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Database: PDB
Entry: 3DDC
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Original site: 3DDC 
HEADER    HYDROLASE/APOPTOSIS                     05-JUN-08   3DDC              
TITLE     CRYSTAL STRUCTURE OF NORE1A IN COMPLEX WITH RAS                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GTPASE HRAS;                                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1-166;                                        
COMPND   5 SYNONYM: TRANSFORMING PROTEIN P21, P21RAS, H-RAS-1, C-H-RAS, HA-RAS; 
COMPND   6 EC: 3.6.5.2;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: RAS ASSOCIATION DOMAIN-CONTAINING FAMILY PROTEIN 5;        
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: RAS BINDING DOMAIN, UNP RESIDUES 200-358;                  
COMPND  13 SYNONYM: NEW RAS EFFECTOR 1, REGULATOR FOR CELL ADHESION AND         
COMPND  14 POLARIZATION ENRICHED IN LYMPHOID TISSUES, RAPL, EFFECTOR PROTEIN    
COMPND  15 NORE1A;                                                              
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 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: HRAS, HRAS1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: CK600K;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PTAC;                                     
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  13 ORGANISM_COMMON: MOUSE;                                              
SOURCE  14 ORGANISM_TAXID: 10090;                                               
SOURCE  15 GENE: RASSF5, NORE1, RAPL;                                           
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PGEX4T1                                   
KEYWDS    ONCOGENE, TUMORSUPPRESSOR, UBIQUITIN FOLD, RAS EFFECTOR, RAP1, H-RAS, 
KEYWDS   2 RASSF1, RASSF5, RAPL, NORE1, GMPPNP, ADAPTOR, APOPTOSIS,             
KEYWDS   3 MICROTUBULES, HYDROLASE-APOPTOSIS COMPLEX, DISEASE MUTATION, GOLGI   
KEYWDS   4 APPARATUS, GTP-BINDING, LIPOPROTEIN, MEMBRANE, METHYLATION,          
KEYWDS   5 NUCLEOTIDE-BINDING, PALMITATE, PRENYLATION, PROTO-ONCOGENE, ANTI-    
KEYWDS   6 ONCOGENE, CELL CYCLE, METAL-BINDING, MICROTUBULE, PHORBOL-ESTER      
KEYWDS   7 BINDING, ZINC-FINGER                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.STIEGLITZ,C.BEE,D.SCHWARZ,O.YILDIZ,A.MOSHNIKOVA,A.KHOKHLATCHEV,     
AUTHOR   2 C.HERRMANN                                                           
REVDAT   5   20-JUL-11 3DDC    1       REMARK                                   
REVDAT   4   13-JUL-11 3DDC    1       VERSN                                    
REVDAT   3   24-FEB-09 3DDC    1       VERSN                                    
REVDAT   2   12-AUG-08 3DDC    1       JRNL                                     
REVDAT   1   15-JUL-08 3DDC    0                                                
JRNL        AUTH   B.STIEGLITZ,C.BEE,D.SCHWARZ,O.YILDIZ,A.MOSHNIKOVA,           
JRNL        AUTH 2 A.KHOKHLATCHEV,C.HERRMANN                                    
JRNL        TITL   NOVEL TYPE OF RAS EFFECTOR INTERACTION ESTABLISHED BETWEEN   
JRNL        TITL 2 TUMOUR SUPPRESSOR NORE1A AND RAS SWITCH II                   
JRNL        REF    EMBO J.                       V.  27  1995 2008              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   18596699                                                     
JRNL        DOI    10.1038/EMBOJ.2008.125                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2                                           
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.59                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 29320                          
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) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1466                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1912                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2320                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 100                          
REMARK   3   BIN FREE R VALUE                    : 0.3590                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2394                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 115                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 30.52                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.05000                                              
REMARK   3    B33 (A**2) : -0.03000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.03000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.134         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.127         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.083         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.765         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2469 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3338 ; 1.456 ; 1.987       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   296 ; 5.847 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   114 ;38.646 ;24.298       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   452 ;14.958 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;20.846 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   378 ; 0.101 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1814 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1044 ; 0.208 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1679 ; 0.305 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   144 ; 0.131 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    48 ; 0.217 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    13 ; 0.196 ; 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):  1530 ; 1.041 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2413 ; 1.709 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1059 ; 2.610 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   925 ; 4.001 ; 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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   200        B   247                          
REMARK   3    RESIDUE RANGE :   B   274        B   356                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.1870  29.7790  14.8380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0088 T22:  -0.0227                                     
REMARK   3      T33:  -0.0191 T12:  -0.0096                                     
REMARK   3      T13:  -0.0008 T23:  -0.0066                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3488 L22:   0.5121                                     
REMARK   3      L33:   0.4181 L12:  -0.6426                                     
REMARK   3      L13:   0.5749 L23:  -0.1375                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0017 S12:   0.0375 S13:  -0.0313                       
REMARK   3      S21:  -0.0026 S22:  -0.0101 S23:   0.0088                       
REMARK   3      S31:   0.0586 S32:  -0.0820 S33:   0.0083                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   166                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.4170  44.7230   0.0820              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0149 T22:  -0.0213                                     
REMARK   3      T33:  -0.0038 T12:   0.0032                                     
REMARK   3      T13:   0.0002 T23:   0.0336                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4639 L22:   0.4517                                     
REMARK   3      L33:   1.0356 L12:  -0.1170                                     
REMARK   3      L13:   0.1793 L23:  -0.4877                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0123 S12:   0.0539 S13:   0.0352                       
REMARK   3      S21:   0.0559 S22:  -0.0721 S23:  -0.0696                       
REMARK   3      S31:  -0.0798 S32:   0.0899 S33:   0.0844                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3DDC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JUN-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB047896.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JUL-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29894                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.780                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.590                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.08600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.6400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 5P21                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM C2H3NAO2, 20% PEG 2000, 250MM      
REMARK 280  (NH4)2SO4, 10MM DTE, PH 4.50, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
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  1.000000  0.000000  0.000000       39.80000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       39.80000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       44.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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       47.19293            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       46.28209            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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 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 B   195                                                      
REMARK 465     SER B   196                                                      
REMARK 465     PRO B   197                                                      
REMARK 465     GLU B   198                                                      
REMARK 465     PHE B   199                                                      
REMARK 465     ALA B   249                                                      
REMARK 465     GLY B   250                                                      
REMARK 465     ILE B   251                                                      
REMARK 465     ARG B   252                                                      
REMARK 465     PRO B   253                                                      
REMARK 465     GLN B   254                                                      
REMARK 465     SER B   255                                                      
REMARK 465     ILE B   256                                                      
REMARK 465     TYR B   257                                                      
REMARK 465     ASP B   258                                                      
REMARK 465     ALA B   259                                                      
REMARK 465     ILE B   260                                                      
REMARK 465     LYS B   261                                                      
REMARK 465     GLU B   262                                                      
REMARK 465     VAL B   263                                                      
REMARK 465     ASN B   264                                                      
REMARK 465     PRO B   265                                                      
REMARK 465     ALA B   266                                                      
REMARK 465     ALA B   267                                                      
REMARK 465     THR B   268                                                      
REMARK 465     THR B   269                                                      
REMARK 465     ASP B   270                                                      
REMARK 465     LYS B   271                                                      
REMARK 465     ARG B   272                                                      
REMARK 465     THR B   273                                                      
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   OE1  GLU A    63     O    HOH A   638              2.05            
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    ILE A  36      -65.37    -90.16                                   
REMARK 500    ASP A 108       35.32   -146.45                                   
REMARK 500    LYS A 117       30.77     70.82                                   
REMARK 500    ARG A 149       -2.67     82.10                                   
REMARK 500    SER B 226     -156.57   -122.89                                   
REMARK 500    VAL B 247     -163.35    -79.40                                   
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 600  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A  17   OG                                                     
REMARK 620 2 THR A  35   OG1  83.5                                              
REMARK 620 3 GNP A 500   O2G 170.3  86.9                                        
REMARK 620 4 GNP A 500   O2B  94.3 175.5  95.3                                  
REMARK 620 5 HOH A 603   O    86.9  87.9  91.6  88.1                            
REMARK 620 6 HOH A 602   O    88.9  91.2  92.5  92.7 175.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 600                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A 500                 
DBREF  3DDC A    1   166  UNP    P01112   RASH_HUMAN       1    166             
DBREF  3DDC B  200   357  UNP    Q5EBH1   RASF5_MOUSE    200    357             
SEQADV 3DDC GLU A   30  UNP  P01112    ASP    30 ENGINEERED MUTATION            
SEQADV 3DDC LYS A   31  UNP  P01112    GLU    31 ENGINEERED MUTATION            
SEQADV 3DDC GLY B  195  UNP  Q5EBH1              EXPRESSION TAG                 
SEQADV 3DDC SER B  196  UNP  Q5EBH1              EXPRESSION TAG                 
SEQADV 3DDC PRO B  197  UNP  Q5EBH1              EXPRESSION TAG                 
SEQADV 3DDC GLU B  198  UNP  Q5EBH1              EXPRESSION TAG                 
SEQADV 3DDC PHE B  199  UNP  Q5EBH1              EXPRESSION TAG                 
SEQADV 3DDC MET B  285  UNP  Q5EBH1    LEU   285 ENGINEERED MUTATION            
SEQADV 3DDC ASP B  302  UNP  Q5EBH1    LYS   302 ENGINEERED MUTATION            
SEQRES   1 A  166  MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA GLY GLY          
SEQRES   2 A  166  VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN ASN          
SEQRES   3 A  166  HIS PHE VAL GLU LYS TYR ASP PRO THR ILE GLU ASP SER          
SEQRES   4 A  166  TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS LEU          
SEQRES   5 A  166  LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR SER          
SEQRES   6 A  166  ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY PHE          
SEQRES   7 A  166  LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE GLU          
SEQRES   8 A  166  ASP ILE HIS GLN TYR ARG GLU GLN ILE LYS ARG VAL LYS          
SEQRES   9 A  166  ASP SER ASP ASP VAL PRO MET VAL LEU VAL GLY ASN LYS          
SEQRES  10 A  166  CYS ASP LEU ALA ALA ARG THR VAL GLU SER ARG GLN ALA          
SEQRES  11 A  166  GLN ASP LEU ALA ARG SER TYR GLY ILE PRO TYR ILE GLU          
SEQRES  12 A  166  THR SER ALA LYS THR ARG GLN GLY VAL GLU ASP ALA PHE          
SEQRES  13 A  166  TYR THR LEU VAL ARG GLU ILE ARG GLN HIS                      
SEQRES   1 B  163  GLY SER PRO GLU PHE PRO PRO THR ILE GLN GLU ILE LYS          
SEQRES   2 B  163  GLN LYS ILE ASP SER TYR ASN SER ARG GLU LYS HIS CYS          
SEQRES   3 B  163  LEU GLY MET LYS LEU SER GLU ASP GLY THR TYR THR GLY          
SEQRES   4 B  163  PHE ILE LYS VAL HIS LEU LYS LEU ARG ARG PRO VAL THR          
SEQRES   5 B  163  VAL PRO ALA GLY ILE ARG PRO GLN SER ILE TYR ASP ALA          
SEQRES   6 B  163  ILE LYS GLU VAL ASN PRO ALA ALA THR THR ASP LYS ARG          
SEQRES   7 B  163  THR SER PHE TYR LEU PRO LEU ASP ALA ILE LYS GLN MET          
SEQRES   8 B  163  HIS ILE SER SER THR THR THR VAL SER GLU VAL ILE GLN          
SEQRES   9 B  163  GLY LEU LEU ASP LYS PHE MET VAL VAL ASP ASN PRO GLN          
SEQRES  10 B  163  LYS PHE ALA LEU PHE LYS ARG ILE HIS LYS ASP GLY GLN          
SEQRES  11 B  163  VAL LEU PHE GLN LYS LEU SER ILE ALA ASP TYR PRO LEU          
SEQRES  12 B  163  TYR LEU ARG LEU LEU ALA GLY PRO ASP THR ASP VAL LEU          
SEQRES  13 B  163  SER PHE VAL LEU LYS GLU ASN                                  
HET     MG  A 600       1                                                       
HET    GNP  A 500      32                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER                      
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  GNP    C10 H17 N6 O13 P3                                            
FORMUL   5  HOH   *115(H2 O)                                                    
HELIX    1   1 GLY A   15  ASN A   26  1                                  12    
HELIX    2   2 GLN A   61  ALA A   66  5                                   6    
HELIX    3   3 MET A   67  GLY A   75  1                                   9    
HELIX    4   4 ASN A   86  ASP A   92  1                                   7    
HELIX    5   5 ASP A   92  ASP A  105  1                                  14    
HELIX    6   6 GLU A  126  GLY A  138  1                                  13    
HELIX    7   7 GLY A  151  GLN A  165  1                                  15    
HELIX    8   8 THR B  202  ARG B  216  1                                  15    
HELIX    9   9 GLU B  217  GLY B  222  5                                   6    
HELIX   10  10 GLU B  227  GLY B  229  5                                   3    
HELIX   11  11 THR B  292  PHE B  304  1                                  13    
HELIX   12  12 ASN B  309  GLN B  311  5                                   3    
HELIX   13  13 TYR B  335  GLY B  344  1                                  10    
SHEET    1   A 9 TYR A 141  GLU A 143  0                                        
SHEET    2   A 9 MET A 111  ASN A 116  1  N  LEU A 113   O  ILE A 142           
SHEET    3   A 9 GLY A  77  ALA A  83  1  N  PHE A  82   O  ASN A 116           
SHEET    4   A 9 THR A   2  VAL A   9  1  N  VAL A   9   O  VAL A  81           
SHEET    5   A 9 GLU A  49  THR A  58  1  O  LEU A  56   N  LEU A   6           
SHEET    6   A 9 GLU A  37  ILE A  46 -1  N  LYS A  42   O  LEU A  53           
SHEET    7   A 9 PHE B 275  SER B 288 -1  O  ILE B 282   N  SER A  39           
SHEET    8   A 9 TYR B 231  VAL B 245 -1  N  LEU B 239   O  ALA B 281           
SHEET    9   A 9 LYS B 224  LEU B 225 -1  N  LYS B 224   O  THR B 232           
SHEET    1   B11 TYR A 141  GLU A 143  0                                        
SHEET    2   B11 MET A 111  ASN A 116  1  N  LEU A 113   O  ILE A 142           
SHEET    3   B11 GLY A  77  ALA A  83  1  N  PHE A  82   O  ASN A 116           
SHEET    4   B11 THR A   2  VAL A   9  1  N  VAL A   9   O  VAL A  81           
SHEET    5   B11 GLU A  49  THR A  58  1  O  LEU A  56   N  LEU A   6           
SHEET    6   B11 GLU A  37  ILE A  46 -1  N  LYS A  42   O  LEU A  53           
SHEET    7   B11 PHE B 275  SER B 288 -1  O  ILE B 282   N  SER A  39           
SHEET    8   B11 TYR B 231  VAL B 245 -1  N  LEU B 239   O  ALA B 281           
SHEET    9   B11 SER B 351  GLU B 356  1  O  LEU B 354   N  HIS B 238           
SHEET   10   B11 PHE B 313  LYS B 321 -1  N  ARG B 318   O  SER B 351           
SHEET   11   B11 GLN B 324  LYS B 329 -1  O  GLN B 324   N  LYS B 321           
LINK         OG  SER A  17                MG    MG A 600     1555   1555  2.11  
LINK         OG1 THR A  35                MG    MG A 600     1555   1555  2.08  
LINK        MG    MG A 600                 O2G GNP A 500     1555   1555  2.02  
LINK        MG    MG A 600                 O2B GNP A 500     1555   1555  2.05  
LINK        MG    MG A 600                 O   HOH A 603     1555   1555  2.03  
LINK        MG    MG A 600                 O   HOH A 602     1555   1555  2.12  
CISPEP   1 PRO B  200    PRO B  201          0       -23.68                     
SITE     1 AC1  2 SER A  17  THR A  35                                          
SITE     1 AC2 20 GLY A  12  GLY A  13  GLY A  15  LYS A  16                    
SITE     2 AC2 20 SER A  17  ALA A  18  PHE A  28  GLU A  30                    
SITE     3 AC2 20 LYS A  31  TYR A  32  PRO A  34  THR A  35                    
SITE     4 AC2 20 GLY A  60  ASN A 116  LYS A 117  ASP A 119                    
SITE     5 AC2 20 LEU A 120  SER A 145  ALA A 146  LYS A 147                    
CRYST1   79.600   88.000   56.500  90.00 125.00  90.00 C 1 2 1       4          
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      0.012563  0.000000  0.008797        0.00000                         
SCALE2      0.000000  0.011364  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021607        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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