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Database: PDB
Entry: 3LWN
LinkDB: 3LWN
Original site: 3LWN 
HEADER    SIGNALING PROTEIN/RHOA-BINDING PROTEIN  24-FEB-10   3LWN              
TITLE     SHIGELLA IPGB2 IN COMPLEX WITH HUMAN RHOA, GDP AND MG2+ (COMPLEX B)   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSFORMING PROTEIN RHOA;                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 2-181;                                            
COMPND   5 SYNONYM: H12;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: IPGB2;                                                     
COMPND   9 CHAIN: F, G;                                                         
COMPND  10 SYNONYM: IPGB2, PROBABLY SECRETED BY THE MXI-SPA SECRETION MACHINERY;
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: RHOA;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: TUNER (DE3);                               
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-28C;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: SHIGELLA FLEXNERI;                              
SOURCE  13 ORGANISM_TAXID: 623;                                                 
SOURCE  14 GENE: IPGB2;                                                         
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: TUNER (DE3);                               
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PET-M 41                                  
KEYWDS    IPGB2, RHOA, GTPASE, GEF, GEF-GTPASE-COMPLEX, WXXXE, TTSS EFFECTOR    
KEYWDS   2 PROTEIN, BACTERIAL GEF, CYTOSKELETON DYNAMICS, SIGNALING PROTEIN-    
KEYWDS   3 RHOA-BINDING PROTEIN COMPLEX                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.U.KLINK,S.BARDEN,T.V.HEIDLER,C.BORCHERS,M.LADWEIN,T.E.B.STRADAL,    
AUTHOR   2 K.ROTTNER,D.W.HEINZ                                                  
REVDAT   3   13-JUL-11 3LWN    1       VERSN                                    
REVDAT   2   02-JUN-10 3LWN    1       JRNL                                     
REVDAT   1   31-MAR-10 3LWN    0                                                
JRNL        AUTH   B.U.KLINK,S.BARDEN,T.V.HEIDLER,C.BORCHERS,M.LADWEIN,         
JRNL        AUTH 2 T.E.B.STRADAL,K.ROTTNER,D.W.HEINZ                            
JRNL        TITL   STRUCTURE OF SHIGELLA IPGB2 IN COMPLEX WITH HUMAN RHOA:      
JRNL        TITL 2 IMPLICATIONS FOR THE MECHANISM OF BACTERIAL GEF-MIMICRY      
JRNL        REF    J.BIOL.CHEM.                  V. 285 17197 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20363740                                                     
JRNL        DOI    10.1074/JBC.M110.107953                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.28 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) : 2.28                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.13                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 34099                          
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) : 0.209                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.291                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1705                            
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) : 2.28                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.34                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2065                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.26                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2520                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 108                          
REMARK   3   BIN FREE R VALUE                    : 0.3240                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5770                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 435                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 31.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.75                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : -0.07000                                             
REMARK   3    B33 (A**2) : 0.06000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.459         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.302         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.224         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.323        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.899                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6064 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8202 ; 1.661 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   757 ; 5.653 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   291 ;36.776 ;24.880       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1159 ;17.564 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    39 ;19.012 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   904 ; 0.111 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4529 ; 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):  3664 ; 0.700 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5970 ; 1.275 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2400 ; 2.255 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2214 ; 3.495 ; 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  : 5                                          
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   181                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.5580   8.5930   8.1600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0229 T22:   0.0819                                     
REMARK   3      T33:   0.0199 T12:   0.0045                                     
REMARK   3      T13:  -0.0119 T23:  -0.0068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4199 L22:   1.9687                                     
REMARK   3      L33:   1.6202 L12:  -0.0716                                     
REMARK   3      L13:   0.3526 L23:   0.5924                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0512 S12:  -0.0366 S13:  -0.0145                       
REMARK   3      S21:  -0.1616 S22:  -0.0804 S23:   0.0586                       
REMARK   3      S31:  -0.0489 S32:  -0.1688 S33:   0.0293                       
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   181                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.5160  11.9190  59.7910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0234 T22:   0.0351                                     
REMARK   3      T33:   0.0239 T12:  -0.0221                                     
REMARK   3      T13:  -0.0041 T23:   0.0073                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7119 L22:   1.8299                                     
REMARK   3      L33:   1.4632 L12:  -0.1698                                     
REMARK   3      L13:   0.4745 L23:   0.0531                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0666 S12:  -0.0101 S13:  -0.0533                       
REMARK   3      S21:  -0.0804 S22:  -0.0265 S23:   0.0037                       
REMARK   3      S31:   0.0868 S32:  -0.0328 S33:  -0.0402                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     8        F   188                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.2720  20.6410  25.0710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0454 T22:   0.0907                                     
REMARK   3      T33:   0.0757 T12:  -0.0383                                     
REMARK   3      T13:  -0.0192 T23:  -0.0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5810 L22:   2.4532                                     
REMARK   3      L33:   1.9449 L12:  -0.6288                                     
REMARK   3      L13:  -0.0290 L23:   0.4089                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0242 S12:  -0.1067 S13:   0.0785                       
REMARK   3      S21:   0.0457 S22:   0.0262 S23:  -0.1333                       
REMARK   3      S31:  -0.0858 S32:   0.1007 S33:  -0.0020                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G     8        G   188                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.2560  23.9120  76.8430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0444 T22:   0.1126                                     
REMARK   3      T33:   0.0992 T12:  -0.0460                                     
REMARK   3      T13:  -0.0187 T23:  -0.0321                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1040 L22:   2.4834                                     
REMARK   3      L33:   2.0233 L12:  -0.6126                                     
REMARK   3      L13:   0.0649 L23:   0.0647                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0546 S12:  -0.1413 S13:   0.1333                       
REMARK   3      S21:   0.1326 S22:   0.0748 S23:  -0.1104                       
REMARK   3      S31:  -0.0182 S32:   0.1544 S33:  -0.0202                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   302        A   442                          
REMARK   3    RESIDUE RANGE :   B   303        B   451                          
REMARK   3    RESIDUE RANGE :   G   189        G   452                          
REMARK   3    RESIDUE RANGE :   F   189        F   440                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.1810  15.8720  39.0610              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1217 T22:   0.1126                                     
REMARK   3      T33:   0.1620 T12:  -0.0291                                     
REMARK   3      T13:  -0.0234 T23:   0.0060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1505 L22:   0.1132                                     
REMARK   3      L33:   0.6253 L12:  -0.0578                                     
REMARK   3      L13:  -0.0178 L23:   0.0813                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0212 S12:  -0.0105 S13:   0.0152                       
REMARK   3      S21:  -0.0050 S22:  -0.0174 S23:  -0.0033                       
REMARK   3      S31:  -0.0204 S32:   0.0342 S33:  -0.0039                       
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 U VALUES : RESIDUAL ONLY                                  
REMARK   4                                                                      
REMARK   4 3LWN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-MAR-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB057822.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-SEP-09                          
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) : 1.54                               
REMARK 200  MONOCHROMATOR                  : RIGAKU                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XSCALE                             
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34100                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.280                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.130                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : 0.13400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.8100                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.28                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.65400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3LW8                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG 3350; PROTEIN WAS          
REMARK 280  TREATED WITH EDTA PRIOR TO CRYSTALLIZATION, PH 7.5, VAPOR           
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
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       37.76500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       51.48000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.85000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       51.48000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.76500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.85000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G                                  
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    -3                                                      
REMARK 465     PRO A    -2                                                      
REMARK 465     LEU A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     PRO B    -2                                                      
REMARK 465     LEU B    -1                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     GLY F    -3                                                      
REMARK 465     ALA F    -2                                                      
REMARK 465     MET F    -1                                                      
REMARK 465     ASP F     0                                                      
REMARK 465     MET F     1                                                      
REMARK 465     LEU F     2                                                      
REMARK 465     GLY F     3                                                      
REMARK 465     THR F     4                                                      
REMARK 465     SER F     5                                                      
REMARK 465     PHE F     6                                                      
REMARK 465     ASN F     7                                                      
REMARK 465     GLY G    -3                                                      
REMARK 465     ALA G    -2                                                      
REMARK 465     MET G    -1                                                      
REMARK 465     ASP G     0                                                      
REMARK 465     MET G     1                                                      
REMARK 465     LEU G     2                                                      
REMARK 465     GLY G     3                                                      
REMARK 465     THR G     4                                                      
REMARK 465     SER G     5                                                      
REMARK 465     PHE G     6                                                      
REMARK 465     ASN G     7                                                      
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   OH   TYR G   167     O    HOH G   220              1.86            
REMARK 500   O    GLU G   185     O    HOH G   407              2.17            
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    ALA A  61      134.45    -37.48                                   
REMARK 500    LYS A  98      -56.78   -123.98                                   
REMARK 500    ASN B  41      135.73    -35.07                                   
REMARK 500    CYS B 107       66.24   -119.69                                   
REMARK 500    GLU F  57      -86.48      4.91                                   
REMARK 500    ALA F 115      -53.38   -140.19                                   
REMARK 500    VAL F 165      -59.40   -122.12                                   
REMARK 500    ILE F 181      -70.89    -88.63                                   
REMARK 500    ALA G 115      -56.03   -138.92                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASN G  64        23.6      L          L   OUTSIDE RANGE           
REMARK 500    TYR G 167        23.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 244        DISTANCE =  5.40 ANGSTROMS                       
REMARK 525    HOH B 258        DISTANCE =  5.68 ANGSTROMS                       
REMARK 525    HOH B 419        DISTANCE =  5.37 ANGSTROMS                       
REMARK 525    HOH B 420        DISTANCE =  5.47 ANGSTROMS                       
REMARK 525    HOH G 393        DISTANCE =  5.60 ANGSTROMS                       
REMARK 525    HOH G 449        DISTANCE =  5.15 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 A 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 200   O                                                      
REMARK 620 2 HOH A 269   O    76.5                                              
REMARK 620 3 HOH A 261   O   142.7 106.2                                        
REMARK 620 4 HOH A 268   O    89.4 120.4 117.9                                  
REMARK 620 5 GDP A 201   O1A  78.0 146.2  81.7  80.9                            
REMARK 620 6 HOH A 232   O    69.3  74.7  75.5 151.1  75.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 182   O                                                      
REMARK 620 2 HOH B 256   O    81.8                                              
REMARK 620 3 HOH B 257   O   106.4 169.3                                        
REMARK 620 4 GDP B 201   O1A  88.2  85.6  87.8                                  
REMARK 620 5 HOH B 228   O    80.8  79.5 108.2 162.5                            
REMARK 620 6 HOH B 207   O   171.1  92.3  78.6  84.7 104.8                      
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 GDP A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 301                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3LW8   RELATED DB: PDB                                   
REMARK 900 IPGB2 IN COMPLEX WITH HUMAN RHOA (COMPLEX A)                         
REMARK 900 RELATED ID: 3LXR   RELATED DB: PDB                                   
REMARK 900 IPGB2 IN COMPLEX WITH HUMAN RHOA (COMPLEX C)                         
REMARK 900 RELATED ID: 3LYQ   RELATED DB: PDB                                   
REMARK 900 IPGB2, APO FORM                                                      
DBREF  3LWN A    2   181  UNP    P61586   RHOA_HUMAN       2    181             
DBREF  3LWN B    2   181  UNP    P61586   RHOA_HUMAN       2    181             
DBREF  3LWN F    1   188  UNP    Q9AJW7   Q9AJW7_SHIFL     1    188             
DBREF  3LWN G    1   188  UNP    Q9AJW7   Q9AJW7_SHIFL     1    188             
SEQADV 3LWN GLY A   -3  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LWN PRO A   -2  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LWN LEU A   -1  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LWN GLY A    0  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LWN SER A    1  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LWN GLY B   -3  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LWN PRO B   -2  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LWN LEU B   -1  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LWN GLY B    0  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LWN SER B    1  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LWN GLY F   -3  UNP  Q9AJW7              EXPRESSION TAG                 
SEQADV 3LWN ALA F   -2  UNP  Q9AJW7              EXPRESSION TAG                 
SEQADV 3LWN MET F   -1  UNP  Q9AJW7              EXPRESSION TAG                 
SEQADV 3LWN ASP F    0  UNP  Q9AJW7              EXPRESSION TAG                 
SEQADV 3LWN GLY G   -3  UNP  Q9AJW7              EXPRESSION TAG                 
SEQADV 3LWN ALA G   -2  UNP  Q9AJW7              EXPRESSION TAG                 
SEQADV 3LWN MET G   -1  UNP  Q9AJW7              EXPRESSION TAG                 
SEQADV 3LWN ASP G    0  UNP  Q9AJW7              EXPRESSION TAG                 
SEQRES   1 A  185  GLY PRO LEU GLY SER ALA ALA ILE ARG LYS LYS LEU VAL          
SEQRES   2 A  185  ILE VAL GLY ASP GLY ALA CYS GLY LYS THR CYS LEU LEU          
SEQRES   3 A  185  ILE VAL PHE SER LYS ASP GLN PHE PRO GLU VAL TYR VAL          
SEQRES   4 A  185  PRO THR VAL PHE GLU ASN TYR VAL ALA ASP ILE GLU VAL          
SEQRES   5 A  185  ASP GLY LYS GLN VAL GLU LEU ALA LEU TRP ASP THR ALA          
SEQRES   6 A  185  GLY GLN GLU ASP TYR ASP ARG LEU ARG PRO LEU SER TYR          
SEQRES   7 A  185  PRO ASP THR ASP VAL ILE LEU MET CYS PHE SER ILE ASP          
SEQRES   8 A  185  SER PRO ASP SER LEU GLU ASN ILE PRO GLU LYS TRP THR          
SEQRES   9 A  185  PRO GLU VAL LYS HIS PHE CYS PRO ASN VAL PRO ILE ILE          
SEQRES  10 A  185  LEU VAL GLY ASN LYS LYS ASP LEU ARG ASN ASP GLU HIS          
SEQRES  11 A  185  THR ARG ARG GLU LEU ALA LYS MET LYS GLN GLU PRO VAL          
SEQRES  12 A  185  LYS PRO GLU GLU GLY ARG ASP MET ALA ASN ARG ILE GLY          
SEQRES  13 A  185  ALA PHE GLY TYR MET GLU CYS SER ALA LYS THR LYS ASP          
SEQRES  14 A  185  GLY VAL ARG GLU VAL PHE GLU MET ALA THR ARG ALA ALA          
SEQRES  15 A  185  LEU GLN ALA                                                  
SEQRES   1 B  185  GLY PRO LEU GLY SER ALA ALA ILE ARG LYS LYS LEU VAL          
SEQRES   2 B  185  ILE VAL GLY ASP GLY ALA CYS GLY LYS THR CYS LEU LEU          
SEQRES   3 B  185  ILE VAL PHE SER LYS ASP GLN PHE PRO GLU VAL TYR VAL          
SEQRES   4 B  185  PRO THR VAL PHE GLU ASN TYR VAL ALA ASP ILE GLU VAL          
SEQRES   5 B  185  ASP GLY LYS GLN VAL GLU LEU ALA LEU TRP ASP THR ALA          
SEQRES   6 B  185  GLY GLN GLU ASP TYR ASP ARG LEU ARG PRO LEU SER TYR          
SEQRES   7 B  185  PRO ASP THR ASP VAL ILE LEU MET CYS PHE SER ILE ASP          
SEQRES   8 B  185  SER PRO ASP SER LEU GLU ASN ILE PRO GLU LYS TRP THR          
SEQRES   9 B  185  PRO GLU VAL LYS HIS PHE CYS PRO ASN VAL PRO ILE ILE          
SEQRES  10 B  185  LEU VAL GLY ASN LYS LYS ASP LEU ARG ASN ASP GLU HIS          
SEQRES  11 B  185  THR ARG ARG GLU LEU ALA LYS MET LYS GLN GLU PRO VAL          
SEQRES  12 B  185  LYS PRO GLU GLU GLY ARG ASP MET ALA ASN ARG ILE GLY          
SEQRES  13 B  185  ALA PHE GLY TYR MET GLU CYS SER ALA LYS THR LYS ASP          
SEQRES  14 B  185  GLY VAL ARG GLU VAL PHE GLU MET ALA THR ARG ALA ALA          
SEQRES  15 B  185  LEU GLN ALA                                                  
SEQRES   1 F  192  GLY ALA MET ASP MET LEU GLY THR SER PHE ASN ASN PHE          
SEQRES   2 F  192  GLY ILE SER LEU SER HIS LYS ARG TYR PHE SER GLY LYS          
SEQRES   3 F  192  VAL ASP GLU ILE ILE ARG CYS THR MET GLY LYS ARG ILE          
SEQRES   4 F  192  VAL LYS ILE SER SER THR LYS ILE ASN THR SER ILE LEU          
SEQRES   5 F  192  SER SER VAL SER GLU GLN ILE GLY GLU ASN ILE THR ASP          
SEQRES   6 F  192  TRP LYS ASN ASP GLU LYS LYS VAL TYR VAL SER ARG VAL          
SEQRES   7 F  192  VAL ASN GLN CYS ILE ASP LYS PHE CYS ALA GLU HIS SER          
SEQRES   8 F  192  ARG LYS ILE GLY ASP ASN LEU ARG LYS GLN ILE PHE LYS          
SEQRES   9 F  192  GLN VAL GLU LYS ASP TYR ARG ILE SER LEU ASP ILE ASN          
SEQRES  10 F  192  ALA ALA GLN SER SER ILE ASN HIS LEU VAL SER GLY SER          
SEQRES  11 F  192  SER TYR PHE LYS LYS LYS MET ASP GLU LEU CYS GLU GLY          
SEQRES  12 F  192  MET ASN ARG SER VAL LYS ASN ASP THR THR SER ASN VAL          
SEQRES  13 F  192  ALA ASN LEU ILE SER ASP GLN PHE PHE GLU LYS ASN VAL          
SEQRES  14 F  192  GLN TYR ILE ASP LEU LYS LYS LEU ARG GLY ASN MET SER          
SEQRES  15 F  192  ASP TYR ILE THR ASN LEU GLU SER PRO PHE                      
SEQRES   1 G  192  GLY ALA MET ASP MET LEU GLY THR SER PHE ASN ASN PHE          
SEQRES   2 G  192  GLY ILE SER LEU SER HIS LYS ARG TYR PHE SER GLY LYS          
SEQRES   3 G  192  VAL ASP GLU ILE ILE ARG CYS THR MET GLY LYS ARG ILE          
SEQRES   4 G  192  VAL LYS ILE SER SER THR LYS ILE ASN THR SER ILE LEU          
SEQRES   5 G  192  SER SER VAL SER GLU GLN ILE GLY GLU ASN ILE THR ASP          
SEQRES   6 G  192  TRP LYS ASN ASP GLU LYS LYS VAL TYR VAL SER ARG VAL          
SEQRES   7 G  192  VAL ASN GLN CYS ILE ASP LYS PHE CYS ALA GLU HIS SER          
SEQRES   8 G  192  ARG LYS ILE GLY ASP ASN LEU ARG LYS GLN ILE PHE LYS          
SEQRES   9 G  192  GLN VAL GLU LYS ASP TYR ARG ILE SER LEU ASP ILE ASN          
SEQRES  10 G  192  ALA ALA GLN SER SER ILE ASN HIS LEU VAL SER GLY SER          
SEQRES  11 G  192  SER TYR PHE LYS LYS LYS MET ASP GLU LEU CYS GLU GLY          
SEQRES  12 G  192  MET ASN ARG SER VAL LYS ASN ASP THR THR SER ASN VAL          
SEQRES  13 G  192  ALA ASN LEU ILE SER ASP GLN PHE PHE GLU LYS ASN VAL          
SEQRES  14 G  192  GLN TYR ILE ASP LEU LYS LYS LEU ARG GLY ASN MET SER          
SEQRES  15 G  192  ASP TYR ILE THR ASN LEU GLU SER PRO PHE                      
HET    GDP  A 201      28                                                       
HET     MG  A 301       1                                                       
HET    GDP  B 201      28                                                       
HET     MG  B 301       1                                                       
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   5  GDP    2(C10 H15 N5 O11 P2)                                         
FORMUL   6   MG    2(MG 2+)                                                     
FORMUL   9  HOH   *435(H2 O)                                                    
HELIX    1   1 GLY A   17  ASP A   28  1                                  12    
HELIX    2   2 LEU A   69  TYR A   74  5                                   6    
HELIX    3   3 SER A   88  LYS A   98  1                                  11    
HELIX    4   4 LYS A   98  CYS A  107  1                                  10    
HELIX    5   5 LYS A  118  ARG A  122  5                                   5    
HELIX    6   6 ASP A  124  MET A  134  1                                  11    
HELIX    7   7 LYS A  140  GLY A  152  1                                  13    
HELIX    8   8 GLY A  166  GLN A  180  1                                  15    
HELIX    9   9 GLY B   17  ASP B   28  1                                  12    
HELIX   10  10 LEU B   69  TYR B   74  5                                   6    
HELIX   11  11 SER B   88  LYS B   98  1                                  11    
HELIX   12  12 LYS B   98  CYS B  107  1                                  10    
HELIX   13  13 LYS B  118  ARG B  122  5                                   5    
HELIX   14  14 ASP B  124  MET B  134  1                                  11    
HELIX   15  15 LYS B  140  ILE B  151  1                                  12    
HELIX   16  16 GLY B  166  GLN B  180  1                                  15    
HELIX   17  17 SER F   40  ILE F   55  1                                  16    
HELIX   18  18 ASN F   58  SER F   87  1                                  30    
HELIX   19  19 GLY F   91  ARG F  107  1                                  17    
HELIX   20  20 SER F  117  GLY F  125  1                                   9    
HELIX   21  21 SER F  126  CYS F  137  1                                  12    
HELIX   22  22 ASN F  141  VAL F  165  1                                  25    
HELIX   23  23 ASP F  169  ASN F  183  1                                  15    
HELIX   24  24 SER G   40  GLY G   56  1                                  17    
HELIX   25  25 ILE G   59  SER G   87  1                                  29    
HELIX   26  26 GLY G   91  ARG G  107  1                                  17    
HELIX   27  27 SER G  117  GLY G  125  1                                   9    
HELIX   28  28 SER G  126  GLU G  138  1                                  13    
HELIX   29  29 ASN G  141  VAL G  165  1                                  25    
HELIX   30  30 ASP G  169  ASN G  183  1                                  15    
SHEET    1   A 6 TYR A  42  VAL A  48  0                                        
SHEET    2   A 6 LYS A  51  ASP A  59 -1  O  LEU A  57   N  TYR A  42           
SHEET    3   A 6 ILE A   4  GLY A  12  1  N  LYS A   6   O  ALA A  56           
SHEET    4   A 6 VAL A  79  SER A  85  1  O  CYS A  83   N  VAL A  11           
SHEET    5   A 6 ILE A 112  ASN A 117  1  O  ILE A 113   N  MET A  82           
SHEET    6   A 6 GLY A 155  GLU A 158  1  O  MET A 157   N  GLY A 116           
SHEET    1   B 6 TYR B  42  VAL B  48  0                                        
SHEET    2   B 6 LYS B  51  TRP B  58 -1  O  LEU B  55   N  ALA B  44           
SHEET    3   B 6 ILE B   4  GLY B  12  1  N  LEU B   8   O  TRP B  58           
SHEET    4   B 6 VAL B  79  SER B  85  1  O  LEU B  81   N  VAL B  11           
SHEET    5   B 6 ILE B 112  ASN B 117  1  O  VAL B 115   N  MET B  82           
SHEET    6   B 6 GLY B 155  GLU B 158  1  O  MET B 157   N  GLY B 116           
SHEET    1   C 3 PHE F   9  ARG F  17  0                                        
SHEET    2   C 3 VAL F  23  MET F  31 -1  O  ARG F  28   N  SER F  12           
SHEET    3   C 3 ARG F  34  SER F  39 -1  O  VAL F  36   N  CYS F  29           
SHEET    1   D 3 GLY G  10  ARG G  17  0                                        
SHEET    2   D 3 VAL G  23  MET G  31 -1  O  THR G  30   N  GLY G  10           
SHEET    3   D 3 ARG G  34  SER G  39 -1  O  ILE G  38   N  ILE G  27           
LINK        MG    MG A 301                 O   HOH A 200     1555   1555  1.93  
LINK        MG    MG A 301                 O   HOH A 269     1555   1555  1.96  
LINK        MG    MG B 301                 O   HOH B 182     1555   1555  1.98  
LINK        MG    MG A 301                 O   HOH A 261     1555   1555  1.99  
LINK        MG    MG A 301                 O   HOH A 268     1555   1555  2.00  
LINK        MG    MG B 301                 O   HOH B 256     1555   1555  2.08  
LINK        MG    MG B 301                 O   HOH B 257     1555   1555  2.13  
LINK         O1A GDP B 201                MG    MG B 301     1555   1555  2.21  
LINK         O1A GDP A 201                MG    MG A 301     1555   1555  2.27  
LINK        MG    MG B 301                 O   HOH B 228     1555   1555  2.31  
LINK        MG    MG B 301                 O   HOH B 207     1555   1555  2.39  
LINK        MG    MG A 301                 O   HOH A 232     1555   1555  2.58  
SITE     1 AC1 23 ASP A  13  ALA A  15  CYS A  16  GLY A  17                    
SITE     2 AC1 23 LYS A  18  THR A  19  CYS A  20  VAL A  35                    
SITE     3 AC1 23 ALA A  61  LYS A 118  ASP A 120  LEU A 121                    
SITE     4 AC1 23 SER A 160  ALA A 161  LYS A 162  HOH A 190                    
SITE     5 AC1 23 HOH A 200  HOH A 229  HOH A 232  HOH A 261                    
SITE     6 AC1 23 HOH A 268  HOH A 283   MG A 301                               
SITE     1 AC2  6 HOH A 200  GDP A 201  HOH A 232  HOH A 261                    
SITE     2 AC2  6 HOH A 268  HOH A 269                                          
SITE     1 AC3 25 GLY B  14  ALA B  15  CYS B  16  GLY B  17                    
SITE     2 AC3 25 LYS B  18  THR B  19  CYS B  20  VAL B  35                    
SITE     3 AC3 25 ALA B  61  LYS B 118  ASP B 120  LEU B 121                    
SITE     4 AC3 25 SER B 160  ALA B 161  LYS B 162  HOH B 182                    
SITE     5 AC3 25 HOH B 191  HOH B 194  HOH B 207  HOH B 220                    
SITE     6 AC3 25 HOH B 221  HOH B 241  HOH B 256  HOH B 257                    
SITE     7 AC3 25  MG B 301                                                     
SITE     1 AC4  6 HOH B 182  GDP B 201  HOH B 207  HOH B 228                    
SITE     2 AC4  6 HOH B 256  HOH B 257                                          
CRYST1   75.530   95.700  102.960  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      0.013240  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010449  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009713        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system