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Database: PDB
Entry: 4URW
LinkDB: 4URW
Original site: 4URW 
HEADER    SIGNALING PROTEIN                       02-JUL-14   4URW              
TITLE     THE CRYSTAL STRUCTURE OF H-RAS AND SOS IN COMPLEX WITH LIGANDS        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GTPASE HRAS;                                               
COMPND   3 CHAIN: R;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1-166;                                        
COMPND   5 SYNONYM: H-RAS-1, HA-RAS, TRANSFORMING PROTEIN P21, C-H-RAS,         
COMPND   6  P21RAS, H-RAS;                                                      
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: SON OF SEVENLESS HOMOLOG 1;                                
COMPND  10 CHAIN: S;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 564-1049;                                     
COMPND  12 SYNONYM: SOS-1, SON OF SEVENLESS-1;                                  
COMPND  13 ENGINEERED: YES                                                      
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;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SIGNALING PROTEIN                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.J.G.WINTER,M.ANDERSON,K.BLADES,C.BRASSINGTON,A.L.BREEZE,C.CHRESTA,  
AUTHOR   2 K.EMBREY,G.FAIRLEY,P.FAULDER,M.R.V.FINLAY,J.G.KETTLE,T.NOWAK,        
AUTHOR   3 R.OVERMAN,S.J.PATEL,P.PERKINS,L.SPADOLA,J.TART,J.TUCKER,G.WRIGLEY    
REVDAT   2   25-MAR-15 4URW    1       JRNL                                     
REVDAT   1   04-MAR-15 4URW    0                                                
JRNL        AUTH   J.WINTER,M.ANDERSON,K.BLADES,C.CHRESTA,K.J.EMBREY,G.FAIRLEY, 
JRNL        AUTH 2 P.FAULDER,M.R.V.FINLAY,J.G.KETTLE,T.NOWAK,R.OVERMAN,         
JRNL        AUTH 3 S.J.PATEL,P.PERKINS,L.SPADOLA,J.TART,J.A.TUCKER,G.WRIGLEY    
JRNL        TITL   SMALL MOLECULE BINDING SITES ON THE RAS:SOS COMPLEX CAN BE   
JRNL        TITL 2 EXPLOITED FOR INHIBITION OF RAS ACTIVATION.                  
JRNL        REF    J.MED.CHEM.                   V.  58  2265 2015              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   25695162                                                     
JRNL        DOI    10.1021/JM501660T                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.76 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.5                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.76                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 63.39                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.57                          
REMARK   3   NUMBER OF REFLECTIONS             : 29346                          
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)  : 0.1842                         
REMARK   3   R VALUE            (WORKING SET)  : 0.1818                         
REMARK   3   FREE R VALUE                      : 0.2302                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.08                           
REMARK   3   FREE R VALUE TEST SET COUNT       : 1491                           
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               : 15                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.76                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.86                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.57                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2728                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2158                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2578                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2109                   
REMARK   3   BIN FREE R VALUE                        : 0.2963                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.50                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 150                      
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            : 5058                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 22                                      
REMARK   3   SOLVENT ATOMS            : 200                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 61.79                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.16                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.5016                                              
REMARK   3    B22 (A**2) : -0.5016                                              
REMARK   3    B33 (A**2) : 1.0032                                               
REMARK   3    B12 (A**2) : 0.0000                                               
REMARK   3    B13 (A**2) : 0.0000                                               
REMARK   3    B23 (A**2) : 0.0000                                               
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.295               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.404               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.266               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.9328                        
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.8951                        
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 10196  ; 2.00   ; HARMONIC            
REMARK   3    BOND ANGLES               : 18435  ; 2.00   ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2256   ; 2.00   ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 143    ; 2.00   ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1455   ; 5.00   ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 10196  ; 20.00  ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.00   ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 674    ; 5.00   ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 11310  ; 4.00   ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.009                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.01                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.04                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 16.72                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4URW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-JUL-14.                  
REMARK 100 THE PDBE ID CODE IS EBI-61147.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-AUG-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29350                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.76                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 119.77                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.7                                
REMARK 200  R MERGE                    (I) : 0.10                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.70                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.76                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.2                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.50                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.30                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1BKD                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.2M SODIUM FORMATE, 2% DMSO             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 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   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z                                                 
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
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  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  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        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       74.70550            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       74.70550            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      100.17200            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       74.70550            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       74.70550            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000      100.17200            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       74.70550            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       74.70550            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000      100.17200            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       74.70550            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       74.70550            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000      100.17200            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       74.70550            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       74.70550            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000      100.17200            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       74.70550            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       74.70550            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      100.17200            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       74.70550            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       74.70550            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000      100.17200            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       74.70550            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       74.70550            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      100.17200            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28890 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.5 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: R, S                                  
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH S3035   LIES ON A SPECIAL POSITION.                         
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     MET R   -18                                                      
REMARK 465     HIS R   -17                                                      
REMARK 465     HIS R   -16                                                      
REMARK 465     HIS R   -15                                                      
REMARK 465     HIS R   -14                                                      
REMARK 465     HIS R   -13                                                      
REMARK 465     HIS R   -12                                                      
REMARK 465     GLY R   -11                                                      
REMARK 465     GLY R   -10                                                      
REMARK 465     GLY R    -9                                                      
REMARK 465     GLU R    -8                                                      
REMARK 465     ASN R    -7                                                      
REMARK 465     LEU R    -6                                                      
REMARK 465     TYR R    -5                                                      
REMARK 465     PHE R    -4                                                      
REMARK 465     GLN R    -3                                                      
REMARK 465     GLY R    -2                                                      
REMARK 465     SER R    -1                                                      
REMARK 465     MET S   563                                                      
REMARK 465     GLU S   564                                                      
REMARK 465     GLU S   565                                                      
REMARK 465     GLU S   654                                                      
REMARK 465     PRO S   655                                                      
REMARK 465     THR S   656                                                      
REMARK 465     GLU S   657                                                      
REMARK 465     ALA S   658                                                      
REMARK 465     ASP S   659                                                      
REMARK 465     ARG S   660                                                      
REMARK 465     ILE S   661                                                      
REMARK 465     ALA S   662                                                      
REMARK 465     ILE S   663                                                      
REMARK 465     GLU S   664                                                      
REMARK 465     ASN S   665                                                      
REMARK 465     GLY S   666                                                      
REMARK 465     ASP S   667                                                      
REMARK 465     GLN S   668                                                      
REMARK 465     PRO S   669                                                      
REMARK 465     ARG S   744                                                      
REMARK 465     ASP S   745                                                      
REMARK 465     ASN S   746                                                      
REMARK 465     GLY S   747                                                      
REMARK 465     PRO S   748                                                      
REMARK 465     GLY S   749                                                      
REMARK 465     HIS S   750                                                      
REMARK 465     ASN S   751                                                      
REMARK 465     ILE S   752                                                      
REMARK 465     THR S   753                                                      
REMARK 465     ARG S  1046                                                      
REMARK 465     PRO S  1047                                                      
REMARK 465     GLY S  1048                                                      
REMARK 465     THR S  1049                                                      
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     HIS R   0    CG   ND1  CD2  CE1  NE2                             
REMARK 470     HIS R  27    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN S 566    CG   CD   OE1  NE2                                  
REMARK 470     LEU S 670    N    CA   CB   CG   CD1  CD2                        
REMARK 470     GLU S 673    CG   CD   OE1  OE2                                  
REMARK 470     LEU S 674    CG   CD1  CD2                                       
REMARK 470     LYS S 675    CG   CD   CE   NZ                                   
REMARK 470     LYS S 679    CG   CD   CE   NZ                                   
REMARK 470     LYS S 724    CG   CD   CE   NZ                                   
REMARK 470     LYS S 727    CG   CD   CE   NZ                                   
REMARK 470     LYS S 735    CE   NZ                                             
REMARK 470     ILE S 742    CG1  CG2  CD1                                       
REMARK 470     LYS S 899    CE   NZ                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN R  61       31.52    -99.08                                   
REMARK 500    ASP R 108       75.20   -118.63                                   
REMARK 500    TYR S 681      -61.50   -131.71                                   
REMARK 500    ALA S 725      -37.46     96.26                                   
REMARK 500    HIS S 764     -110.11   -115.22                                   
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 S3125        DISTANCE =  5.60 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DXO S2046                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4URU   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF H-RAS AND SOS IN COMPLEX                   
REMARK 900  WITH LIGANDS                                                        
REMARK 900 RELATED ID: 4URV   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF H-RAS AND SOS IN COMPLEX                   
REMARK 900  WITH LIGANDS                                                        
REMARK 900 RELATED ID: 4URX   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF H-RAS AND SOS IN COMPLEX                   
REMARK 900  WITH LIGANDS                                                        
REMARK 900 RELATED ID: 4URY   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF H-RAS AND SOS IN COMPLEX                   
REMARK 900  WITH LIGANDS                                                        
REMARK 900 RELATED ID: 4URZ   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF H-RAS AND SOS IN COMPLEX                   
REMARK 900  WITH LIGANDS                                                        
REMARK 900 RELATED ID: 4US0   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF H-RAS AND SOS IN COMPLEX                   
REMARK 900  WITH LIGANDS                                                        
REMARK 900 RELATED ID: 4US1   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF H-RAS AND SOS IN COMPLEX                   
REMARK 900  WITH LIGANDS                                                        
REMARK 900 RELATED ID: 4US2   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF H-RAS AND SOS IN COMPLEX                   
REMARK 900  WITH LIGANDS                                                        
DBREF  4URW R    1   166  UNP    P01112   RASH_HUMAN       1    166             
DBREF  4URW S  564  1049  UNP    Q07889   SOS1_HUMAN     564   1049             
SEQADV 4URW MET R  -18  UNP  P01112              EXPRESSION TAG                 
SEQADV 4URW HIS R  -17  UNP  P01112              EXPRESSION TAG                 
SEQADV 4URW HIS R  -16  UNP  P01112              EXPRESSION TAG                 
SEQADV 4URW HIS R  -15  UNP  P01112              EXPRESSION TAG                 
SEQADV 4URW HIS R  -14  UNP  P01112              EXPRESSION TAG                 
SEQADV 4URW HIS R  -13  UNP  P01112              EXPRESSION TAG                 
SEQADV 4URW HIS R  -12  UNP  P01112              EXPRESSION TAG                 
SEQADV 4URW GLY R  -11  UNP  P01112              EXPRESSION TAG                 
SEQADV 4URW GLY R  -10  UNP  P01112              EXPRESSION TAG                 
SEQADV 4URW GLY R   -9  UNP  P01112              EXPRESSION TAG                 
SEQADV 4URW GLU R   -8  UNP  P01112              EXPRESSION TAG                 
SEQADV 4URW ASN R   -7  UNP  P01112              EXPRESSION TAG                 
SEQADV 4URW LEU R   -6  UNP  P01112              EXPRESSION TAG                 
SEQADV 4URW TYR R   -5  UNP  P01112              EXPRESSION TAG                 
SEQADV 4URW PHE R   -4  UNP  P01112              EXPRESSION TAG                 
SEQADV 4URW GLN R   -3  UNP  P01112              EXPRESSION TAG                 
SEQADV 4URW GLY R   -2  UNP  P01112              EXPRESSION TAG                 
SEQADV 4URW SER R   -1  UNP  P01112              EXPRESSION TAG                 
SEQADV 4URW HIS R    0  UNP  P01112              EXPRESSION TAG                 
SEQADV 4URW MET S  563  UNP  Q07889              EXPRESSION TAG                 
SEQRES   1 R  185  MET HIS HIS HIS HIS HIS HIS GLY GLY GLY GLU ASN LEU          
SEQRES   2 R  185  TYR PHE GLN GLY SER HIS MET THR GLU TYR LYS LEU VAL          
SEQRES   3 R  185  VAL VAL GLY ALA GLY GLY VAL GLY LYS SER ALA LEU THR          
SEQRES   4 R  185  ILE GLN LEU ILE GLN ASN HIS PHE VAL ASP GLU TYR ASP          
SEQRES   5 R  185  PRO THR ILE GLU ASP SER TYR ARG LYS GLN VAL VAL ILE          
SEQRES   6 R  185  ASP GLY GLU THR CYS LEU LEU ASP ILE LEU ASP THR ALA          
SEQRES   7 R  185  GLY GLN GLU GLU TYR SER ALA MET ARG ASP GLN TYR MET          
SEQRES   8 R  185  ARG THR GLY GLU GLY PHE LEU CYS VAL PHE ALA ILE ASN          
SEQRES   9 R  185  ASN THR LYS SER PHE GLU ASP ILE HIS GLN TYR ARG GLU          
SEQRES  10 R  185  GLN ILE LYS ARG VAL LYS ASP SER ASP ASP VAL PRO MET          
SEQRES  11 R  185  VAL LEU VAL GLY ASN LYS CYS ASP LEU ALA ALA ARG THR          
SEQRES  12 R  185  VAL GLU SER ARG GLN ALA GLN ASP LEU ALA ARG SER TYR          
SEQRES  13 R  185  GLY ILE PRO TYR ILE GLU THR SER ALA LYS THR ARG GLN          
SEQRES  14 R  185  GLY VAL GLU ASP ALA PHE TYR THR LEU VAL ARG GLU ILE          
SEQRES  15 R  185  ARG GLN HIS                                                  
SEQRES   1 S  487  MET GLU GLU GLN MET ARG LEU PRO SER ALA ASP VAL TYR          
SEQRES   2 S  487  ARG PHE ALA GLU PRO ASP SER GLU GLU ASN ILE ILE PHE          
SEQRES   3 S  487  GLU GLU ASN MET GLN PRO LYS ALA GLY ILE PRO ILE ILE          
SEQRES   4 S  487  LYS ALA GLY THR VAL ILE LYS LEU ILE GLU ARG LEU THR          
SEQRES   5 S  487  TYR HIS MET TYR ALA ASP PRO ASN PHE VAL ARG THR PHE          
SEQRES   6 S  487  LEU THR THR TYR ARG SER PHE CYS LYS PRO GLN GLU LEU          
SEQRES   7 S  487  LEU SER LEU ILE ILE GLU ARG PHE GLU ILE PRO GLU PRO          
SEQRES   8 S  487  GLU PRO THR GLU ALA ASP ARG ILE ALA ILE GLU ASN GLY          
SEQRES   9 S  487  ASP GLN PRO LEU SER ALA GLU LEU LYS ARG PHE ARG LYS          
SEQRES  10 S  487  GLU TYR ILE GLN PRO VAL GLN LEU ARG VAL LEU ASN VAL          
SEQRES  11 S  487  CYS ARG HIS TRP VAL GLU HIS HIS PHE TYR ASP PHE GLU          
SEQRES  12 S  487  ARG ASP ALA TYR LEU LEU GLN ARG MET GLU GLU PHE ILE          
SEQRES  13 S  487  GLY THR VAL ARG GLY LYS ALA MET LYS LYS TRP VAL GLU          
SEQRES  14 S  487  SER ILE THR LYS ILE ILE GLN ARG LYS LYS ILE ALA ARG          
SEQRES  15 S  487  ASP ASN GLY PRO GLY HIS ASN ILE THR PHE GLN SER SER          
SEQRES  16 S  487  PRO PRO THR VAL GLU TRP HIS ILE SER ARG PRO GLY HIS          
SEQRES  17 S  487  ILE GLU THR PHE ASP LEU LEU THR LEU HIS PRO ILE GLU          
SEQRES  18 S  487  ILE ALA ARG GLN LEU THR LEU LEU GLU SER ASP LEU TYR          
SEQRES  19 S  487  ARG ALA VAL GLN PRO SER GLU LEU VAL GLY SER VAL TRP          
SEQRES  20 S  487  THR LYS GLU ASP LYS GLU ILE ASN SER PRO ASN LEU LEU          
SEQRES  21 S  487  LYS MET ILE ARG HIS THR THR ASN LEU THR LEU TRP PHE          
SEQRES  22 S  487  GLU LYS CYS ILE VAL GLU THR GLU ASN LEU GLU GLU ARG          
SEQRES  23 S  487  VAL ALA VAL VAL SER ARG ILE ILE GLU ILE LEU GLN VAL          
SEQRES  24 S  487  PHE GLN GLU LEU ASN ASN PHE ASN GLY VAL LEU GLU VAL          
SEQRES  25 S  487  VAL SER ALA MET ASN SER SER PRO VAL TYR ARG LEU ASP          
SEQRES  26 S  487  HIS THR PHE GLU GLN ILE PRO SER ARG GLN LYS LYS ILE          
SEQRES  27 S  487  LEU GLU GLU ALA HIS GLU LEU SER GLU ASP HIS TYR LYS          
SEQRES  28 S  487  LYS TYR LEU ALA LYS LEU ARG SER ILE ASN PRO PRO CYS          
SEQRES  29 S  487  VAL PRO PHE PHE GLY ILE TYR LEU THR ASN ILE LEU LYS          
SEQRES  30 S  487  THR GLU GLU GLY ASN PRO GLU VAL LEU LYS ARG HIS GLY          
SEQRES  31 S  487  LYS GLU LEU ILE ASN PHE SER LYS ARG ARG LYS VAL ALA          
SEQRES  32 S  487  GLU ILE THR GLY GLU ILE GLN GLN TYR GLN ASN GLN PRO          
SEQRES  33 S  487  TYR CYS LEU ARG VAL GLU SER ASP ILE LYS ARG PHE PHE          
SEQRES  34 S  487  GLU ASN LEU ASN PRO MET GLY ASN SER MET GLU LYS GLU          
SEQRES  35 S  487  PHE THR ASP TYR LEU PHE ASN LYS SER LEU GLU ILE GLU          
SEQRES  36 S  487  PRO ARG ASN PRO LYS PRO LEU PRO ARG PHE PRO LYS LYS          
SEQRES  37 S  487  TYR SER TYR PRO LEU LYS SER PRO GLY VAL ARG PRO SER          
SEQRES  38 S  487  ASN PRO ARG PRO GLY THR                                      
HET    DXO  S2046      22                                                       
HETNAM     DXO 2-(2,6-DIMETHYLPHENYL)-4-(METHYLSULFANYL)-6-                     
HETNAM   2 DXO  (PIPERAZIN-1-YL)-1,3,5-TRIAZINE                                 
FORMUL   3  DXO    C16 H21 N5 S                                                 
FORMUL   4  HOH   *200(H2 O)                                                    
HELIX    1   1 SER R   17  GLN R   25  1                                   9    
HELIX    2   2 ILE R   36  SER R   39  5                                   4    
HELIX    3   3 TYR R   64  ALA R   66  5                                   3    
HELIX    4   4 MET R   67  THR R   74  1                                   8    
HELIX    5   5 ASN R   86  ASP R   92  1                                   7    
HELIX    6   6 ASP R   92  ASP R  105  1                                  14    
HELIX    7   7 GLU R  126  GLY R  138  1                                  13    
HELIX    8   8 GLY R  151  GLN R  165  1                                  15    
HELIX    9   9 TYR S  575  GLU S  579  5                                   5    
HELIX   10  10 THR S  605  THR S  614  1                                  10    
HELIX   11  11 ASP S  620  TYR S  631  1                                  12    
HELIX   12  12 ARG S  632  PHE S  634  5                                   3    
HELIX   13  13 LYS S  636  GLU S  649  1                                  14    
HELIX   14  14 SER S  671  TYR S  681  1                                  11    
HELIX   15  15 TYR S  681  HIS S  700  1                                  20    
HELIX   16  16 PHE S  701  ARG S  706  1                                   6    
HELIX   17  17 ASP S  707  VAL S  721  1                                  15    
HELIX   18  18 MET S  726  ALA S  743  1                                  18    
HELIX   19  19 HIS S  770  PHE S  774  5                                   5    
HELIX   20  20 HIS S  780  ALA S  798  1                                  19    
HELIX   21  21 GLN S  800  LEU S  804  5                                   5    
HELIX   22  22 LEU S  804  LYS S  811  5                                   8    
HELIX   23  23 ASP S  813  SER S  818  1                                   6    
HELIX   24  24 SER S  818  GLU S  841  1                                  24    
HELIX   25  25 ASN S  844  ASN S  866  1                                  23    
HELIX   26  26 ASN S  867  SER S  880  1                                  14    
HELIX   27  27 SER S  880  ARG S  885  1                                   6    
HELIX   28  28 LEU S  886  GLN S  892  1                                   7    
HELIX   29  29 PRO S  894  LEU S  907  1                                  14    
HELIX   30  30 SER S  908  ILE S  922  1                                  15    
HELIX   31  31 PHE S  930  GLY S  943  1                                  14    
HELIX   32  32 PHE S  958  TYR S  974  1                                  17    
HELIX   33  33 GLU S  984  ASN S  993  1                                  10    
HELIX   34  34 MET S 1001  GLU S 1017  1                                  17    
SHEET    1  RA 6 ARG R  41  ILE R  46  0                                        
SHEET    2  RA 6 GLU R  49  ASP R  57 -1  O  GLU R  49   N  ILE R  46           
SHEET    3  RA 6 THR R   2  GLY R  10  1  O  THR R   2   N  LEU R  52           
SHEET    4  RA 6 GLY R  77  ALA R  83  1  O  GLY R  77   N  VAL R   7           
SHEET    5  RA 6 MET R 111  LYS R 117  1  O  VAL R 112   N  CYS R  80           
SHEET    6  RA 6 TYR R 141  SER R 145  1  O  ILE R 142   N  GLY R 115           
SHEET    1  SA 4 ILE S 586  MET S 592  0                                        
SHEET    2  SA 4 PRO S 599  GLY S 604 -1  O  ILE S 600   N  GLU S 589           
SHEET    3  SA 4 LYS S 953  ASN S 957 -1  O  ILE S 956   N  GLY S 604           
SHEET    4  SA 4 VAL S 947  ARG S 950 -1  O  LEU S 948   N  LEU S 955           
CISPEP   1 PRO S  924    PRO S  925          0        -0.77                     
CISPEP   2 ASN S 1020    PRO S 1021          0         4.44                     
SITE     1 AC1  8 MET S 878  TYR S 884  ASP S 887  PHE S 890                    
SITE     2 AC1  8 LYS S 898  LEU S 901  GLU S 902  HIS S 905                    
CRYST1  149.411  149.411  200.344  90.00  90.00  90.00 I 4 2 2      16          
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      0.006693  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006693  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004991        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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