     53.88                                   
REMARK 500    LYS B  96      -54.15   -128.21                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 202        DISTANCE =  5.87 ANGSTROMS                       
REMARK 525    HOH B 247        DISTANCE =  5.85 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 503  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GNP B 502   O3G                                                    
REMARK 620 2 GNP B 502   O2B 102.7                                              
REMARK 620 3 THR B  35   OG1  93.1 164.0                                        
REMARK 620 4 THR B  17   OG1 168.5  88.6  75.8                                  
REMARK 620 5 HOH B 235   O    96.5  95.1  85.7  80.1                            
REMARK 620 6 HOH B 236   O    95.7  86.4  89.3  87.1 167.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 501  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GNP A 500   O2G                                                    
REMARK 620 2 GNP A 500   O2B  99.3                                              
REMARK 620 3 THR A  35   OG1  93.1 167.5                                        
REMARK 620 4 THR A  17   OG1 170.0  90.2  77.3                                  
REMARK 620 5 HOH A 233   O    89.0  89.5  89.4  87.9                            
REMARK 620 6 HOH A 234   O   100.8  89.3  89.6  82.2 170.1                      
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 GNP A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 503                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4GZL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4GZM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3SBE   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3TH5   RELATED DB: PDB                                   
DBREF  3SBD A    2   177  UNP    P63000   RAC1_HUMAN       2    177             
DBREF  3SBD B    2   177  UNP    P63000   RAC1_HUMAN       2    177             
SEQADV 3SBD GLY A   -9  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SBD SER A   -8  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SBD HIS A   -7  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SBD MET A   -6  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SBD GLU A   -5  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SBD ASN A   -4  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SBD LEU A   -3  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SBD TYR A   -2  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SBD PHE A   -1  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SBD GLN A    0  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SBD GLY A    1  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SBD SER A   29  UNP  P63000    PRO    29 ENGINEERED MUTATION            
SEQADV 3SBD GLY B   -9  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SBD SER B   -8  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SBD HIS B   -7  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SBD MET B   -6  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SBD GLU B   -5  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SBD ASN B   -4  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SBD LEU B   -3  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SBD TYR B   -2  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SBD PHE B   -1  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SBD GLN B    0  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SBD GLY B    1  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SBD SER B   29  UNP  P63000    PRO    29 ENGINEERED MUTATION            
SEQRES   1 A  187  GLY SER HIS MET GLU ASN LEU TYR PHE GLN GLY GLN ALA          
SEQRES   2 A  187  ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA VAL GLY LYS          
SEQRES   3 A  187  THR CYS LEU LEU ILE SER TYR THR THR ASN ALA PHE SER          
SEQRES   4 A  187  GLY GLU TYR ILE PRO THR VAL PHE ASP ASN TYR SER ALA          
SEQRES   5 A  187  ASN VAL MET VAL ASP GLY LYS PRO VAL ASN LEU GLY LEU          
SEQRES   6 A  187  TRP ASP THR ALA GLY GLN GLU ASP TYR ASP ARG LEU ARG          
SEQRES   7 A  187  PRO LEU SER TYR PRO GLN THR ASP VAL PHE LEU ILE CYS          
SEQRES   8 A  187  PHE SER LEU VAL SER PRO ALA SER PHE GLU ASN VAL ARG          
SEQRES   9 A  187  ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS CYS PRO ASN          
SEQRES  10 A  187  THR PRO ILE ILE LEU VAL GLY THR LYS LEU ASP LEU ARG          
SEQRES  11 A  187  ASP ASP LYS ASP THR ILE GLU LYS LEU LYS GLU LYS LYS          
SEQRES  12 A  187  LEU THR PRO ILE THR TYR PRO GLN GLY LEU ALA MET ALA          
SEQRES  13 A  187  LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU CYS SER ALA          
SEQRES  14 A  187  LEU THR GLN ARG GLY LEU LYS THR VAL PHE ASP GLU ALA          
SEQRES  15 A  187  ILE ARG ALA VAL LEU                                          
SEQRES   1 B  187  GLY SER HIS MET GLU ASN LEU TYR PHE GLN GLY GLN ALA          
SEQRES   2 B  187  ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA VAL GLY LYS          
SEQRES   3 B  187  THR CYS LEU LEU ILE SER TYR THR THR ASN ALA PHE SER          
SEQRES   4 B  187  GLY GLU TYR ILE PRO THR VAL PHE ASP ASN TYR SER ALA          
SEQRES   5 B  187  ASN VAL MET VAL ASP GLY LYS PRO VAL ASN LEU GLY LEU          
SEQRES   6 B  187  TRP ASP THR ALA GLY GLN GLU ASP TYR ASP ARG LEU ARG          
SEQRES   7 B  187  PRO LEU SER TYR PRO GLN THR ASP VAL PHE LEU ILE CYS          
SEQRES   8 B  187  PHE SER LEU VAL SER PRO ALA SER PHE GLU ASN VAL ARG          
SEQRES   9 B  187  ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS CYS PRO ASN          
SEQRES  10 B  187  THR PRO ILE ILE LEU VAL GLY THR LYS LEU ASP LEU ARG          
SEQRES  11 B  187  ASP ASP LYS ASP THR ILE GLU LYS LEU LYS GLU LYS LYS          
SEQRES  12 B  187  LEU THR PRO ILE THR TYR PRO GLN GLY LEU ALA MET ALA          
SEQRES  13 B  187  LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU CYS SER ALA          
SEQRES  14 B  187  LEU THR GLN ARG GLY LEU LYS THR VAL PHE ASP GLU ALA          
SEQRES  15 B  187  ILE ARG ALA VAL LEU                                          
HET    GNP  A 500      32                                                       
HET     MG  A 501       1                                                       
HET    GNP  B 502      32                                                       
HET     MG  B 503       1                                                       
HETNAM     GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER                      
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   3  GNP    2(C10 H17 N6 O13 P3)                                         
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   7  HOH   *146(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  ASP A  121  1                                   6    
HELIX    7   7 ASP A  122  GLU A  131  1                                  10    
HELIX    8   8 THR A  138  ILE A  149  1                                  12    
HELIX    9   9 GLY A  164  ALA A  175  1                                  12    
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  ALA B  175  1                                  12    
SHEET    1   A 6 PHE A  37  VAL A  46  0                                        
SHEET    2   A 6 LYS A  49  THR A  58 -1  O  VAL A  51   N  VAL A  44           
SHEET    3   A 6 GLN A   2  GLY A  10  1  N  ILE A   4   O  GLY A  54           
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 PHE B  37  VAL B  46  0                                        
SHEET    2   B 6 LYS B  49  THR B  58 -1  O  LEU B  55   N  TYR B  40           
SHEET    3   B 6 ALA B   3  GLY B  10  1  N  CYS B   6   O  TRP B  56           
SHEET    4   B 6 VAL B  77  SER B  83  1  O  LEU B  79   N  VAL B   7           
SHEET    5   B 6 ILE B 110  THR B 115  1  O  THR B 115   N  PHE B  82           
SHEET    6   B 6 LYS B 153  GLU B 156  1  O  LEU B 155   N  LEU B 112           
LINK         O3G GNP B 502                MG    MG B 503     1555   1555  1.87  
LINK         O2G GNP A 500                MG    MG A 501     1555   1555  1.89  
LINK         O2B GNP A 500                MG    MG A 501     1555   1555  2.05  
LINK         O2B GNP B 502                MG    MG B 503     1555   1555  2.05  
LINK         OG1 THR B  35                MG    MG B 503     1555   1555  2.12  
LINK         OG1 THR A  35                MG    MG A 501     1555   1555  2.14  
LINK         OG1 THR A  17                MG    MG A 501     1555   1555  2.15  
LINK         OG1 THR B  17                MG    MG B 503     1555   1555  2.18  
LINK        MG    MG B 503                 O   HOH B 235     1555   1555  2.05  
LINK        MG    MG A 501                 O   HOH A 233     1555   1555  2.07  
LINK        MG    MG A 501                 O   HOH A 234     1555   1555  2.09  
LINK        MG    MG B 503                 O   HOH B 236     1555   1555  2.20  
SITE     1 AC1 26 GLY A  12  ALA A  13  VAL A  14  GLY A  15                    
SITE     2 AC1 26 LYS A  16  THR A  17  CYS A  18  PHE A  28                    
SITE     3 AC1 26 SER A  29  GLY A  30  TYR A  32  THR A  35                    
SITE     4 AC1 26 GLY A  60  LYS A 116  ASP A 118  LEU A 119                    
SITE     5 AC1 26 SER A 158  ALA A 159  LEU A 160  HOH A 187                    
SITE     6 AC1 26 HOH A 203  HOH A 233  HOH A 234  HOH A 237                    
SITE     7 AC1 26  MG A 501  LYS B  49                                          
SITE     1 AC2  5 THR A  17  THR A  35  HOH A 233  HOH A 234                    
SITE     2 AC2  5 GNP A 500                                                     
SITE     1 AC3 25 GLY B  12  ALA B  13  VAL B  14  GLY B  15                    
SITE     2 AC3 25 LYS B  16  THR B  17  CYS B  18  PHE B  28                    
SITE     3 AC3 25 SER B  29  GLY B  30  TYR B  32  THR B  35                    
SITE     4 AC3 25 GLY B  60  LYS B 116  ASP B 118  LEU B 119                    
SITE     5 AC3 25 SER B 158  ALA B 159  LEU B 160  HOH B 184                    
SITE     6 AC3 25 HOH B 191  HOH B 201  HOH B 235  HOH B 236                    
SITE     7 AC3 25  MG B 503                                                     
SITE     1 AC4  5 THR B  17  THR B  35  HOH B 235  HOH B 236                    
SITE     2 AC4  5 GNP B 502                                                     
CRYST1   50.266   80.021   94.910  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      0.019894  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012497  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010536        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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