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Database: PDB
Entry: 4DSO
LinkDB: 4DSO
Original site: 4DSO 
HEADER    HYDROLASE                               19-FEB-12   4DSO              
TITLE     SMALL-MOLECULE LIGANDS BIND TO A DISTINCT POCKET IN RAS AND INHIBIT   
TITLE    2 SOS-MEDIATED NUCLEOTIDE EXCHANGE ACTIVITY                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GTPASE KRAS, ISOFORM 2B;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: KRAS 4B, K-RAS 2, KI-RAS, C-K-RAS, C-KI-RAS, GTPASE KRAS, N-
COMPND   5 TERMINALLY PROCESSED;                                                
COMPND   6 EC: 3.6.-.-;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: KRAS, KRAS2, RASK2;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SMALL G-PROTEIN, SIGNALING, HYDROLASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.OH,T.MAURER,L.S.GARRENTON,K.PITTS,D.J.ANDERSON,N.J.SKELTON,         
AUTHOR   2 B.P.FAUBER,B.PAN,S.MALEK,D.STOKOE,M.LUDLAM,K.K.BOWMAN,J.WU,          
AUTHOR   3 A.M.GIANNETTI,M.A.STAROVASNIK,I.MELLMAN,P.K.JACKSON,J.RULDOLPH,      
AUTHOR   4 G.FANG,W.WANG                                                        
REVDAT   3   06-JUN-12 4DSO    1       COMPND DBREF  SEQADV REMARK              
REVDAT   2   18-APR-12 4DSO    1       JRNL                                     
REVDAT   1   04-APR-12 4DSO    0                                                
JRNL        AUTH   T.MAURER,L.S.GARRENTON,A.OH,K.PITTS,D.J.ANDERSON,            
JRNL        AUTH 2 N.J.SKELTON,B.P.FAUBER,B.PAN,S.MALEK,D.STOKOE,M.J.LUDLAM,    
JRNL        AUTH 3 K.K.BOWMAN,J.WU,A.M.GIANNETTI,M.A.STAROVASNIK,I.MELLMAN,     
JRNL        AUTH 4 P.K.JACKSON,J.RUDOLPH,W.WANG,G.FANG                          
JRNL        TITL   SMALL-MOLECULE LIGANDS BIND TO A DISTINCT POCKET IN RAS AND  
JRNL        TITL 2 INHIBIT SOS-MEDIATED NUCLEOTIDE EXCHANGE ACTIVITY.           
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 109  5299 2012              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   22431598                                                     
JRNL        DOI    10.1073/PNAS.1116510109                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.92                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 14782                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.207                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 781                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 25                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.89                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 887                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.89                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2270                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 46                           
REMARK   3   BIN FREE R VALUE                    : 0.2850                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1417                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 48                                      
REMARK   3   SOLVENT ATOMS            : 149                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.08                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.41000                                             
REMARK   3    B22 (A**2) : -0.41000                                             
REMARK   3    B33 (A**2) : 0.61000                                              
REMARK   3    B12 (A**2) : -0.20000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.141         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.129         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.095         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.887         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1487 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):   997 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2011 ; 2.066 ; 1.996       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2428 ; 0.953 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   179 ; 7.500 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    71 ;39.387 ;24.648       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   261 ;14.615 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;20.783 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   222 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1638 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   295 ; 0.005 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   329 ; 0.227 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1121 ; 0.214 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   728 ; 0.178 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):   768 ; 0.086 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   134 ; 0.204 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     2 ; 0.105 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    25 ; 0.231 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    52 ; 0.308 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    14 ; 0.498 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1178 ; 1.200 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   369 ; 0.211 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1443 ; 1.358 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   684 ; 2.084 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   568 ; 2.880 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   448        A   449                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.5910  19.1790   4.5500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0000 T22:   0.0000                                     
REMARK   3      T33:   0.0000 T12:   0.0000                                     
REMARK   3      T13:   0.0000 T23:   0.0000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3018 L22:   6.4875                                     
REMARK   3      L33:   0.8736 L12:  -0.8399                                     
REMARK   3      L13:   0.2515 L23:   2.2513                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1552 S12:  -0.2858 S13:   0.2268                       
REMARK   3      S21:  -0.4001 S22:   0.2020 S23:   0.0300                       
REMARK   3      S31:  -0.3711 S32:   0.0326 S33:  -0.0468                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 5                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   180                          
REMARK   3    RESIDUE RANGE :   A   201        A   201                          
REMARK   3    RESIDUE RANGE :   A   203        A   203                          
REMARK   3    RESIDUE RANGE :   A   204        A   204                          
REMARK   3    RESIDUE RANGE :   A   301        A   422                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.6410   9.9230   0.1420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1602 T22:  -0.1241                                     
REMARK   3      T33:  -0.1587 T12:   0.0134                                     
REMARK   3      T13:  -0.0318 T23:  -0.0184                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3176 L22:   4.4417                                     
REMARK   3      L33:   2.7320 L12:   0.9070                                     
REMARK   3      L13:   0.6767 L23:   0.7526                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0434 S12:  -0.2859 S13:   0.3336                       
REMARK   3      S21:   0.2113 S22:  -0.0184 S23:  -0.0459                       
REMARK   3      S31:  -0.1016 S32:   0.1147 S33:   0.0618                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   423        A   447                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.2190   6.2470  -0.5870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0846 T22:  -0.0692                                     
REMARK   3      T33:   0.0067 T12:   0.0409                                     
REMARK   3      T13:  -0.0254 T23:  -0.0179                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8309 L22:   1.8630                                     
REMARK   3      L33:   0.9806 L12:   0.5690                                     
REMARK   3      L13:   1.1152 L23:   0.3902                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0781 S12:  -0.2659 S13:   0.3223                       
REMARK   3      S21:   0.0436 S22:  -0.0957 S23:   0.1188                       
REMARK   3      S31:  -0.0867 S32:   0.0456 S33:   0.1738                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4DSO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-FEB-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB070732.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JAN-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97945                            
REMARK 200  MONOCHROMATOR                  : SIDE SCATTERING BENT CUBE-ROOT I   
REMARK 200                                   -BEAM SINGLE CRYSTAL; ASYMMETRIC   
REMARK 200                                   CUT 4.965 DEGS                     
REMARK 200  OPTICS                         : SIDE SCATTERING BENT CUBE-ROOT I   
REMARK 200                                   -BEAM SINGLE CRYSTAL; ASYMMETRIC   
REMARK 200                                   CUT 4.965 DEGS                     
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14782                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.99                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.15800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 UL + 0.2 UL DROPS CONTAINING 40      
REMARK 280  MG/ML KRAS, 0.1 M TRISCL, 25% POLYETHYLENE GLYCOL 4000, 0.2 M       
REMARK 280  NAOAC, 2% BENZAMIDINE-HCL, PH 8.5, VAPOR DIFFUSION, SITTING DROP,   
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.68700            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       22.91330            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       25.91633            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       39.68700            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       22.91330            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       25.91633            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       39.68700            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       22.91330            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       25.91633            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       45.82660            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       51.83267            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       45.82660            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       51.83267            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       45.82660            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       51.83267            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 A 431  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 A     0                                                      
REMARK 465     SER A   181                                                      
REMARK 465     LYS A   182                                                      
REMARK 465     THR A   183                                                      
REMARK 465     LYS A   184                                                      
REMARK 465     CYS A   185                                                      
REMARK 465     VAL A   186                                                      
REMARK 465     ILE A   187                                                      
REMARK 465     MET A   188                                                      
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     LYS A 175    CG   CD   CE   NZ                                   
REMARK 470     LYS A 176    CG   CD   CE   NZ                                   
REMARK 470     LYS A 177    CG   CD   CE   NZ                                   
REMARK 470     LYS A 178    CG   CD   CE   NZ                                   
REMARK 470     LYS A 179    CG   CD   CE   NZ                                   
REMARK 470     LYS A 180    CG   CD   CE   NZ                                   
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   OD1  ASP A    30     O    HOH A   347              2.00            
REMARK 500   O    MET A    67     O    HOH A   388              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   327     O    HOH A   379     3555     1.01            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG A  73   NE    ARG A  73   CZ      0.150                       
REMARK 500    ARG A  73   CZ    ARG A  73   NH1     0.114                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  73   NE  -  CZ  -  NH1 ANGL. DEV. =   7.7 DEGREES          
REMARK 500    ARG A  73   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  37      108.43   -171.59                                   
REMARK 500    GLU A  62     -144.20     81.50                                   
REMARK 500    GLU A  63      -59.35     61.56                                   
REMARK 500    TYR A  64      178.19    -39.05                                   
REMARK 500    SER A  65       -9.93    106.23                                   
REMARK 500    ALA A  66      -71.29    -96.43                                   
REMARK 500    LYS A 117       33.43     74.55                                   
REMARK 500    ARG A 149       -0.11     75.44                                   
REMARK 500    ASP A 173     -146.62     54.52                                   
REMARK 500    LYS A 175     -158.70   -155.63                                   
REMARK 500    LYS A 176      -61.83     80.32                                   
REMARK 500    LYS A 177      -67.88   -105.38                                   
REMARK 500    LYS A 178      175.70     76.89                                   
REMARK 500    LYS A 179      -89.34   -168.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU A   62     GLU A   63                 -149.82                    
REMARK 500 TYR A   64     SER A   65                 -143.96                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 202  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GSP A 201   O3G                                                    
REMARK 620 2 SER A  17   OG  172.6                                              
REMARK 620 3 HOH A 322   O    96.6  86.8                                        
REMARK 620 4 GSP A 201   O2B  96.7  89.7  91.5                                  
REMARK 620 5 THR A  35   OG1  90.2  83.3  88.0 173.0                            
REMARK 620 6 HOH A 366   O    87.3  89.0 175.6  90.0  90.0                      
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 GSP A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 204                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4DSN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DST   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DSU   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE MATCHES UNIPROT ENTRY P01116, ISOFORM 2B WITH           
REMARK 999 IDENTIFIER P01116-2.                                                 
DBREF  4DSO A    2   188  UNP    P01116   RASK_HUMAN       2    188             
SEQADV 4DSO GLY A    0  UNP  P01116              EXPRESSION TAG                 
SEQADV 4DSO SER A    1  UNP  P01116              EXPRESSION TAG                 
SEQADV 4DSO ASP A   12  UNP  P01116    GLY    12 ENGINEERED MUTATION            
SEQRES   1 A  189  GLY SER THR GLU TYR LYS LEU VAL VAL VAL GLY ALA ASP          
SEQRES   2 A  189  GLY VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN          
SEQRES   3 A  189  ASN HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP          
SEQRES   4 A  189  SER TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS          
SEQRES   5 A  189  LEU LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR          
SEQRES   6 A  189  SER ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY          
SEQRES   7 A  189  PHE LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE          
SEQRES   8 A  189  GLU ASP ILE HIS HIS TYR ARG GLU GLN ILE LYS ARG VAL          
SEQRES   9 A  189  LYS ASP SER GLU ASP VAL PRO MET VAL LEU VAL GLY ASN          
SEQRES  10 A  189  LYS CYS ASP LEU PRO SER ARG THR VAL ASP THR LYS GLN          
SEQRES  11 A  189  ALA GLN ASP LEU ALA ARG SER TYR GLY ILE PRO PHE ILE          
SEQRES  12 A  189  GLU THR SER ALA LYS THR ARG GLN GLY VAL ASP ASP ALA          
SEQRES  13 A  189  PHE TYR THR LEU VAL ARG GLU ILE ARG LYS HIS LYS GLU          
SEQRES  14 A  189  LYS MET SER LYS ASP GLY LYS LYS LYS LYS LYS LYS SER          
SEQRES  15 A  189  LYS THR LYS CYS VAL ILE MET                                  
HET    GSP  A 201      32                                                       
HET     MG  A 202       1                                                       
HET    BEN  A 203       9                                                       
HET    GOL  A 204       6                                                       
HETNAM     GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     BEN BENZAMIDINE                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  GSP    C10 H16 N5 O13 P3 S                                          
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  BEN    C7 H8 N2                                                     
FORMUL   5  GOL    C3 H8 O3                                                     
FORMUL   6  HOH   *149(H2 O)                                                    
HELIX    1   1 GLY A   15  ASN A   26  1                                  12    
HELIX    2   2 MET A   67  GLY A   75  1                                   9    
HELIX    3   3 ASN A   86  LYS A  104  1                                  19    
HELIX    4   4 ASP A  126  GLY A  138  1                                  13    
HELIX    5   5 GLY A  151  ASP A  173  1                                  23    
SHEET    1   A 6 GLU A  37  ILE A  46  0                                        
SHEET    2   A 6 GLU A  49  THR A  58 -1  O  CYS A  51   N  VAL A  44           
SHEET    3   A 6 THR A   2  VAL A   9  1  N  VAL A   8   O  LEU A  56           
SHEET    4   A 6 GLY A  77  ALA A  83  1  O  LEU A  79   N  VAL A   9           
SHEET    5   A 6 MET A 111  ASN A 116  1  O  VAL A 114   N  CYS A  80           
SHEET    6   A 6 PHE A 141  GLU A 143  1  O  ILE A 142   N  LEU A 113           
LINK         O3G GSP A 201                MG    MG A 202     1555   1555  1.85  
LINK         OG  SER A  17                MG    MG A 202     1555   1555  1.96  
LINK        MG    MG A 202                 O   HOH A 322     1555   1555  2.04  
LINK         O2B GSP A 201                MG    MG A 202     1555   1555  2.13  
LINK         OG1 THR A  35                MG    MG A 202     1555   1555  2.15  
LINK        MG    MG A 202                 O   HOH A 366     1555   1555  2.27  
SITE     1 AC1 28 ASP A  12  GLY A  13  VAL A  14  GLY A  15                    
SITE     2 AC1 28 LYS A  16  SER A  17  ALA A  18  PHE A  28                    
SITE     3 AC1 28 VAL A  29  ASP A  30  GLU A  31  TYR A  32                    
SITE     4 AC1 28 THR A  35  GLY A  60  ASN A 116  LYS A 117                    
SITE     5 AC1 28 ASP A 119  LEU A 120  SER A 145  ALA A 146                    
SITE     6 AC1 28 LYS A 147   MG A 202  HOH A 322  HOH A 347                    
SITE     7 AC1 28 HOH A 366  HOH A 419  HOH A 429  HOH A 436                    
SITE     1 AC2  5 SER A  17  THR A  35  GSP A 201  HOH A 322                    
SITE     2 AC2  5 HOH A 366                                                     
SITE     1 AC3  9 LEU A   6  SER A  39  ARG A  41  ASP A  54                    
SITE     2 AC3  9 LEU A  56  THR A  74  CYS A 118  HOH A 316                    
SITE     3 AC3  9 HOH A 317                                                     
SITE     1 AC4  7 GLU A  62  ARG A  68  ASP A  92  HIS A  95                    
SITE     2 AC4  7 TYR A  96  GLN A  99  HOH A 384                               
CRYST1   79.374   79.374   77.749  90.00  90.00 120.00 H 3           9          
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      0.012599  0.007274  0.000000        0.00000                         
SCALE2      0.000000  0.014548  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012862        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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