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Database: PDB
Entry: 5WFQ
LinkDB: 5WFQ
Original site: 5WFQ 
HEADER    SIGNALING PROTEIN                       12-JUL-17   5WFQ              
TITLE     LIGAND-BOUND RAS:SOS:RAS COMPLEX                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GTPASE HRAS;                                               
COMPND   3 CHAIN: Q, R;                                                         
COMPND   4 SYNONYM: H-RAS-1,HA-RAS,TRANSFORMING PROTEIN P21,C-H-RAS,P21RAS;     
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: SON OF SEVENLESS HOMOLOG 1;                                
COMPND   8 CHAIN: N;                                                            
COMPND   9 SYNONYM: SOS-1;                                                      
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HRAS, HRAS1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: SOS1;                                                          
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    RAS, SOS, ONCOPROTEIN, PROTEIN-PROTEIN INTERACTION, MAPK, SIGNALING   
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Q.SUN,J.PHAN,M.C.BURNS,S.W.FESIK                                      
REVDAT   1   23-MAY-18 5WFQ    0                                                
JRNL        AUTH   M.C.BURNS,J.E.HOWES,Q.SUN,A.J.LITTLE,D.V.CAMPER,J.R.ABBOTT,  
JRNL        AUTH 2 J.PHAN,T.LEE,A.G.WATERSON,O.W.ROSSANESE,S.W.FESIK            
JRNL        TITL   HIGH-THROUGHPUT SCREENING IDENTIFIES SMALL MOLECULES THAT    
JRNL        TITL 2 BIND TO THE RAS:SOS:RAS COMPLEX AND PERTURB RAS SIGNALING.   
JRNL        REF    ANAL. BIOCHEM.                V. 548    44 2018              
JRNL        REFN                   ISSN 1096-0309                               
JRNL        PMID   29444450                                                     
JRNL        DOI    10.1016/J.AB.2018.01.025                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.26 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.26                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.41                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 68928                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.196                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.880                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1988                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 48.4159 -  5.4443    0.96     4920   145  0.1768 0.1868        
REMARK   3     2  5.4443 -  4.3222    0.97     4805   138  0.1518 0.1511        
REMARK   3     3  4.3222 -  3.7761    0.98     4793   142  0.1420 0.1826        
REMARK   3     4  3.7761 -  3.4309    0.98     4776   139  0.1560 0.1946        
REMARK   3     5  3.4309 -  3.1851    0.99     4760   147  0.1658 0.1795        
REMARK   3     6  3.1851 -  2.9973    0.99     4780   140  0.1787 0.2281        
REMARK   3     7  2.9973 -  2.8472    0.99     4760   142  0.1806 0.2049        
REMARK   3     8  2.8472 -  2.7233    0.99     4772   144  0.1854 0.2387        
REMARK   3     9  2.7233 -  2.6185    0.99     4763   142  0.1838 0.1909        
REMARK   3    10  2.6185 -  2.5281    0.99     4771   137  0.1815 0.1941        
REMARK   3    11  2.5281 -  2.4491    0.99     4756   138  0.1853 0.2110        
REMARK   3    12  2.4491 -  2.3791    0.99     4771   143  0.1920 0.2503        
REMARK   3    13  2.3791 -  2.3164    0.99     4789   147  0.1946 0.2150        
REMARK   3    14  2.3164 -  2.2599    0.99     4724   144  0.2077 0.2443        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.520           
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           6752                                  
REMARK   3   ANGLE     :  1.026           9137                                  
REMARK   3   CHIRALITY :  0.039           1001                                  
REMARK   3   PLANARITY :  0.004           1184                                  
REMARK   3   DIHEDRAL  : 14.927           2596                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5WFQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000228548.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUN-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 68935                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.260                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 9.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.0900                            
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 4NYI                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE, 2.0 M SODIUM       
REMARK 280  FORMATE, PH 4.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K    
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       91.34000            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       91.34000            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       88.68500            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       91.34000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       91.34000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       88.68500            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       91.34000            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       91.34000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       88.68500            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       91.34000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       91.34000            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       88.68500            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       91.34000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       91.34000            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       88.68500            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       91.34000            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       91.34000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       88.68500            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       91.34000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       91.34000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       88.68500            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       91.34000            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       91.34000            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       88.68500            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q, R, N                               
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 N1457  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     GLY Q     0                                                      
REMARK 465     GLY N   565                                                      
REMARK 465     PRO N   594                                                      
REMARK 465     LYS N   595                                                      
REMARK 465     ALA N   596                                                      
REMARK 465     ARG N   744                                                      
REMARK 465     ASP N   745                                                      
REMARK 465     ASN N   746                                                      
REMARK 465     GLY N   747                                                      
REMARK 465     PRO N   748                                                      
REMARK 465     GLY N   749                                                      
REMARK 465     HIS N   750                                                      
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     TYR Q  64    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TRP N 809    O                                                   
REMARK 470     ARG N1026    O                                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH N  1531     O    HOH N  1566              1.86            
REMARK 500   O    HOH R   265     O    HOH R   310              1.87            
REMARK 500   O    HOH R   261     O    HOH R   291              1.87            
REMARK 500   O    HOH R   302     O    HOH R   326              1.90            
REMARK 500   O    HOH N  1589     O    HOH N  1616              1.96            
REMARK 500   O    HOH Q   416     O    HOH Q   417              1.96            
REMARK 500   O    HOH N  1609     O    HOH N  1617              1.96            
REMARK 500   O    HOH N  1578     O    HOH N  1585              1.96            
REMARK 500   O    HOH N  1641     O    HOH N  1653              1.97            
REMARK 500   O    HOH N  1283     O    HOH N  1464              1.97            
REMARK 500   O    HOH N  1243     O    HOH N  1265              1.99            
REMARK 500   O    HOH R   273     O    HOH R   298              1.99            
REMARK 500   O    HOH N  1391     O    HOH N  1552              2.00            
REMARK 500   OE1  GLU N   579     O    HOH N  1201              2.02            
REMARK 500   O    PHE R    28     O    HOH R   201              2.03            
REMARK 500   O    HOH N  1633     O    HOH N  1649              2.04            
REMARK 500   CE1  HIS R    27     NH2  ARG R   149              2.05            
REMARK 500   O    HOH N  1555     O    HOH N  1624              2.06            
REMARK 500   OE2  GLU Q    37     O    HOH Q   301              2.06            
REMARK 500   O    HOH R   286     O    HOH R   312              2.06            
REMARK 500   O    HOH N  1588     O    HOH N  1605              2.09            
REMARK 500   O    HOH N  1253     O    HOH N  1514              2.09            
REMARK 500   O    HOH R   214     O    HOH R   290              2.10            
REMARK 500   O    HOH R   311     O    HOH R   316              2.12            
REMARK 500   O    HOH Q   304     O    HOH Q   400              2.12            
REMARK 500   O    HOH Q   380     O    HOH Q   413              2.12            
REMARK 500   O    HOH N  1280     O    HOH N  1590              2.14            
REMARK 500   O    HOH Q   381     O    HOH Q   415              2.14            
REMARK 500   OE1  GLU N   864     NH2  ARG N  1041              2.15            
REMARK 500   O    HOH Q   395     O    HOH Q   422              2.15            
REMARK 500   O    HOH Q   388     O    HOH Q   413              2.15            
REMARK 500   O    HOH N  1235     O    HOH N  1543              2.16            
REMARK 500   O    HOH N  1546     O    HOH N  1644              2.16            
REMARK 500   OG   SER N   633     O    HOH N  1202              2.16            
REMARK 500   O    HOH Q   351     O    HOH Q   414              2.17            
REMARK 500   ND2  ASN N  1011     O    HOH N  1203              2.17            
REMARK 500   OD2  ASP R   105     O    HOH R   202              2.18            
REMARK 500   OE2  GLU Q    31     O    HOH Q   302              2.18            
REMARK 500   O    HOH N  1408     O    HOH N  1613              2.18            
REMARK 500   OD1  ASP R    92     O    HOH R   203              2.19            
REMARK 500   CE1  HIS R    27     CZ   ARG R   149              2.19            
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    GLU Q  37      115.98   -168.45                                   
REMARK 500    ALA Q 122       68.35    -69.71                                   
REMARK 500    ARG Q 149       -0.91     80.31                                   
REMARK 500    GLN R  25      157.47    -45.67                                   
REMARK 500    HIS R  27      134.62     82.27                                   
REMARK 500    PHE R  28       -6.53     75.42                                   
REMARK 500    ASP R  38       -2.10     79.78                                   
REMARK 500    THR R  58       30.31    -94.70                                   
REMARK 500    GLN N 755      -33.96    118.25                                   
REMARK 500    SER N 756      158.77    162.32                                   
REMARK 500    HIS N 764     -117.54   -120.51                                   
REMARK 500    HIS N 770       56.95    -95.72                                   
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 Q 201  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER Q  17   OG                                                     
REMARK 620 2 THR Q  35   OG1  80.5                                              
REMARK 620 3 GNP Q 202   O1G 173.8  93.6                                        
REMARK 620 4 GNP Q 202   O1B  91.2 170.1  94.4                                  
REMARK 620 5 HOH Q 312   O    89.2  94.5  93.2  90.8                            
REMARK 620 6 HOH Q 339   O    87.8  88.8  90.2  85.4 175.1                      
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 Q 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GNP Q 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5UV N 1101                
DBREF  5WFQ Q    1   166  UNP    P01112   RASH_HUMAN       1    166             
DBREF  5WFQ R    1   166  UNP    P01112   RASH_HUMAN       1    166             
DBREF  5WFQ N  566  1046  UNP    Q07889   SOS1_HUMAN     566   1046             
SEQADV 5WFQ GLY Q    0  UNP  P01112              EXPRESSION TAG                 
SEQADV 5WFQ GLY R    0  UNP  P01112              EXPRESSION TAG                 
SEQADV 5WFQ GLY N  565  UNP  Q07889              EXPRESSION TAG                 
SEQRES   1 Q  167  GLY MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA GLY          
SEQRES   2 Q  167  GLY VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN          
SEQRES   3 Q  167  ASN HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP          
SEQRES   4 Q  167  SER TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS          
SEQRES   5 Q  167  LEU LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR          
SEQRES   6 Q  167  SER ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY          
SEQRES   7 Q  167  PHE LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE          
SEQRES   8 Q  167  GLU ASP ILE HIS GLN TYR ARG GLU GLN ILE LYS ARG VAL          
SEQRES   9 Q  167  LYS ASP SER ASP ASP VAL PRO MET VAL LEU VAL GLY ASN          
SEQRES  10 Q  167  LYS CYS ASP LEU ALA ALA ARG THR VAL GLU SER ARG GLN          
SEQRES  11 Q  167  ALA GLN ASP LEU ALA ARG SER TYR GLY ILE PRO TYR ILE          
SEQRES  12 Q  167  GLU THR SER ALA LYS THR ARG GLN GLY VAL GLU ASP ALA          
SEQRES  13 Q  167  PHE TYR THR LEU VAL ARG GLU ILE ARG GLN HIS                  
SEQRES   1 R  167  GLY MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA GLY          
SEQRES   2 R  167  GLY VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN          
SEQRES   3 R  167  ASN HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP          
SEQRES   4 R  167  SER TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS          
SEQRES   5 R  167  LEU LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR          
SEQRES   6 R  167  SER ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY          
SEQRES   7 R  167  PHE LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE          
SEQRES   8 R  167  GLU ASP ILE HIS GLN TYR ARG GLU GLN ILE LYS ARG VAL          
SEQRES   9 R  167  LYS ASP SER ASP ASP VAL PRO MET VAL LEU VAL GLY ASN          
SEQRES  10 R  167  LYS CYS ASP LEU ALA ALA ARG THR VAL GLU SER ARG GLN          
SEQRES  11 R  167  ALA GLN ASP LEU ALA ARG SER TYR GLY ILE PRO TYR ILE          
SEQRES  12 R  167  GLU THR SER ALA LYS THR ARG GLN GLY VAL GLU ASP ALA          
SEQRES  13 R  167  PHE TYR THR LEU VAL ARG GLU ILE ARG GLN HIS                  
SEQRES   1 N  482  GLY GLN MET ARG LEU PRO SER ALA ASP VAL TYR ARG PHE          
SEQRES   2 N  482  ALA GLU PRO ASP SER GLU GLU ASN ILE ILE PHE GLU GLU          
SEQRES   3 N  482  ASN MET GLN PRO LYS ALA GLY ILE PRO ILE ILE LYS ALA          
SEQRES   4 N  482  GLY THR VAL ILE LYS LEU ILE GLU ARG LEU THR TYR HIS          
SEQRES   5 N  482  MET TYR ALA ASP PRO ASN PHE VAL ARG THR PHE LEU THR          
SEQRES   6 N  482  THR TYR ARG SER PHE CYS LYS PRO GLN GLU LEU LEU SER          
SEQRES   7 N  482  LEU ILE ILE GLU ARG PHE GLU ILE PRO GLU PRO GLU PRO          
SEQRES   8 N  482  THR GLU ALA ASP ARG ILE ALA ILE GLU ASN GLY ASP GLN          
SEQRES   9 N  482  PRO LEU SER ALA GLU LEU LYS ARG PHE ARG LYS GLU TYR          
SEQRES  10 N  482  ILE GLN PRO VAL GLN LEU ARG VAL LEU ASN VAL CYS ARG          
SEQRES  11 N  482  HIS TRP VAL GLU HIS HIS PHE TYR ASP PHE GLU ARG ASP          
SEQRES  12 N  482  ALA TYR LEU LEU GLN ARG MET GLU GLU PHE ILE GLY THR          
SEQRES  13 N  482  VAL ARG GLY LYS ALA MET LYS LYS TRP VAL GLU SER ILE          
SEQRES  14 N  482  THR LYS ILE ILE GLN ARG LYS LYS ILE ALA ARG ASP ASN          
SEQRES  15 N  482  GLY PRO GLY HIS ASN ILE THR PHE GLN SER SER PRO PRO          
SEQRES  16 N  482  THR VAL GLU TRP HIS ILE SER ARG PRO GLY HIS ILE GLU          
SEQRES  17 N  482  THR PHE ASP LEU LEU THR LEU HIS PRO ILE GLU ILE ALA          
SEQRES  18 N  482  ARG GLN LEU THR LEU LEU GLU SER ASP LEU TYR ARG ALA          
SEQRES  19 N  482  VAL GLN PRO SER GLU LEU VAL GLY SER VAL TRP THR LYS          
SEQRES  20 N  482  GLU ASP LYS GLU ILE ASN SER PRO ASN LEU LEU LYS MET          
SEQRES  21 N  482  ILE ARG HIS THR THR ASN LEU THR LEU TRP PHE GLU LYS          
SEQRES  22 N  482  CYS ILE VAL GLU THR GLU ASN LEU GLU GLU ARG VAL ALA          
SEQRES  23 N  482  VAL VAL SER ARG ILE ILE GLU ILE LEU GLN VAL PHE GLN          
SEQRES  24 N  482  GLU LEU ASN ASN PHE ASN GLY VAL LEU GLU VAL VAL SER          
SEQRES  25 N  482  ALA MET ASN SER SER PRO VAL TYR ARG LEU ASP HIS THR          
SEQRES  26 N  482  PHE GLU GLN ILE PRO SER ARG GLN LYS LYS ILE LEU GLU          
SEQRES  27 N  482  GLU ALA HIS GLU LEU SER GLU ASP HIS TYR LYS LYS TYR          
SEQRES  28 N  482  LEU ALA LYS LEU ARG SER ILE ASN PRO PRO CYS VAL PRO          
SEQRES  29 N  482  PHE PHE GLY ILE TYR LEU THR ASN ILE LEU LYS THR GLU          
SEQRES  30 N  482  GLU GLY ASN PRO GLU VAL LEU LYS ARG HIS GLY LYS GLU          
SEQRES  31 N  482  LEU ILE ASN PHE SER LYS ARG ARG LYS VAL ALA GLU ILE          
SEQRES  32 N  482  THR GLY GLU ILE GLN GLN TYR GLN ASN GLN PRO TYR CYS          
SEQRES  33 N  482  LEU ARG VAL GLU SER ASP ILE LYS ARG PHE PHE GLU ASN          
SEQRES  34 N  482  LEU ASN PRO MET GLY ASN SER MET GLU LYS GLU PHE THR          
SEQRES  35 N  482  ASP TYR LEU PHE ASN LYS SER LEU GLU ILE GLU PRO ARG          
SEQRES  36 N  482  ASN PRO LYS PRO LEU PRO ARG PHE PRO LYS LYS TYR SER          
SEQRES  37 N  482  TYR PRO LEU LYS SER PRO GLY VAL ARG PRO SER ASN PRO          
SEQRES  38 N  482  ARG                                                          
HET     MG  Q 201       1                                                       
HET    GNP  Q 202      32                                                       
HET    5UV  N1101      24                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER                      
HETNAM     5UV 7-CHLORANYL-~{N}-(3-CHLORANYL-4-FLUORANYL-PHENYL)-1,2,           
HETNAM   2 5UV  3,4-TETRAHYDROACRIDIN-9-AMINE                                   
FORMUL   4   MG    MG 2+                                                        
FORMUL   5  GNP    C10 H17 N6 O13 P3                                            
FORMUL   6  5UV    C19 H15 CL2 F N2                                             
FORMUL   7  HOH   *708(H2 O)                                                    
HELIX    1 AA1 GLY Q   15  ASN Q   26  1                                  12    
HELIX    2 AA2 GLN Q   61  MET Q   67  5                                   7    
HELIX    3 AA3 ARG Q   68  GLY Q   75  1                                   8    
HELIX    4 AA4 ASN Q   86  ASP Q  105  1                                  20    
HELIX    5 AA5 GLU Q  126  GLY Q  138  1                                  13    
HELIX    6 AA6 GLY Q  151  HIS Q  166  1                                  16    
HELIX    7 AA7 SER R   17  GLN R   25  1                                   9    
HELIX    8 AA8 TYR R   64  ALA R   66  5                                   3    
HELIX    9 AA9 MET R   67  THR R   74  1                                   8    
HELIX   10 AB1 ASN R   86  ASP R   92  1                                   7    
HELIX   11 AB2 ASP R   92  ASP R  105  1                                  14    
HELIX   12 AB3 GLU R  126  GLY R  138  1                                  13    
HELIX   13 AB4 GLY R  151  GLN R  165  1                                  15    
HELIX   14 AB5 TYR N  575  GLU N  579  5                                   5    
HELIX   15 AB6 THR N  605  THR N  614  1                                  10    
HELIX   16 AB7 ASP N  620  TYR N  631  1                                  12    
HELIX   17 AB8 ARG N  632  PHE N  634  5                                   3    
HELIX   18 AB9 LYS N  636  GLU N  649  1                                  14    
HELIX   19 AC1 THR N  656  ASN N  665  1                                  10    
HELIX   20 AC2 SER N  671  TYR N  681  1                                  11    
HELIX   21 AC3 TYR N  681  HIS N  700  1                                  20    
HELIX   22 AC4 PHE N  701  ARG N  706  1                                   6    
HELIX   23 AC5 ASP N  707  THR N  720  1                                  14    
HELIX   24 AC6 MET N  726  ILE N  742  1                                  17    
HELIX   25 AC7 HIS N  770  PHE N  774  5                                   5    
HELIX   26 AC8 HIS N  780  ALA N  798  1                                  19    
HELIX   27 AC9 GLN N  800  VAL N  808  5                                   9    
HELIX   28 AD1 ASP N  813  SER N  818  1                                   6    
HELIX   29 AD2 SER N  818  GLU N  841  1                                  24    
HELIX   30 AD3 ASN N  844  LEU N  865  1                                  22    
HELIX   31 AD4 ASN N  867  ASN N  879  1                                  13    
HELIX   32 AD5 SER N  880  ARG N  885  1                                   6    
HELIX   33 AD6 LEU N  886  ILE N  893  1                                   8    
HELIX   34 AD7 PRO N  894  LEU N  907  1                                  14    
HELIX   35 AD8 SER N  908  ARG N  920  1                                  13    
HELIX   36 AD9 PHE N  930  GLY N  943  1                                  14    
HELIX   37 AE1 PHE N  958  TYR N  974  1                                  17    
HELIX   38 AE2 GLU N  984  ASN N  993  1                                  10    
HELIX   39 AE3 MET N 1001  GLU N 1017  1                                  17    
SHEET    1 AA1 6 GLU Q  37  ILE Q  46  0                                        
SHEET    2 AA1 6 GLU Q  49  THR Q  58 -1  O  ILE Q  55   N  TYR Q  40           
SHEET    3 AA1 6 THR Q   2  VAL Q   9  1  N  LEU Q   6   O  ASP Q  54           
SHEET    4 AA1 6 GLY Q  77  ALA Q  83  1  O  VAL Q  81   N  VAL Q   9           
SHEET    5 AA1 6 MET Q 111  ASN Q 116  1  O  ASN Q 116   N  PHE Q  82           
SHEET    6 AA1 6 TYR Q 141  GLU Q 143  1  O  ILE Q 142   N  LEU Q 113           
SHEET    1 AA2 6 ARG R  41  ILE R  46  0                                        
SHEET    2 AA2 6 GLU R  49  ASP R  57 -1  O  LEU R  53   N  LYS R  42           
SHEET    3 AA2 6 THR R   2  GLY R  10  1  N  LEU R   6   O  ASP R  54           
SHEET    4 AA2 6 GLY R  77  ALA R  83  1  O  VAL R  81   N  VAL R   9           
SHEET    5 AA2 6 MET R 111  LYS R 117  1  O  VAL R 114   N  CYS R  80           
SHEET    6 AA2 6 TYR R 141  SER R 145  1  O  THR R 144   N  LYS R 117           
SHEET    1 AA3 4 ILE N 586  PHE N 588  0                                        
SHEET    2 AA3 4 ILE N 601  GLY N 604 -1  O  ALA N 603   N  ILE N 587           
SHEET    3 AA3 4 LYS N 953  ASN N 957 -1  O  ILE N 956   N  GLY N 604           
SHEET    4 AA3 4 VAL N 947  ARG N 950 -1  N  LEU N 948   O  LEU N 955           
LINK         OG  SER Q  17                MG    MG Q 201     1555   1555  2.09  
LINK         OG1 THR Q  35                MG    MG Q 201     1555   1555  2.10  
LINK        MG    MG Q 201                 O1G GNP Q 202     1555   1555  1.88  
LINK        MG    MG Q 201                 O1B GNP Q 202     1555   1555  2.04  
LINK        MG    MG Q 201                 O   HOH Q 312     1555   1555  2.04  
LINK        MG    MG Q 201                 O   HOH Q 339     1555   1555  2.01  
CISPEP   1 PHE N  754    GLN N  755          0         2.26                     
CISPEP   2 PRO N  924    PRO N  925          0        10.74                     
CISPEP   3 ASN N 1020    PRO N 1021          0         6.22                     
SITE     1 AC1  5 SER Q  17  THR Q  35  GNP Q 202  HOH Q 312                    
SITE     2 AC1  5 HOH Q 339                                                     
SITE     1 AC2 29 GLY Q  12  GLY Q  13  VAL Q  14  GLY Q  15                    
SITE     2 AC2 29 LYS Q  16  SER Q  17  ALA Q  18  PHE Q  28                    
SITE     3 AC2 29 VAL Q  29  ASP Q  30  GLU Q  31  TYR Q  32                    
SITE     4 AC2 29 PRO Q  34  THR Q  35  GLY Q  60  GLN Q  61                    
SITE     5 AC2 29 ASN Q 116  LYS Q 117  ASP Q 119  LEU Q 120                    
SITE     6 AC2 29 SER Q 145  ALA Q 146  LYS Q 147   MG Q 201                    
SITE     7 AC2 29 HOH Q 312  HOH Q 325  HOH Q 327  HOH Q 339                    
SITE     8 AC2 29 HOH Q 357                                                     
SITE     1 AC3  9 VAL N 852  MET N 878  ASN N 879  VAL N 883                    
SITE     2 AC3  9 TYR N 884  LEU N 886  ASP N 887  PHE N 890                    
SITE     3 AC3  9 GLU N 902                                                     
CRYST1  182.680  182.680  177.370  90.00  90.00  90.00 I 4 2 2      32          
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      0.005474  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005474  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005638        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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