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Database: PDB
Entry: 2H7V
LinkDB: 2H7V
Original site: 2H7V 
HEADER    SIGNALING PROTEIN                       04-JUN-06   2H7V              
TITLE     CO-CRYSTAL STRUCTURE OF YPKA-RAC1                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MIGRATION-INDUCING PROTEIN 5;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1, ISOFORM RAC1;   
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PROTEIN KINASE YPKA;                                       
COMPND   9 CHAIN: C, D;                                                         
COMPND  10 SYNONYM: PROTEIN KINASE A, TARGETED EFFECTOR PROTEIN KINASE;         
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MIG5, RAC1;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX4T3;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: YERSINIA PSEUDOTUBERCULOSIS;                    
SOURCE  13 ORGANISM_TAXID: 633;                                                 
SOURCE  14 GENE: YPKA;                                                          
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PGEX4T3                                   
KEYWDS    YPKA, YOPO, RAC1, GDI, GTPASE, YERSINIA, SIGNALING PROTEIN            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.PREHNA,M.IVANOV,J.B.BLISKA,C.E.STEBBINS                             
REVDAT   3   13-JUL-11 2H7V    1       VERSN                                    
REVDAT   2   24-FEB-09 2H7V    1       VERSN                                    
REVDAT   1   19-SEP-06 2H7V    0                                                
JRNL        AUTH   G.PREHNA,M.I.IVANOV,J.B.BLISKA,C.E.STEBBINS                  
JRNL        TITL   YERSINIA VIRULENCE DEPENDS ON MIMICRY OF HOST RHO-FAMILY     
JRNL        TITL 2 NUCLEOTIDE DISSOCIATION INHIBITORS.                          
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 126   869 2006              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   16959567                                                     
JRNL        DOI    10.1016/J.CELL.2006.06.056                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 95.78                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 51262                          
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) : 0.222                           
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2552                            
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3649                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.50                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3730                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 162                          
REMARK   3   BIN FREE R VALUE                    : 0.4030                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7058                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 75                                      
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) : 62.65                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 7.30000                                              
REMARK   3    B22 (A**2) : 0.97000                                              
REMARK   3    B33 (A**2) : -5.70000                                             
REMARK   3    B12 (A**2) : 4.77000                                              
REMARK   3    B13 (A**2) : -3.29000                                             
REMARK   3    B23 (A**2) : -0.77000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.354         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.261         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.254         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 26.265        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7223 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  6710 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9775 ; 1.666 ; 1.987       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 15624 ; 0.866 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   883 ; 7.039 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   318 ;35.492 ;24.308       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1340 ;19.171 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    53 ;17.951 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1147 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7826 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1367 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1914 ; 0.242 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  7111 ; 0.185 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3697 ; 0.190 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  4635 ; 0.093 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   203 ; 0.196 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     2 ; 0.059 ; 0.200       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     2 ; 0.034 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    21 ; 0.219 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):   109 ; 0.226 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     4 ; 0.140 ; 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):  5686 ; 0.874 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1803 ; 0.136 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7200 ; 1.091 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3128 ; 1.579 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2575 ; 2.504 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   178                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.3250 -13.9150 -34.1240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0837 T22:  -0.3251                                     
REMARK   3      T33:  -0.1239 T12:   0.0965                                     
REMARK   3      T13:  -0.0052 T23:  -0.0404                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6988 L22:   6.4001                                     
REMARK   3      L33:   4.5338 L12:  -2.5200                                     
REMARK   3      L13:   2.4130 L23:  -2.4713                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2353 S12:  -0.0195 S13:   0.3198                       
REMARK   3      S21:  -0.1464 S22:  -0.1275 S23:  -0.5774                       
REMARK   3      S31:  -0.4192 S32:   0.3443 S33:   0.3628                       
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     1        B   179                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.4060 -13.5380 -98.9150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0516 T22:  -0.0891                                     
REMARK   3      T33:  -0.0465 T12:  -0.0576                                     
REMARK   3      T13:  -0.0191 T23:   0.0372                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.0317 L22:   1.3848                                     
REMARK   3      L33:   3.3601 L12:  -1.5120                                     
REMARK   3      L13:   3.2496 L23:  -0.5097                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2300 S12:   0.1122 S13:   0.9175                       
REMARK   3      S21:  -0.0668 S22:  -0.2511 S23:  -0.1441                       
REMARK   3      S31:  -0.7157 S32:   0.0197 S33:   0.4811                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   439        C   514                          
REMARK   3    RESIDUE RANGE :   C   532        C   648                          
REMARK   3    RESIDUE RANGE :   C   657        C   702                          
REMARK   3    RESIDUE RANGE :   C   704        C   732                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.2680 -37.5410 -71.3430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0359 T22:  -0.1176                                     
REMARK   3      T33:  -0.0211 T12:  -0.0392                                     
REMARK   3      T13:  -0.0016 T23:   0.0044                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1446 L22:   1.1338                                     
REMARK   3      L33:   6.6549 L12:   0.4021                                     
REMARK   3      L13:  -0.9244 L23:  -2.6789                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1305 S12:   0.1575 S13:   0.0637                       
REMARK   3      S21:  -0.0424 S22:   0.3416 S23:   0.0289                       
REMARK   3      S31:   0.7001 S32:   0.0917 S33:  -0.2111                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   441        D   486                          
REMARK   3    RESIDUE RANGE :   D   489        D   512                          
REMARK   3    RESIDUE RANGE :   D   533        D   647                          
REMARK   3    RESIDUE RANGE :   D   658        D   732                          
REMARK   3    ORIGIN FOR THE GROUP (A): -25.9680  -4.6970 -56.5220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2540 T22:   0.0845                                     
REMARK   3      T33:   0.0071 T12:   0.0858                                     
REMARK   3      T13:  -0.0901 T23:   0.0405                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5454 L22:   4.1627                                     
REMARK   3      L33:   7.7321 L12:   0.0415                                     
REMARK   3      L13:  -0.0440 L23:   5.6665                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0116 S12:   0.2689 S13:  -0.2143                       
REMARK   3      S21:   0.6369 S22:  -0.3275 S23:   0.2754                       
REMARK   3      S31:   0.7133 S32:  -1.2313 S33:   0.3392                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2H7V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUN-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB038039.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-APR-05; 21-APR-05               
REMARK 200  TEMPERATURE           (KELVIN) : 80; NULL                           
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : NSLS; NSLS                         
REMARK 200  BEAMLINE                       : X29A; X29A                         
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1; 1.1                           
REMARK 200  MONOCHROMATOR                  : SI(111); SI(111)                   
REMARK 200  OPTICS                         : ROSENBAUM-ROCK DOUBLE CRYSTAL      
REMARK 200                                   SAGITTAL FOCUSING MONOCHROMETER    
REMARK 200                                   AND VERTICAL FOCUSING MIRROR;      
REMARK 200                                   ROSENBAUM-ROCK DOUBLE CRYSTAL      
REMARK 200                                   SAGITTAL FOCUSING MONOCHROMETER    
REMARK 200                                   AND VERTICAL FOCUSING MIRROR       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315; ADSC QUANTUM     
REMARK 200                                   315                                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51987                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 95.780                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.67                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.41800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ID 2H7O, 1MH1                                    
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES PH 6.5-7.5, 5%-8%            
REMARK 280  PEGMME2000 MICRO SEEDING, VAPOR DIFFUSION, SITTING DROP,            
REMARK 280  TEMPERATURE 295K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 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 300 REMARK: DIMER CONSISTING OF ONE YPKA MOLECULE AND ONE RAC1           
REMARK 300 MOLECULE. BIOLOGICAL CONTACT IS RESIDUES 574 TO 601 OF YPKA.         
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     PRO A   179                                                      
REMARK 465     PRO A   180                                                      
REMARK 465     PRO A   181                                                      
REMARK 465     VAL A   182                                                      
REMARK 465     LYS A   183                                                      
REMARK 465     LYS A   184                                                      
REMARK 465     PRO B   180                                                      
REMARK 465     PRO B   181                                                      
REMARK 465     VAL B   182                                                      
REMARK 465     LYS B   183                                                      
REMARK 465     LYS B   184                                                      
REMARK 465     GLY C   430                                                      
REMARK 465     PRO C   431                                                      
REMARK 465     VAL C   432                                                      
REMARK 465     ASP C   433                                                      
REMARK 465     SER C   434                                                      
REMARK 465     THR C   435                                                      
REMARK 465     ASP C   436                                                      
REMARK 465     VAL C   437                                                      
REMARK 465     ARG C   438                                                      
REMARK 465     ARG C   515                                                      
REMARK 465     GLU C   516                                                      
REMARK 465     GLY C   517                                                      
REMARK 465     ASP C   518                                                      
REMARK 465     THR C   519                                                      
REMARK 465     LYS C   520                                                      
REMARK 465     ASN C   521                                                      
REMARK 465     SER C   522                                                      
REMARK 465     SER C   523                                                      
REMARK 465     THR C   524                                                      
REMARK 465     GLU C   525                                                      
REMARK 465     VAL C   526                                                      
REMARK 465     SER C   527                                                      
REMARK 465     PRO C   528                                                      
REMARK 465     TYR C   529                                                      
REMARK 465     HIS C   530                                                      
REMARK 465     ARG C   531                                                      
REMARK 465     VAL C   649                                                      
REMARK 465     VAL C   650                                                      
REMARK 465     LYS C   651                                                      
REMARK 465     PHE C   652                                                      
REMARK 465     GLY C   653                                                      
REMARK 465     THR C   654                                                      
REMARK 465     GLU C   655                                                      
REMARK 465     GLN C   656                                                      
REMARK 465     GLY D   430                                                      
REMARK 465     PRO D   431                                                      
REMARK 465     VAL D   432                                                      
REMARK 465     ASP D   433                                                      
REMARK 465     SER D   434                                                      
REMARK 465     THR D   435                                                      
REMARK 465     ASP D   436                                                      
REMARK 465     VAL D   437                                                      
REMARK 465     ARG D   438                                                      
REMARK 465     ARG D   439                                                      
REMARK 465     ILE D   440                                                      
REMARK 465     GLY D   487                                                      
REMARK 465     GLY D   488                                                      
REMARK 465     LYS D   513                                                      
REMARK 465     GLY D   514                                                      
REMARK 465     ARG D   515                                                      
REMARK 465     GLU D   516                                                      
REMARK 465     GLY D   517                                                      
REMARK 465     ASP D   518                                                      
REMARK 465     THR D   519                                                      
REMARK 465     LYS D   520                                                      
REMARK 465     ASN D   521                                                      
REMARK 465     SER D   522                                                      
REMARK 465     SER D   523                                                      
REMARK 465     THR D   524                                                      
REMARK 465     GLU D   525                                                      
REMARK 465     VAL D   526                                                      
REMARK 465     SER D   527                                                      
REMARK 465     PRO D   528                                                      
REMARK 465     TYR D   529                                                      
REMARK 465     HIS D   530                                                      
REMARK 465     ARG D   531                                                      
REMARK 465     SER D   532                                                      
REMARK 465     PRO D   648                                                      
REMARK 465     VAL D   649                                                      
REMARK 465     VAL D   650                                                      
REMARK 465     LYS D   651                                                      
REMARK 465     PHE D   652                                                      
REMARK 465     GLY D   653                                                      
REMARK 465     THR D   654                                                      
REMARK 465     GLU D   655                                                      
REMARK 465     GLN D   656                                                      
REMARK 465     TYR D   657                                                      
REMARK 465     MET D   703                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU C   709     O    HOH C    30              2.16            
REMARK 500   OG1  THR D   658     ND1  HIS D   661              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU B  62   CG    GLU B  62   CD      0.103                       
REMARK 500    CYS B  81   CB    CYS B  81   SG     -0.111                       
REMARK 500    CYS B 105   CB    CYS B 105   SG     -0.109                       
REMARK 500    SER C 629   C     SER C 629   O       0.153                       
REMARK 500    GLY C 630   N     GLY C 630   CA     -0.124                       
REMARK 500    GLU D 728   CB    GLU D 728   CG      0.117                       
REMARK 500    GLU D 728   CG    GLU D 728   CD      0.107                       
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  68   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG A  68   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    LEU B 134   CA  -  CB  -  CG  ANGL. DEV. =  16.2 DEGREES          
REMARK 500    ARG C 628   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 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    TYR A  32      124.08     57.21                                   
REMARK 500    GLN A  61      -81.15    170.16                                   
REMARK 500    GLU A  62      -53.51   -165.05                                   
REMARK 500    LYS A  96      -57.43   -127.66                                   
REMARK 500    LYS A 132       43.90   -142.94                                   
REMARK 500    PRO A 136      154.96    -49.20                                   
REMARK 500    SER B   2B    -147.96    -73.74                                   
REMARK 500    LYS B   1A     113.13     67.05                                   
REMARK 500    ASN B  26       14.56     57.02                                   
REMARK 500    TYR B  32      108.73     50.49                                   
REMARK 500    ALA B  59       -6.80   -147.29                                   
REMARK 500    GLN B  61       64.47   -169.01                                   
REMARK 500    ASP B  63      -40.32    146.84                                   
REMARK 500    SER B  86       78.99   -155.35                                   
REMARK 500    LYS B  96      -53.04   -133.22                                   
REMARK 500    LYS B 133       60.24     28.25                                   
REMARK 500    LEU C 464      117.12    -37.40                                   
REMARK 500    GLU C 486       36.83   -153.89                                   
REMARK 500    GLN C 581       71.13    -56.81                                   
REMARK 500    GLN C 582      -40.25    151.06                                   
REMARK 500    GLN C 584      178.61     57.18                                   
REMARK 500    ALA C 633      -50.17    -27.22                                   
REMARK 500    ARG C 647       90.91   -172.37                                   
REMARK 500    GLU C 678      -14.40    -48.96                                   
REMARK 500    THR C 680      -54.10    -27.35                                   
REMARK 500    LEU C 702       73.53   -102.74                                   
REMARK 500    LYS D 462       71.29     41.81                                   
REMARK 500    ASP D 492       10.43    -60.55                                   
REMARK 500    PHE D 534      -33.12   -159.91                                   
REMARK 500    MET D 535      -39.91    -34.69                                   
REMARK 500    LEU D 536      -73.35    -40.99                                   
REMARK 500    GLN D 552     -128.24     79.19                                   
REMARK 500    THR D 553       91.37     54.62                                   
REMARK 500    GLN D 584      142.98     72.49                                   
REMARK 500    PRO D 585       83.34    -27.94                                   
REMARK 500    VAL D 586      133.55    -39.52                                   
REMARK 500    SER D 645      106.33    -55.63                                   
REMARK 500    THR D 646        8.12     42.44                                   
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 ARG C  485     GLU C  486                  146.46                    
REMARK 500 GLY C  630     SER C  631                  141.91                    
REMARK 500 ASP D  551     GLN D  552                  134.20                    
REMARK 500 GLN D  552     THR D  553                 -148.46                    
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 201  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  35   O                                                      
REMARK 620 2 THR A  17   OG1  74.4                                              
REMARK 620 3 GDP A 200   O1B 158.3 126.7                                        
REMARK 620 4 GDP A 200   O3B 146.1  71.7  55.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 201  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B  17   OG1                                                    
REMARK 620 2 GDP B 200   O3B  85.7                                              
REMARK 620 3 GDP B 200   O1B 135.0  49.3                                        
REMARK 620 4 THR B  35   O    78.2 146.8 139.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 200                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2H7O   RELATED DB: PDB                                   
DBREF  2H7V A    1   184  UNP    P63000   RAC1_HUMAN       1    184             
DBREF  2H7V B    1   184  UNP    P63000   RAC1_HUMAN       1    184             
DBREF  2H7V C  434   732  UNP    Q05608   YPKA_YERPS     434    732             
DBREF  2H7V D  434   732  UNP    Q05608   YPKA_YERPS     434    732             
SEQADV 2H7V GLY A    1B UNP  P63000              CLONING ARTIFACT               
SEQADV 2H7V SER A    2B UNP  P63000              CLONING ARTIFACT               
SEQADV 2H7V LYS A    1A UNP  P63000              CLONING ARTIFACT               
SEQADV 2H7V LEU A    2A UNP  P63000              CLONING ARTIFACT               
SEQADV 2H7V SER A   78  UNP  P63000    PHE    78 ENGINEERED                     
SEQADV 2H7V GLY B    1B UNP  P63000              CLONING ARTIFACT               
SEQADV 2H7V SER B    2B UNP  P63000              CLONING ARTIFACT               
SEQADV 2H7V LYS B    1A UNP  P63000              CLONING ARTIFACT               
SEQADV 2H7V LEU B    2A UNP  P63000              CLONING ARTIFACT               
SEQADV 2H7V SER B   78  UNP  P63000    PHE    78 ENGINEERED                     
SEQADV 2H7V GLY C  430  UNP  Q05608              CLONING ARTIFACT               
SEQADV 2H7V PRO C  431  UNP  Q05608              CLONING ARTIFACT               
SEQADV 2H7V VAL C  432  UNP  Q05608              CLONING ARTIFACT               
SEQADV 2H7V ASP C  433  UNP  Q05608              CLONING ARTIFACT               
SEQADV 2H7V GLY D  430  UNP  Q05608              CLONING ARTIFACT               
SEQADV 2H7V PRO D  431  UNP  Q05608              CLONING ARTIFACT               
SEQADV 2H7V VAL D  432  UNP  Q05608              CLONING ARTIFACT               
SEQADV 2H7V ASP D  433  UNP  Q05608              CLONING ARTIFACT               
SEQRES   1 A  188  GLY SER LYS LEU MET GLN ALA ILE LYS CYS VAL VAL VAL          
SEQRES   2 A  188  GLY ASP GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER          
SEQRES   3 A  188  TYR THR THR ASN ALA PHE PRO GLY GLU TYR ILE PRO THR          
SEQRES   4 A  188  VAL PHE ASP ASN TYR SER ALA ASN VAL MET VAL ASP GLY          
SEQRES   5 A  188  LYS PRO VAL ASN LEU GLY LEU TRP ASP THR ALA GLY GLN          
SEQRES   6 A  188  GLU ASP TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN          
SEQRES   7 A  188  THR ASP VAL SER LEU ILE CYS PHE SER LEU VAL SER PRO          
SEQRES   8 A  188  ALA SER PHE GLU ASN VAL ARG ALA LYS TRP TYR PRO GLU          
SEQRES   9 A  188  VAL ARG HIS HIS CYS PRO ASN THR PRO ILE ILE LEU VAL          
SEQRES  10 A  188  GLY THR LYS LEU ASP LEU ARG ASP ASP LYS ASP THR ILE          
SEQRES  11 A  188  GLU LYS LEU LYS GLU LYS LYS LEU THR PRO ILE THR TYR          
SEQRES  12 A  188  PRO GLN GLY LEU ALA MET ALA LYS GLU ILE GLY ALA VAL          
SEQRES  13 A  188  LYS TYR LEU GLU CYS SER ALA LEU THR GLN ARG GLY LEU          
SEQRES  14 A  188  LYS THR VAL PHE ASP GLU ALA ILE ARG ALA VAL LEU CYS          
SEQRES  15 A  188  PRO PRO PRO VAL LYS LYS                                      
SEQRES   1 B  188  GLY SER LYS LEU MET GLN ALA ILE LYS CYS VAL VAL VAL          
SEQRES   2 B  188  GLY ASP GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER          
SEQRES   3 B  188  TYR THR THR ASN ALA PHE PRO GLY GLU TYR ILE PRO THR          
SEQRES   4 B  188  VAL PHE ASP ASN TYR SER ALA ASN VAL MET VAL ASP GLY          
SEQRES   5 B  188  LYS PRO VAL ASN LEU GLY LEU TRP ASP THR ALA GLY GLN          
SEQRES   6 B  188  GLU ASP TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN          
SEQRES   7 B  188  THR ASP VAL SER LEU ILE CYS PHE SER LEU VAL SER PRO          
SEQRES   8 B  188  ALA SER PHE GLU ASN VAL ARG ALA LYS TRP TYR PRO GLU          
SEQRES   9 B  188  VAL ARG HIS HIS CYS PRO ASN THR PRO ILE ILE LEU VAL          
SEQRES  10 B  188  GLY THR LYS LEU ASP LEU ARG ASP ASP LYS ASP THR ILE          
SEQRES  11 B  188  GLU LYS LEU LYS GLU LYS LYS LEU THR PRO ILE THR TYR          
SEQRES  12 B  188  PRO GLN GLY LEU ALA MET ALA LYS GLU ILE GLY ALA VAL          
SEQRES  13 B  188  LYS TYR LEU GLU CYS SER ALA LEU THR GLN ARG GLY LEU          
SEQRES  14 B  188  LYS THR VAL PHE ASP GLU ALA ILE ARG ALA VAL LEU CYS          
SEQRES  15 B  188  PRO PRO PRO VAL LYS LYS                                      
SEQRES   1 C  303  GLY PRO VAL ASP SER THR ASP VAL ARG ARG ILE THR PRO          
SEQRES   2 C  303  LYS LYS LEU ARG GLU LEU SER ASP LEU LEU ARG THR HIS          
SEQRES   3 C  303  LEU SER SER ALA ALA THR LYS GLN LEU ASP MET GLY GLY          
SEQRES   4 C  303  VAL LEU SER ASP LEU ASP THR MET LEU VAL ALA LEU ASP          
SEQRES   5 C  303  LYS ALA GLU ARG GLU GLY GLY VAL ASP LYS ASP GLN LEU          
SEQRES   6 C  303  LYS SER PHE ASN SER LEU ILE LEU LYS THR TYR ARG VAL          
SEQRES   7 C  303  ILE GLU ASP TYR VAL LYS GLY ARG GLU GLY ASP THR LYS          
SEQRES   8 C  303  ASN SER SER THR GLU VAL SER PRO TYR HIS ARG SER ASN          
SEQRES   9 C  303  PHE MET LEU SER ILE VAL GLU PRO SER LEU GLN ARG ILE          
SEQRES  10 C  303  GLN LYS HIS LEU ASP GLN THR HIS SER PHE SER ASP ILE          
SEQRES  11 C  303  GLY SER LEU VAL ARG ALA HIS LYS HIS LEU GLU THR LEU          
SEQRES  12 C  303  LEU GLU VAL LEU VAL THR LEU SER GLN GLN GLY GLN PRO          
SEQRES  13 C  303  VAL SER SER GLU THR TYR GLY PHE LEU ASN ARG LEU ALA          
SEQRES  14 C  303  GLU ALA LYS ILE THR LEU SER GLN GLN LEU ASN THR LEU          
SEQRES  15 C  303  GLN GLN GLN GLN GLU SER ALA LYS ALA GLN LEU SER ILE          
SEQRES  16 C  303  LEU ILE ASN ARG SER GLY SER TRP ALA ASP VAL ALA ARG          
SEQRES  17 C  303  GLN SER LEU GLN ARG PHE ASP SER THR ARG PRO VAL VAL          
SEQRES  18 C  303  LYS PHE GLY THR GLU GLN TYR THR ALA ILE HIS ARG GLN          
SEQRES  19 C  303  MET MET ALA ALA HIS ALA ALA ILE THR LEU GLN GLU VAL          
SEQRES  20 C  303  SER GLU PHE THR ASP ASP MET ARG ASN PHE THR VAL ASP          
SEQRES  21 C  303  SER ILE PRO LEU LEU ILE GLN LEU GLY ARG SER SER LEU          
SEQRES  22 C  303  MET ASP GLU HIS LEU VAL GLU GLN ARG GLU LYS LEU ARG          
SEQRES  23 C  303  GLU LEU THR THR ILE ALA GLU ARG LEU ASN ARG LEU GLU          
SEQRES  24 C  303  ARG GLU TRP MET                                              
SEQRES   1 D  303  GLY PRO VAL ASP SER THR ASP VAL ARG ARG ILE THR PRO          
SEQRES   2 D  303  LYS LYS LEU ARG GLU LEU SER ASP LEU LEU ARG THR HIS          
SEQRES   3 D  303  LEU SER SER ALA ALA THR LYS GLN LEU ASP MET GLY GLY          
SEQRES   4 D  303  VAL LEU SER ASP LEU ASP THR MET LEU VAL ALA LEU ASP          
SEQRES   5 D  303  LYS ALA GLU ARG GLU GLY GLY VAL ASP LYS ASP GLN LEU          
SEQRES   6 D  303  LYS SER PHE ASN SER LEU ILE LEU LYS THR TYR ARG VAL          
SEQRES   7 D  303  ILE GLU ASP TYR VAL LYS GLY ARG GLU GLY ASP THR LYS          
SEQRES   8 D  303  ASN SER SER THR GLU VAL SER PRO TYR HIS ARG SER ASN          
SEQRES   9 D  303  PHE MET LEU SER ILE VAL GLU PRO SER LEU GLN ARG ILE          
SEQRES  10 D  303  GLN LYS HIS LEU ASP GLN THR HIS SER PHE SER ASP ILE          
SEQRES  11 D  303  GLY SER LEU VAL ARG ALA HIS LYS HIS LEU GLU THR LEU          
SEQRES  12 D  303  LEU GLU VAL LEU VAL THR LEU SER GLN GLN GLY GLN PRO          
SEQRES  13 D  303  VAL SER SER GLU THR TYR GLY PHE LEU ASN ARG LEU ALA          
SEQRES  14 D  303  GLU ALA LYS ILE THR LEU SER GLN GLN LEU ASN THR LEU          
SEQRES  15 D  303  GLN GLN GLN GLN GLU SER ALA LYS ALA GLN LEU SER ILE          
SEQRES  16 D  303  LEU ILE ASN ARG SER GLY SER TRP ALA ASP VAL ALA ARG          
SEQRES  17 D  303  GLN SER LEU GLN ARG PHE ASP SER THR ARG PRO VAL VAL          
SEQRES  18 D  303  LYS PHE GLY THR GLU GLN TYR THR ALA ILE HIS ARG GLN          
SEQRES  19 D  303  MET MET ALA ALA HIS ALA ALA ILE THR LEU GLN GLU VAL          
SEQRES  20 D  303  SER GLU PHE THR ASP ASP MET ARG ASN PHE THR VAL ASP          
SEQRES  21 D  303  SER ILE PRO LEU LEU ILE GLN LEU GLY ARG SER SER LEU          
SEQRES  22 D  303  MET ASP GLU HIS LEU VAL GLU GLN ARG GLU LYS LEU ARG          
SEQRES  23 D  303  GLU LEU THR THR ILE ALA GLU ARG LEU ASN ARG LEU GLU          
SEQRES  24 D  303  ARG GLU TRP MET                                              
HET     MG  A 201       1                                                       
HET     MG  B 201       1                                                       
HET    GDP  A 200      28                                                       
HET    GDP  B 200      28                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
FORMUL   5   MG    2(MG 2+)                                                     
FORMUL   7  GDP    2(C10 H15 N5 O11 P2)                                         
FORMUL   9  HOH   *75(H2 O)                                                     
HELIX    1   1 GLY A   15  ASN A   26  1                                  12    
HELIX    2   2 GLU A   62  ARG A   68  1                                   7    
HELIX    3   3 PRO A   69  TYR A   72  5                                   4    
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  5                                   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  LEU A  177  1                                  14    
HELIX   10  10 GLY B   15  ASN B   26  1                                  12    
HELIX   11  11 ASP B   63  ARG B   68  1                                   6    
HELIX   12  12 PRO B   69  TYR B   72  5                                   4    
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  ASP B  121  5                                   6    
HELIX   16  16 ASP B  122  GLU B  131  1                                  10    
HELIX   17  17 THR B  138  GLY B  150  1                                  13    
HELIX   18  18 GLY B  164  CYS B  178  1                                  15    
HELIX   19  19 THR C  441  THR C  461  1                                  21    
HELIX   20  20 ASP C  465  ARG C  485  1                                  21    
HELIX   21  21 ASP C  490  LYS C  513  1                                  24    
HELIX   22  22 ASN C  533  LYS C  548  1                                  16    
HELIX   23  23 ASP C  558  GLN C  581  1                                  24    
HELIX   24  24 SER C  587  GLY C  630  1                                  44    
HELIX   25  25 TRP C  632  SER C  645  1                                  14    
HELIX   26  26 THR C  658  VAL C  676  1                                  19    
HELIX   27  27 PHE C  679  GLY C  698  1                                  20    
HELIX   28  28 ASP C  704  MET C  732  1                                  29    
HELIX   29  29 LYS D  444  THR D  461  1                                  18    
HELIX   30  30 ASP D  465  GLU D  484  1                                  20    
HELIX   31  31 ASP D  490  ASP D  492  5                                   3    
HELIX   32  32 GLN D  493  TYR D  511  1                                  19    
HELIX   33  33 PHE D  534  VAL D  539  1                                   6    
HELIX   34  34 VAL D  539  LEU D  550  1                                  12    
HELIX   35  35 SER D  555  SER D  557  5                                   3    
HELIX   36  36 ASP D  558  GLY D  583  1                                  26    
HELIX   37  37 SER D  587  SER D  645  1                                  59    
HELIX   38  38 THR D  658  VAL D  676  1                                  19    
HELIX   39  39 PHE D  679  GLY D  698  1                                  20    
HELIX   40  40 ASP D  704  MET D  732  1                                  29    
SHEET    1   A 6 TYR A  40  VAL A  46  0                                        
SHEET    2   A 6 LYS A  49  TRP A  56 -1  O  LEU A  53   N  ALA A  42           
SHEET    3   A 6 GLN A   2  VAL A   9  1  N  ILE A   4   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  VAL A 113   N  ILE A  80           
SHEET    6   A 6 LYS A 153  GLU A 156  1  O  LEU A 155   N  LEU A 112           
SHEET    1   B 6 TYR B  40  VAL B  44  0                                        
SHEET    2   B 6 VAL B  51  TRP B  56 -1  O  VAL B  51   N  VAL B  44           
SHEET    3   B 6 GLN B   2  GLY B  10  1  N  ILE B   4   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  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        MG    MG A 201                 O   THR A  35     1555   1555  1.95  
LINK        MG    MG A 201                 OG1 THR A  17     1555   1555  2.37  
LINK        MG    MG A 201                 O1B GDP A 200     1555   1555  2.96  
LINK        MG    MG A 201                 O3B GDP A 200     1555   1555  2.53  
LINK        MG    MG B 201                 OG1 THR B  17     1555   1555  2.33  
LINK        MG    MG B 201                 O3B GDP B 200     1555   1555  2.10  
LINK        MG    MG B 201                 O1B GDP B 200     1555   1555  3.14  
LINK        MG    MG B 201                 O   THR B  35     1555   1555  1.97  
SITE     1 AC1  3 THR A  17  THR A  35  GDP A 200                               
SITE     1 AC2  3 THR B  17  THR B  35  GDP B 200                               
SITE     1 AC3 15 ASP A  11  ALA A  13  VAL A  14  GLY A  15                    
SITE     2 AC3 15 LYS A  16  THR A  17  CYS A  18  PHE A  28                    
SITE     3 AC3 15 ILE A  33  LYS A 116  ASP A 118  LEU A 119                    
SITE     4 AC3 15 ALA A 159  LEU A 160   MG A 201                               
SITE     1 AC4 15 ALA B  13  VAL B  14  GLY B  15  LYS B  16                    
SITE     2 AC4 15 THR B  17  CYS B  18  PHE B  28  ILE B  33                    
SITE     3 AC4 15 LYS B 116  ASP B 118  LEU B 119  SER B 158                    
SITE     4 AC4 15 ALA B 159  LEU B 160   MG B 201                               
CRYST1   66.398   75.519   99.772  92.08 103.38 115.79 P 1           2          
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      0.015061  0.007277  0.004779        0.00000                         
SCALE2      0.000000  0.014707  0.002328        0.00000                         
SCALE3      0.000000  0.000000  0.010431        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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