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Database: PDB
Entry: 1A2B
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Original site: 1A2B 
HEADER    ONCOGENE PROTEIN                        26-DEC-97   1A2B              
TITLE     HUMAN RHOA COMPLEXED WITH GTP ANALOGUE                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSFORMING PROTEIN RHOA;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 1 - 181;                                          
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 OTHER_DETAILS: COMPLEXED WITH ONE GTPGAMMAS AND ONE MG ION           
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOSOL;                        
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PRSET B (INVITROGEN CO.)                  
KEYWDS    SMALL G-PROTEIN, SIGNAL TRANSDUCTION, GTPASE, RAS                     
KEYWDS   2 SUPERFAMILY, ONCOGENE PROTEIN                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.IHARA,S.MURAGUCHI,M.KATO,T.SHIMIZU,M.SHIRAKAWA,S.KURODA,            
AUTHOR   2 K.KAIBUCHI,T.HAKOSHIMA                                               
REVDAT   2   24-FEB-09 1A2B    1       VERSN                                    
REVDAT   1   17-JUN-98 1A2B    0                                                
JRNL        AUTH   K.IHARA,S.MURAGUCHI,M.KATO,T.SHIMIZU,M.SHIRAKAWA,            
JRNL        AUTH 2 S.KURODA,K.KAIBUCHI,T.HAKOSHIMA                              
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN RHOA IN A DOMINANTLY              
JRNL        TITL 2 ACTIVE FORM COMPLEXED WITH A GTP ANALOGUE.                   
JRNL        REF    J.BIOL.CHEM.                  V. 273  9656 1998              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   9545299                                                      
JRNL        DOI    10.1074/JBC.273.16.9656                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   E.F.PAI,U.KRENGEL,G.A.PETSKO,R.S.GOODY,W.KABSCH,             
REMARK   1  AUTH 2 A.WITTINGHOFER                                               
REMARK   1  TITL   REFINED CRYSTAL STRUCTURE OF THE TRIPHOSPHATE                
REMARK   1  TITL 2 CONFORMATION OF H-RAS P21 AT 1.35 A RESOLUTION:              
REMARK   1  TITL 3 IMPLICATIONS FOR THE MECHANISM OF GTP HYDROLYSIS             
REMARK   1  REF    EMBO J.                       V.   9  2351 1990              
REMARK   1  REFN                   ISSN 0261-4189                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.8                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0001                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 86.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 8382                           
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 SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 893                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.51                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 66.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 717                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3060                       
REMARK   3   BIN FREE R VALUE                    : 0.3810                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 77                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1417                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 38                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.31                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.36                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.10                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1A2B COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : MAR-97                             
REMARK 200  TEMPERATURE           (KELVIN) : 283                                
REMARK 200  PH                             : 7.5-8.5                            
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 RUH3R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE(002)                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : PROCESS                            
REMARK 200  DATA SCALING SOFTWARE          : PROCESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8683                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.3                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.08750                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.9100                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.040                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.8                                            
REMARK 200 STARTING MODEL: PDB ENTRY 5P21                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE OBTAINED AT 277 K BY       
REMARK 280  THE HANGING-DROP VAPOR DIFFUSION METHOD FROM SOLUTIONS              
REMARK 280  CONTAINING 10 MG/ML(PROTEIN,GTPGAMMAS,MG2+ MIXTURE), 10% PEG        
REMARK 280  8000,7.5% 14-DIOXANE, 50 MM TRIS-HCL PH 8.5, EQUILIBRATED           
REMARK 280  AGAINST 20% PEG 8000,15% 14-DIOXANE, 100 MM TRIS-HCL PH 8.5,        
REMARK 280  VAPOR DIFFUSION - HANGING DROP                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       31.01000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.39000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.01000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.39000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
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    ASP A  13      174.30    -57.18                                   
REMARK 500    LYS A  27       -4.72   -142.98                                   
REMARK 500    ASP A  28       -9.47     63.87                                   
REMARK 500    ASP A  65      -19.53    -47.83                                   
REMARK 500    PRO A  75      -78.92    -23.27                                   
REMARK 500    LYS A 164       -2.10     83.49                                   
REMARK 500    ASP A 165      107.97    -53.50                                   
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 609        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH A 622        DISTANCE =  5.75 ANGSTROMS                       
REMARK 525    HOH A 632        DISTANCE =  5.06 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 550  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GSP A 538   O2G                                                    
REMARK 620 2 THR A  19   OG1 173.5                                              
REMARK 620 3 THR A  37   OG1  91.2  95.0                                        
REMARK 620 4 GSP A 538   O2B  81.7  91.8 167.6                                  
REMARK 620 5 HOH A 604   O    94.3  84.0  85.9  84.5                            
REMARK 620 6 HOH A 605   O    83.9  96.8 102.2  87.2 171.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 550                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSP A 538                 
DBREF  1A2B A    1   181  UNP    P61586   RHOA_HUMAN       1    181             
SEQADV 1A2B VAL A   14  UNP  P61586    GLY    14 ENGINEERED                     
SEQRES   1 A  182  SER MET ALA ALA ILE ARG LYS LYS LEU VAL ILE VAL GLY          
SEQRES   2 A  182  ASP VAL ALA CYS GLY LYS THR CYS LEU LEU ILE VAL PHE          
SEQRES   3 A  182  SER LYS ASP GLN PHE PRO GLU VAL TYR VAL PRO THR VAL          
SEQRES   4 A  182  PHE GLU ASN TYR VAL ALA ASP ILE GLU VAL ASP GLY LYS          
SEQRES   5 A  182  GLN VAL GLU LEU ALA LEU TRP ASP THR ALA GLY GLN GLU          
SEQRES   6 A  182  ASP TYR ASP ARG LEU ARG PRO LEU SER TYR PRO ASP THR          
SEQRES   7 A  182  ASP VAL ILE LEU MET CYS PHE SER ILE ASP SER PRO ASP          
SEQRES   8 A  182  SER LEU GLU ASN ILE PRO GLU LYS TRP THR PRO GLU VAL          
SEQRES   9 A  182  LYS HIS PHE CYS PRO ASN VAL PRO ILE ILE LEU VAL GLY          
SEQRES  10 A  182  ASN LYS LYS ASP LEU ARG ASN ASP GLU HIS THR ARG ARG          
SEQRES  11 A  182  GLU LEU ALA LYS MET LYS GLN GLU PRO VAL LYS PRO GLU          
SEQRES  12 A  182  GLU GLY ARG ASP MET ALA ASN ARG ILE GLY ALA PHE GLY          
SEQRES  13 A  182  TYR MET GLU CYS SER ALA LYS THR LYS ASP GLY VAL ARG          
SEQRES  14 A  182  GLU VAL PHE GLU MET ALA THR ARG ALA ALA LEU GLN ALA          
HET     MG  A 550       1                                                       
HET    GSP  A 538      32                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE                       
FORMUL   2   MG    MG 2+                                                        
FORMUL   3  GSP    C10 H16 N5 O13 P3 S                                          
FORMUL   4  HOH   *38(H2 O)                                                     
HELIX    1   1 LYS A   18  LYS A   27  1                                  10    
HELIX    2   2 GLU A   64  LEU A   72  5                                   9    
HELIX    3   3 PRO A   89  GLU A   97  5                                   9    
HELIX    4   4 TRP A   99  PHE A  106  1                                   8    
HELIX    5   5 LYS A  119  ARG A  122  5                                   4    
HELIX    6   6 GLU A  125  LYS A  133  1                                   9    
HELIX    7   7 PRO A  141  ARG A  150  1                                  10    
HELIX    8   8 VAL A  167  LEU A  179  1                                  13    
SHEET    1   A 6 GLY A 155  GLU A 158  0                                        
SHEET    2   A 6 PRO A 111  ASN A 117  1  N  LEU A 114   O  GLY A 155           
SHEET    3   A 6 VAL A  79  SER A  85  1  N  ILE A  80   O  PRO A 111           
SHEET    4   A 6 ARG A   5  GLY A  12  1  N  VAL A   9   O  VAL A  79           
SHEET    5   A 6 LYS A  51  THR A  60  1  N  GLU A  54   O  LYS A   6           
SHEET    6   A 6 PHE A  39  VAL A  48 -1  N  VAL A  48   O  LYS A  51           
LINK         O2G GSP A 538                MG    MG A 550     1555   1555  2.27  
LINK        MG    MG A 550                 OG1 THR A  19     1555   1555  2.00  
LINK        MG    MG A 550                 OG1 THR A  37     1555   1555  2.06  
LINK        MG    MG A 550                 O2B GSP A 538     1555   1555  2.47  
LINK        MG    MG A 550                 O   HOH A 604     1555   1555  1.95  
LINK        MG    MG A 550                 O   HOH A 605     1555   1555  1.98  
SITE     1 AC1  5 THR A  19  THR A  37  GSP A 538  HOH A 604                    
SITE     2 AC1  5 HOH A 605                                                     
SITE     1 AC2 21 ASP A  13  ALA A  15  CYS A  16  GLY A  17                    
SITE     2 AC2 21 LYS A  18  THR A  19  CYS A  20  TYR A  34                    
SITE     3 AC2 21 THR A  37  GLY A  62  LYS A 118  ASP A 120                    
SITE     4 AC2 21 LEU A 121  SER A 160  ALA A 161  LYS A 162                    
SITE     5 AC2 21  MG A 550  HOH A 601  HOH A 602  HOH A 604                    
SITE     6 AC2 21 HOH A 605                                                     
CRYST1   62.020   74.780   50.520  90.00  90.00  90.00 P 21 21 2     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016124  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013373  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019794        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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