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Database: PDB
Entry: 421P
LinkDB: 421P
Original site: 421P 
HEADER    ONCOGENE PROTEIN                        06-JUN-91   421P              
TITLE     THREE-DIMENSIONAL STRUCTURES OF H-RAS P21 MUTANTS: MOLECULAR BASIS FOR
TITLE    2 THEIR INABILITY TO FUNCTION AS SIGNAL SWITCH MOLECULES               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: H-RAS P21 PROTEIN;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606                                                 
KEYWDS    ONCOGENE PROTEIN                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    U.KRENGEL,J.JOHN,A.SCHERER,W.KABSCH,A.WITTINGHOFER,E.F.PAI            
REVDAT   5   29-NOV-17 421P    1       HELIX                                    
REVDAT   4   07-MAR-12 421P    1       COMPND SEQADV VERSN                      
REVDAT   3   24-FEB-09 421P    1       VERSN                                    
REVDAT   2   01-APR-03 421P    1       JRNL                                     
REVDAT   1   31-JAN-94 421P    0                                                
JRNL        AUTH   U.KRENGEL,I.SCHLICHTING,A.SCHERER,R.SCHUMANN,M.FRECH,J.JOHN, 
JRNL        AUTH 2 W.KABSCH,E.F.PAI,A.WITTINGHOFER                              
JRNL        TITL   THREE-DIMENSIONAL STRUCTURES OF H-RAS P21 MUTANTS: MOLECULAR 
JRNL        TITL 2 BASIS FOR THEIR INABILITY TO FUNCTION AS SIGNAL SWITCH       
JRNL        TITL 3 MOLECULES.                                                   
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V.  62   539 1990              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   2199064                                                      
JRNL        DOI    10.1016/0092-8674(90)90018-A                                 
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 CONFORMATION   
REMARK   1  TITL 2 OF H-RAS P21 AT 1.35 ANGSTROMS RESOLUTION: IMPLICATIONS FOR  
REMARK   1  TITL 3 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.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
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           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
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            : 1329                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 202                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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) : 0.017                           
REMARK   3   BOND ANGLES            (DEGREES) : 3.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: RESIDUES 61 - 64 (GLN - GLU - GLU -       
REMARK   3  TYR) ADOPT SEVERAL CONFORMATIONS IN THE CRYSTAL. THE COORDINATES    
REMARK   3  GIVEN APPROXIMATE ONE OF THESE. THE ELECTRON DENSITY FOR THIS       
REMARK   3  PART OF THE STRUCTURE IS NOT AS WELL DEFINED AS FOR THE REST OF     
REMARK   3  THE STRUCTURE.                                                      
REMARK   4                                                                      
REMARK   4 421P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000179220.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      108.13333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       54.06667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       54.06667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      108.13333            
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 SECONDARY STRUCTURE ELEMENTS HAVE BEEN ASSIGNED ACCORDING            
REMARK 400 TO THE PROGRAM DSSP (W.KABSCH AND C.SANDER, 1983,                    
REMARK 400 BIOPOLYMERS 22:2577-2637).                                           
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ALA A 122    CB                                                  
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    LEU A   6   CA  -  CB  -  CG  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    ARG A  12   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ASP A  33   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    VAL A  44   N   -  CA  -  CB  ANGL. DEV. = -14.8 DEGREES          
REMARK 500    ARG A  68   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A  68   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    TYR A  96   CB  -  CG  -  CD2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A 123   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    GLN A 129   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    TYR A 137   CA  -  C   -  N   ANGL. DEV. =  18.2 DEGREES          
REMARK 500    TYR A 137   O   -  C   -  N   ANGL. DEV. = -14.2 DEGREES          
REMARK 500    ARG A 161   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG A 164   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 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    ASP A  33       79.67   -156.83                                   
REMARK 500    ILE A  36      -63.45   -100.25                                   
REMARK 500    GLN A  61     -148.11   -123.71                                   
REMARK 500    GLU A  62     -164.94    106.69                                   
REMARK 500    GLU A  63       16.96    -66.33                                   
REMARK 500    SER A  65     -115.66   -118.43                                   
REMARK 500    MET A  67       -5.93    -45.84                                   
REMARK 500    LYS A 117       36.37     76.25                                   
REMARK 500    ALA A 122       65.63     85.30                                   
REMARK 500    ARG A 149       10.27     83.20                                   
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 168  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A  17   OG                                                     
REMARK 620 2 THR A  35   OG1  85.5                                              
REMARK 620 3 GNP A 167   O2G 168.9 103.3                                        
REMARK 620 4 GNP A 167   O2B  92.1 176.3  79.4                                  
REMARK 620 5 HOH A 246   O    90.6 106.5  80.5  76.2                            
REMARK 620 6 HOH A 205   O    87.1  90.7  99.4  86.4 162.4                      
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 168                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A 167                 
DBREF  421P A    1   166  UNP    P01112   RASH_HUMAN       1    166             
SEQADV 421P ARG A   12  UNP  P01112    GLY    12 ENGINEERED MUTATION            
SEQRES   1 A  166  MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA ARG GLY          
SEQRES   2 A  166  VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN ASN          
SEQRES   3 A  166  HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP SER          
SEQRES   4 A  166  TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS LEU          
SEQRES   5 A  166  LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR SER          
SEQRES   6 A  166  ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY PHE          
SEQRES   7 A  166  LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE GLU          
SEQRES   8 A  166  ASP ILE HIS GLN TYR ARG GLU GLN ILE LYS ARG VAL LYS          
SEQRES   9 A  166  ASP SER ASP ASP VAL PRO MET VAL LEU VAL GLY ASN LYS          
SEQRES  10 A  166  CYS ASP LEU ALA ALA ARG THR VAL GLU SER ARG GLN ALA          
SEQRES  11 A  166  GLN ASP LEU ALA ARG SER TYR GLY ILE PRO TYR ILE GLU          
SEQRES  12 A  166  THR SER ALA LYS THR ARG GLN GLY VAL GLU ASP ALA PHE          
SEQRES  13 A  166  TYR THR LEU VAL ARG GLU ILE ARG GLN HIS                      
HET     MG  A 168       1                                                       
HET    GNP  A 167      32                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER                      
FORMUL   2   MG    MG 2+                                                        
FORMUL   3  GNP    C10 H17 N6 O13 P3                                            
FORMUL   4  HOH   *202(H2 O)                                                    
HELIX    1  A1 LYS A   16  GLN A   25  1                                  10    
HELIX    2  A2 ASP A   69  THR A   74  1RES. 66-68 IN 3/10 CONFRMTN        6    
HELIX    3  A3 THR A   87  LYS A  104  1KINK AT ASP 92                    18    
HELIX    4  A4 SER A  127  SER A  136  1                                  10    
HELIX    5  A5 VAL A  152  ARG A  164  1                                  13    
SHEET    1   S 6 GLU A  37  ILE A  46  0                                        
SHEET    2   S 6 GLU A  49  THR A  58 -1  O  LEU A  53   N  LYS A  42           
SHEET    3   S 6 THR A   2  GLY A  10  1  N  LEU A   6   O  ASP A  54           
SHEET    4   S 6 GLY A  77  ALA A  83  1  N  LEU A  79   O  VAL A   7           
SHEET    5   S 6 MET A 111  ASN A 116  1  N  VAL A 114   O  CYS A  80           
SHEET    6   S 6 TYR A 141  THR A 144  1  N  ILE A 142   O  LEU A 113           
LINK        MG    MG A 168                 OG  SER A  17     1555   1555  2.34  
LINK        MG    MG A 168                 OG1 THR A  35     1555   1555  2.31  
LINK        MG    MG A 168                 O2G GNP A 167     1555   1555  2.35  
LINK        MG    MG A 168                 O2B GNP A 167     1555   1555  2.33  
LINK        MG    MG A 168                 O   HOH A 246     1555   1555  2.47  
LINK        MG    MG A 168                 O   HOH A 205     1555   5675  2.32  
SITE     1 AC1  5 SER A  17  THR A  35  GNP A 167  HOH A 205                    
SITE     2 AC1  5 HOH A 246                                                     
SITE     1 AC2 27 ARG A  12  GLY A  13  VAL A  14  GLY A  15                    
SITE     2 AC2 27 LYS A  16  SER A  17  ALA A  18  PHE A  28                    
SITE     3 AC2 27 VAL A  29  ASP A  30  GLU A  31  PRO A  34                    
SITE     4 AC2 27 THR A  35  GLY A  60  ASN A 116  LYS A 117                    
SITE     5 AC2 27 ASP A 119  LEU A 120  SER A 145  ALA A 146                    
SITE     6 AC2 27 LYS A 147   MG A 168  HOH A 205  HOH A 246                    
SITE     7 AC2 27 HOH A 276  HOH A 313  HOH A 365                               
CRYST1   40.400   40.400  162.200  90.00  90.00 120.00 P 32 2 1      6          
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      0.024752  0.014291  0.000000        0.00000                         
SCALE2      0.000000  0.028582  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006165        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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