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Database: PDB
Entry: 1NVV
LinkDB: 1NVV
Original site: 1NVV 
HEADER    SIGNALING PROTEIN                       04-FEB-03   1NVV              
TITLE     STRUCTURAL EVIDENCE FOR FEEDBACK ACTIVATION BY RASGTP OF              
TITLE    2 THE RAS-SPECIFIC NUCLEOTIDE EXCHANGE FACTOR SOS                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSFORMING PROTEIN P21/H-RAS-1;                          
COMPND   3 CHAIN: Q;                                                            
COMPND   4 FRAGMENT: RESIDUES 1-166;                                            
COMPND   5 SYNONYM: C-H-RAS;                                                    
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: TRANSFORMING PROTEIN P21/H-RAS-1;                          
COMPND  10 CHAIN: R;                                                            
COMPND  11 FRAGMENT: RESIDUES 1-166;                                            
COMPND  12 SYNONYM: C-H-RAS;                                                    
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: SON OF SEVENLESS PROTEIN HOMOLOG 1;                        
COMPND  16 CHAIN: S;                                                            
COMPND  17 FRAGMENT: RESIDUES 566-1046, INCLUDING RAS GUANINE                   
COMPND  18 NUCLEOTIDE EXCHANGE FACTOR FRAGMENT;                                 
COMPND  19 SYNONYM: SOS-1;                                                      
COMPND  20 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 OR HRAS1;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: P-PROEXHT;                                
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: HRAS OR HRAS1;                                                 
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: P-PROEXHT;                                
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 GENE: SOS1;                                                          
SOURCE  26 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  28 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: P-PROEXHT                                 
KEYWDS    PROTO-ONCOGENE, GTP-BINDING, GUANINE-NUCLEOTIDE RELEASING             
KEYWDS   2 FACTOR, SIGNALING PROTEIN                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.M.MARGARIT,H.SONDERMANN,B.E.HALL,B.NAGAR,A.HOELZ,                   
AUTHOR   2 M.PIRRUCCELLO,D.BAR-SAGI,J.KURIYAN                                   
REVDAT   2   24-FEB-09 1NVV    1       VERSN                                    
REVDAT   1   01-APR-03 1NVV    0                                                
JRNL        AUTH   S.M.MARGARIT,H.SONDERMANN,B.E.HALL,B.NAGAR,A.HOELZ,          
JRNL        AUTH 2 M.PIRRUCCELLO,D.BAR-SAGI,J.KURIYAN                           
JRNL        TITL   STRUCTURAL EVIDENCE FOR FEEDBACK ACTIVATION BY               
JRNL        TITL 2 RASGTP OF THE RAS-SPECIFIC NUCLEOTIDE EXCHANGE               
JRNL        TITL 3 FACTOR SOS                                                   
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 112   685 2003              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   12628188                                                     
JRNL        DOI    10.1016/S0092-8674(03)00149-1                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.18 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.18                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 64.19                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 72440                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5164                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.18                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.32                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 75.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 9201                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2600                       
REMARK   3   BIN FREE R VALUE                    : 0.2970                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 6.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 666                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.011                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6535                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 315                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.71000                                              
REMARK   3    B22 (A**2) : 1.71000                                              
REMARK   3    B33 (A**2) : -3.43000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.26                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.38                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.31                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.26                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.95                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.580 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.640 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.620 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.130 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.37                                                 
REMARK   3   BSOL        : 31.86                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : RASSOS_COMPLEX                                 
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : WATER_REP.TOP                                  
REMARK   3  TOPOLOGY FILE  4   : RASSOS_COMPLEX                                 
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1NVV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAR-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB018262.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-SEP-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.100                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 74722                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.180                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 64.190                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.18                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.35200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1NVU                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.93                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2-1.5 M PHOSPHATE, 100 MM HEPES,       
REMARK 280  PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K             
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       92.08150            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       92.08150            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       89.53800            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       92.08150            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       92.08150            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       89.53800            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       92.08150            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       92.08150            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       89.53800            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       92.08150            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       92.08150            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       89.53800            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       92.08150            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       92.08150            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       89.53800            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       92.08150            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       92.08150            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       89.53800            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       92.08150            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       92.08150            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       89.53800            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       92.08150            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       92.08150            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       89.53800            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 300 REMARK: TWO MOLECULES OF RAS BOUND TO ONE MOLECULE OF SOS, ONE       
REMARK 300 AT THE ACTIVE SITE (CHAINID, R) AND THE OTHER AT A DISTAL SITE       
REMARK 300 (CHAINID, Q). THE DISTAL RAS HAS GTP BOUND TO IT, WHILE THE          
REMARK 300 ACTIVE SITE RAS IS NUCLEOTIDE-FREE.                                  
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: 8560 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 36480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 24-MERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 100180 ANGSTROM**2                        
REMARK 350 SURFACE AREA OF THE COMPLEX: 260130 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -526.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q, S, R                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   5  0.000000  0.000000 -1.000000      179.07600            
REMARK 350   BIOMT1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   6  0.000000  0.000000 -1.000000      179.07600            
REMARK 350   BIOMT1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   7  0.000000  0.000000 -1.000000      179.07600            
REMARK 350   BIOMT1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   8  0.000000  0.000000 -1.000000      179.07600            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC                
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 43610 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 136550 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -270.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q, S, R                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 18540 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 71530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -118.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q, S, R                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      179.07600            
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     ASN S   591                                                      
REMARK 465     MET S   592                                                      
REMARK 465     GLN S   593                                                      
REMARK 465     PRO S   594                                                      
REMARK 465     LYS S   595                                                      
REMARK 465     ALA S   596                                                      
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 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    ILE Q  36      -60.60   -109.19                                   
REMARK 500    GLU Q  63       24.54    -74.44                                   
REMARK 500    ALA Q  64       23.01   -152.61                                   
REMARK 500    LYS Q 117       39.28     73.97                                   
REMARK 500    ARG Q 149       -2.66     80.01                                   
REMARK 500    LYS R  42      116.23   -166.09                                   
REMARK 500    ASP R 119     -152.09   -148.54                                   
REMARK 500    ASP S 620       72.42   -168.40                                   
REMARK 500    TYR S 681      -59.08   -129.43                                   
REMARK 500    HIS S 700       44.20   -142.30                                   
REMARK 500    GLN S 755      -70.99    -59.64                                   
REMARK 500    HIS S 764     -113.68   -119.28                                   
REMARK 500    HIS S 770       56.20    -97.15                                   
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 Q1002  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER Q  17   OG                                                     
REMARK 620 2 THR Q  35   OG1  82.6                                              
REMARK 620 3 GNP Q1001   O2G 171.8  89.9                                        
REMARK 620 4 HOH Q1008   O    92.7  87.9  83.6                                  
REMARK 620 5 GNP Q1001   O2B  91.9 169.6  95.0  83.6                            
REMARK 620 N                    1     2     3     4                             
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 1002                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 R 1003                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 S 1047                
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 S 1048                
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 S 1049                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 Q 1007                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP Q 1001                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1BKD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1NVU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1NVW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1NVX   RELATED DB: PDB                                   
DBREF  1NVV Q    1   166  UNP    P01112   RASH_HUMAN       1    166             
DBREF  1NVV R    1   166  UNP    P01112   RASH_HUMAN       1    166             
DBREF  1NVV S  566  1046  UNP    Q07889   SOS1_HUMAN     566   1046             
SEQADV 1NVV ALA Q   64  UNP  P01112    TYR    64 ENGINEERED                     
SEQRES   1 Q  166  MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA GLY GLY          
SEQRES   2 Q  166  VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN ASN          
SEQRES   3 Q  166  HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP SER          
SEQRES   4 Q  166  TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS LEU          
SEQRES   5 Q  166  LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU ALA SER          
SEQRES   6 Q  166  ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY PHE          
SEQRES   7 Q  166  LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE GLU          
SEQRES   8 Q  166  ASP ILE HIS GLN TYR ARG GLU GLN ILE LYS ARG VAL LYS          
SEQRES   9 Q  166  ASP SER ASP ASP VAL PRO MET VAL LEU VAL GLY ASN LYS          
SEQRES  10 Q  166  CYS ASP LEU ALA ALA ARG THR VAL GLU SER ARG GLN ALA          
SEQRES  11 Q  166  GLN ASP LEU ALA ARG SER TYR GLY ILE PRO TYR ILE GLU          
SEQRES  12 Q  166  THR SER ALA LYS THR ARG GLN GLY VAL GLU ASP ALA PHE          
SEQRES  13 Q  166  TYR THR LEU VAL ARG GLU ILE ARG GLN HIS                      
SEQRES   1 R  166  MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA GLY GLY          
SEQRES   2 R  166  VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN ASN          
SEQRES   3 R  166  HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP SER          
SEQRES   4 R  166  TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS LEU          
SEQRES   5 R  166  LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR SER          
SEQRES   6 R  166  ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY PHE          
SEQRES   7 R  166  LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE GLU          
SEQRES   8 R  166  ASP ILE HIS GLN TYR ARG GLU GLN ILE LYS ARG VAL LYS          
SEQRES   9 R  166  ASP SER ASP ASP VAL PRO MET VAL LEU VAL GLY ASN LYS          
SEQRES  10 R  166  CYS ASP LEU ALA ALA ARG THR VAL GLU SER ARG GLN ALA          
SEQRES  11 R  166  GLN ASP LEU ALA ARG SER TYR GLY ILE PRO TYR ILE GLU          
SEQRES  12 R  166  THR SER ALA LYS THR ARG GLN GLY VAL GLU ASP ALA PHE          
SEQRES  13 R  166  TYR THR LEU VAL ARG GLU ILE ARG GLN HIS                      
SEQRES   1 S  481  GLN MET ARG LEU PRO SER ALA ASP VAL TYR ARG PHE ALA          
SEQRES   2 S  481  GLU PRO ASP SER GLU GLU ASN ILE ILE PHE GLU GLU ASN          
SEQRES   3 S  481  MET GLN PRO LYS ALA GLY ILE PRO ILE ILE LYS ALA GLY          
SEQRES   4 S  481  THR VAL ILE LYS LEU ILE GLU ARG LEU THR TYR HIS MET          
SEQRES   5 S  481  TYR ALA ASP PRO ASN PHE VAL ARG THR PHE LEU THR THR          
SEQRES   6 S  481  TYR ARG SER PHE CYS LYS PRO GLN GLU LEU LEU SER LEU          
SEQRES   7 S  481  ILE ILE GLU ARG PHE GLU ILE PRO GLU PRO GLU PRO THR          
SEQRES   8 S  481  GLU ALA ASP ARG ILE ALA ILE GLU ASN GLY ASP GLN PRO          
SEQRES   9 S  481  LEU SER ALA GLU LEU LYS ARG PHE ARG LYS GLU TYR ILE          
SEQRES  10 S  481  GLN PRO VAL GLN LEU ARG VAL LEU ASN VAL CYS ARG HIS          
SEQRES  11 S  481  TRP VAL GLU HIS HIS PHE TYR ASP PHE GLU ARG ASP ALA          
SEQRES  12 S  481  TYR LEU LEU GLN ARG MET GLU GLU PHE ILE GLY THR VAL          
SEQRES  13 S  481  ARG GLY LYS ALA MET LYS LYS TRP VAL GLU SER ILE THR          
SEQRES  14 S  481  LYS ILE ILE GLN ARG LYS LYS ILE ALA ARG ASP ASN GLY          
SEQRES  15 S  481  PRO GLY HIS ASN ILE THR PHE GLN SER SER PRO PRO THR          
SEQRES  16 S  481  VAL GLU TRP HIS ILE SER ARG PRO GLY HIS ILE GLU THR          
SEQRES  17 S  481  PHE ASP LEU LEU THR LEU HIS PRO ILE GLU ILE ALA ARG          
SEQRES  18 S  481  GLN LEU THR LEU LEU GLU SER ASP LEU TYR ARG ALA VAL          
SEQRES  19 S  481  GLN PRO SER GLU LEU VAL GLY SER VAL TRP THR LYS GLU          
SEQRES  20 S  481  ASP LYS GLU ILE ASN SER PRO ASN LEU LEU LYS MET ILE          
SEQRES  21 S  481  ARG HIS THR THR ASN LEU THR LEU TRP PHE GLU LYS CYS          
SEQRES  22 S  481  ILE VAL GLU THR GLU ASN LEU GLU GLU ARG VAL ALA VAL          
SEQRES  23 S  481  VAL SER ARG ILE ILE GLU ILE LEU GLN VAL PHE GLN GLU          
SEQRES  24 S  481  LEU ASN ASN PHE ASN GLY VAL LEU GLU VAL VAL SER ALA          
SEQRES  25 S  481  MET ASN SER SER PRO VAL TYR ARG LEU ASP HIS THR PHE          
SEQRES  26 S  481  GLU GLN ILE PRO SER ARG GLN LYS LYS ILE LEU GLU GLU          
SEQRES  27 S  481  ALA HIS GLU LEU SER GLU ASP HIS TYR LYS LYS TYR LEU          
SEQRES  28 S  481  ALA LYS LEU ARG SER ILE ASN PRO PRO CYS VAL PRO PHE          
SEQRES  29 S  481  PHE GLY ILE TYR LEU THR ASN ILE LEU LYS THR GLU GLU          
SEQRES  30 S  481  GLY ASN PRO GLU VAL LEU LYS ARG HIS GLY LYS GLU LEU          
SEQRES  31 S  481  ILE ASN PHE SER LYS ARG ARG LYS VAL ALA GLU ILE THR          
SEQRES  32 S  481  GLY GLU ILE GLN GLN TYR GLN ASN GLN PRO TYR CYS LEU          
SEQRES  33 S  481  ARG VAL GLU SER ASP ILE LYS ARG PHE PHE GLU ASN LEU          
SEQRES  34 S  481  ASN PRO MET GLY ASN SER MET GLU LYS GLU PHE THR ASP          
SEQRES  35 S  481  TYR LEU PHE ASN LYS SER LEU GLU ILE GLU PRO ARG ASN          
SEQRES  36 S  481  PRO LYS PRO LEU PRO ARG PHE PRO LYS LYS TYR SER TYR          
SEQRES  37 S  481  PRO LEU LYS SER PRO GLY VAL ARG PRO SER ASN PRO ARG          
HET     MG  Q1002       1                                                       
HET    PO4  R1003       5                                                       
HET    PO4  S1047       5                                                       
HET    PO4  S1048       5                                                       
HET    PO4  S1049       5                                                       
HET    PO4  Q1007       5                                                       
HET    GNP  Q1001      32                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER                      
FORMUL   4   MG    MG 2+                                                        
FORMUL   5  PO4    5(O4 P 3-)                                                   
FORMUL  10  GNP    C10 H17 N6 O13 P3                                            
FORMUL  11  HOH   *315(H2 O)                                                    
HELIX    1   1 GLY Q   15  ASN Q   26  1                                  12    
HELIX    2   2 GLN Q   61  SER Q   65  5                                   5    
HELIX    3   3 MET Q   67  ARG Q   73  1                                   7    
HELIX    4   4 ASN Q   86  LYS Q  104  1                                  19    
HELIX    5   5 GLU Q  126  GLY Q  138  1                                  13    
HELIX    6   6 GLY Q  151  HIS Q  166  1                                  16    
HELIX    7   7 GLY R   15  GLN R   25  1                                  11    
HELIX    8   8 TYR R   64  ALA R   66  5                                   3    
HELIX    9   9 MET R   67  THR R   74  1                                   8    
HELIX   10  10 ASN R   86  ASP R   92  1                                   7    
HELIX   11  11 ASP R   92  LYS R  104  1                                  13    
HELIX   12  12 GLU R  126  GLY R  138  1                                  13    
HELIX   13  13 SER R  145  ARG R  149  5                                   5    
HELIX   14  14 GLY R  151  GLN R  165  1                                  15    
HELIX   15  15 TYR S  575  GLU S  579  5                                   5    
HELIX   16  16 THR S  605  THR S  614  1                                  10    
HELIX   17  17 ASP S  620  TYR S  631  1                                  12    
HELIX   18  18 ARG S  632  PHE S  634  5                                   3    
HELIX   19  19 LYS S  636  GLU S  649  1                                  14    
HELIX   20  20 THR S  656  GLU S  664  1                                   9    
HELIX   21  21 SER S  671  TYR S  681  1                                  11    
HELIX   22  22 TYR S  681  HIS S  700  1                                  20    
HELIX   23  23 PHE S  701  ASP S  707  1                                   7    
HELIX   24  24 ASP S  707  VAL S  721  1                                  15    
HELIX   25  25 GLY S  723  ALA S  743  1                                  21    
HELIX   26  26 HIS S  770  PHE S  774  5                                   5    
HELIX   27  27 HIS S  780  ALA S  798  1                                  19    
HELIX   28  28 VAL S  799  VAL S  799  5                                   1    
HELIX   29  29 GLN S  800  LYS S  811  5                                  12    
HELIX   30  30 ASP S  813  SER S  818  1                                   6    
HELIX   31  31 SER S  818  GLU S  841  1                                  24    
HELIX   32  32 ASN S  844  LEU S  865  1                                  22    
HELIX   33  33 ASN S  867  ASN S  879  1                                  13    
HELIX   34  34 SER S  880  ARG S  885  1                                   6    
HELIX   35  35 LEU S  886  GLN S  892  1                                   7    
HELIX   36  36 PRO S  894  ILE S  922  1                                  29    
HELIX   37  37 PHE S  930  GLY S  943  1                                  14    
HELIX   38  38 PHE S  958  TYR S  974  1                                  17    
HELIX   39  39 GLU S  984  ASN S  993  1                                  10    
HELIX   40  40 MET S 1001  GLU S 1017  1                                  17    
SHEET    1   A 6 GLU Q  37  ILE Q  46  0                                        
SHEET    2   A 6 GLU Q  49  THR Q  58 -1  O  ASP Q  57   N  ASP Q  38           
SHEET    3   A 6 THR Q   2  GLY Q  10  1  N  TYR Q   4   O  ASP Q  54           
SHEET    4   A 6 GLY Q  77  ALA Q  83  1  O  VAL Q  81   N  VAL Q   9           
SHEET    5   A 6 MET Q 111  ASN Q 116  1  O  ASN Q 116   N  PHE Q  82           
SHEET    6   A 6 TYR Q 141  GLU Q 143  1  O  ILE Q 142   N  LEU Q 113           
SHEET    1   B 6 ARG R  41  ILE R  46  0                                        
SHEET    2   B 6 GLU R  49  LEU R  56 -1  O  CYS R  51   N  VAL R  44           
SHEET    3   B 6 GLU R   3  GLY R  10  1  N  TYR R   4   O  LEU R  52           
SHEET    4   B 6 GLY R  77  ALA R  83  1  O  LEU R  79   N  VAL R   9           
SHEET    5   B 6 MET R 111  ASN R 116  1  O  VAL R 114   N  CYS R  80           
SHEET    6   B 6 TYR R 141  THR R 144  1  O  THR R 144   N  GLY R 115           
SHEET    1   C 4 ILE S 586  PHE S 588  0                                        
SHEET    2   C 4 ILE S 601  GLY S 604 -1  O  ALA S 603   N  ILE S 587           
SHEET    3   C 4 LYS S 953  ASN S 957 -1  O  ILE S 956   N  GLY S 604           
SHEET    4   C 4 VAL S 947  ARG S 950 -1  N  LEU S 948   O  LEU S 955           
LINK        MG    MG Q1002                 OG  SER Q  17     1555   1555  2.12  
LINK        MG    MG Q1002                 OG1 THR Q  35     1555   1555  2.11  
LINK        MG    MG Q1002                 O2G GNP Q1001     1555   1555  2.10  
LINK        MG    MG Q1002                 O   HOH Q1008     1555   1555  2.02  
LINK        MG    MG Q1002                 O2B GNP Q1001     1555   1555  2.07  
CISPEP   1 PRO S  924    PRO S  925          0         3.30                     
CISPEP   2 ASN S 1020    PRO S 1021          0        -0.40                     
SITE     1 AC1  4 SER Q  17  THR Q  35  GNP Q1001  HOH Q1008                    
SITE     1 AC2  7 GLY R  13  VAL R  14  GLY R  15  LYS R  16                    
SITE     2 AC2  7 SER R  17  ALA R  59  GLU R  62                               
SITE     1 AC3  6 HOH S  75  HOH S 238  ARG S 625  HIS S 695                    
SITE     2 AC3  6 HIS S 699  HIS S 700                                          
SITE     1 AC4  6 GLU R  63  ARG R 128  GLN R 131  HOH R1038                    
SITE     2 AC4  6 LYS S 814  ARG S 826                                          
SITE     1 AC5  7 HOH S  43  HOH S 210  ARG S 660  TYR S 709                    
SITE     2 AC5  7 ARG S 713  GLU S 716  HIS S 951                               
SITE     1 AC6  3 ASP Q 154  TYR Q 157  ARG Q 161                               
SITE     1 AC7 26 GLY Q  12  GLY Q  13  VAL Q  14  GLY Q  15                    
SITE     2 AC7 26 LYS Q  16  SER Q  17  ALA Q  18  PHE Q  28                    
SITE     3 AC7 26 VAL Q  29  ASP Q  30  GLU Q  31  PRO Q  34                    
SITE     4 AC7 26 THR Q  35  GLY Q  60  GLN Q  61  ASN Q 116                    
SITE     5 AC7 26 LYS Q 117  ASP Q 119  LEU Q 120  SER Q 145                    
SITE     6 AC7 26 ALA Q 146  LYS Q 147   MG Q1002  HOH Q1008                    
SITE     7 AC7 26 HOH Q1023  HOH Q1043                                          
CRYST1  184.163  184.163  179.076  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      0.005430  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005430  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005584        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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