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Database: PDB
Entry: 4DLY
LinkDB: 4DLY
Original site: 4DLY 
HEADER    SIGNALING PROTEIN                       06-FEB-12   4DLY              
TITLE     SET 1 CACL2/DTT, ORDERED OFF                                          
CAVEAT     4DLY    CHIRALITY ERROR AT C2 CENTER OF DTT A 204                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GTPASE HRAS;                                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: H-RAS-1, HA-RAS, TRANSFORMING PROTEIN P21, C-H-RAS, P21RAS, 
COMPND   5 GTPASE HRAS, N-TERMINALLY PROCESSED;                                 
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HRAS, HRAS1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21                                     
KEYWDS    GTP-BINDING, NUCLEOTIDE BINDING, SIGNALING PROTEIN                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.HOLZAPFEL,C.MATTOS                                                  
REVDAT   4   15-NOV-17 4DLY    1       REMARK                                   
REVDAT   3   17-OCT-12 4DLY    1       JRNL                                     
REVDAT   2   15-AUG-12 4DLY    1       TITLE                                    
REVDAT   1   08-AUG-12 4DLY    0                                                
JRNL        AUTH   G.HOLZAPFEL,G.BUHRMAN,C.MATTOS                               
JRNL        TITL   SHIFT IN THE EQUILIBRIUM BETWEEN ON AND OFF STATES OF THE    
JRNL        TITL 2 ALLOSTERIC SWITCH IN RAS-GPPNHP AFFECTED BY SMALL MOLECULES  
JRNL        TITL 3 AND BULK SOLVENT COMPOSITION.                                
JRNL        REF    BIOCHEMISTRY                  V.  51  6114 2012              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   22845804                                                     
JRNL        DOI    10.1021/BI300509J                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.57 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.6.1_336                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.57                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.23                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.230                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 27768                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.160                           
REMARK   3   R VALUE            (WORKING SET) : 0.158                           
REMARK   3   FREE R VALUE                     : 0.179                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.120                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1976                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 28.2306 -  3.3809    1.00     2735   209  0.1651 0.1784        
REMARK   3     2  3.3809 -  2.6842    1.00     2658   201  0.1645 0.1767        
REMARK   3     3  2.6842 -  2.3451    1.00     2633   201  0.1578 0.1867        
REMARK   3     4  2.3451 -  2.1308    0.99     2607   199  0.1551 0.1794        
REMARK   3     5  2.1308 -  1.9781    0.99     2583   196  0.1449 0.1628        
REMARK   3     6  1.9781 -  1.8615    0.98     2551   199  0.1411 0.1603        
REMARK   3     7  1.8615 -  1.7683    0.98     2559   195  0.1437 0.1760        
REMARK   3     8  1.7683 -  1.6913    0.97     2515   193  0.1440 0.1731        
REMARK   3     9  1.6913 -  1.6262    0.96     2513   191  0.1482 0.1787        
REMARK   3    10  1.6262 -  1.5701    0.95     2438   192  0.1576 0.1822        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.40                                          
REMARK   3   B_SOL              : 60.04                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.160            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.100           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.25                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.41140                                             
REMARK   3    B22 (A**2) : -0.41140                                             
REMARK   3    B33 (A**2) : 0.82270                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           1393                                  
REMARK   3   ANGLE     :  1.272           1891                                  
REMARK   3   CHIRALITY :  0.336            213                                  
REMARK   3   PLANARITY :  0.004            242                                  
REMARK   3   DIHEDRAL  : 15.833            525                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4DLY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-FEB-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000070495.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : CRYSTAL                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28221                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.570                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 10.90                              
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.57                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 200 MM CACL2, PH 7.5,      
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
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   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3                                      
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3                                   
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3                                  
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3                                      
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3                                   
REMARK 290      18555   -X+1/3,-X+Y+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 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000       44.10350            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       25.46317            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       44.71400            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       44.10350            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       25.46317            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       44.71400            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       44.10350            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       25.46317            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       44.71400            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       44.10350            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       25.46317            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       44.71400            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       44.10350            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       25.46317            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       44.71400            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       44.10350            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       25.46317            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       44.71400            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       50.92634            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       89.42800            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       50.92634            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       89.42800            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       50.92634            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000       89.42800            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       50.92634            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       89.42800            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       50.92634            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000       89.42800            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       50.92634            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000       89.42800            
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 15530 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -243.0 KCAL/MOL                       
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 350   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000      152.77901            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000     -132.31050            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000       76.38950            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4 -0.500000  0.866025  0.000000     -132.31050            
REMARK 350   BIOMT2   4  0.866025  0.500000  0.000000       76.38950            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000     -134.14200            
REMARK 350   BIOMT1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   5  0.000000 -1.000000  0.000000      152.77901            
REMARK 350   BIOMT3   5  0.000000  0.000000 -1.000000     -134.14200            
REMARK 350   BIOMT1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   6  0.000000  0.000000 -1.000000     -134.14200            
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 MG    MG A 203  LIES ON A SPECIAL POSITION.                          
REMARK 375 CA    CA A 205  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 362  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 370  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 378  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 383  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 388  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 455  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 475  LIES ON A SPECIAL POSITION.                          
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     GLU A  62    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 128    CG   CD   NE   CZ   NH1  NH2                        
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      -85.62    -92.31                                   
REMARK 500    ARG A 149       -5.00     81.72                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 202  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GNP A 208   O2G                                                    
REMARK 620 2 GNP A 208   O2B  95.7                                              
REMARK 620 3 SER A  17   OG  171.8  92.1                                        
REMARK 620 4 HOH A 437   O    91.6  91.8  85.3                                  
REMARK 620 5 THR A  35   OG1  90.4 173.5  82.0  90.3                            
REMARK 620 6 HOH A 301   O    92.8  88.5  90.2 175.5  88.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 203  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 357   O                                                      
REMARK 620 2 HOH A 336   O    81.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 206  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 138   O                                                      
REMARK 620 2 HOH A 417   O    91.3                                              
REMARK 620 3 HOH A 469   O   150.7  81.9                                        
REMARK 620 4 HOH A 461   O    94.0 171.8  90.4                                  
REMARK 620 5 HOH A 459   O    75.1  74.0  75.6 101.4                            
REMARK 620 6 HOH A 446   O   129.1  80.3  78.0 101.0 145.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 205  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG A 102   O                                                      
REMARK 620 2 ASP A 105   OD2  85.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE A  28   O                                                      
REMARK 620 2 ASP A  30   OD2  84.0                                              
REMARK 620 3 HOH A 307   O    91.0  87.0                                        
REMARK 620 4 HOH A 442   O   162.0  78.1  89.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA 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 MG A 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT A 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 205                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT A 207                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A 208                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4DLR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DLS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DLT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DLU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DLV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DLW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DLX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DLZ   RELATED DB: PDB                                   
DBREF  4DLY A    1   166  UNP    P01112   RASH_HUMAN       1    166             
SEQADV 4DLY GLU A   70  UNP  P01112    GLN    70 CONFLICT                       
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 ASP GLU 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 GLU 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                      
HET     CA  A 201       1                                                       
HET     MG  A 202       1                                                       
HET     MG  A 203       1                                                       
HET    DTT  A 204       8                                                       
HET     CA  A 205       1                                                       
HET     CA  A 206       1                                                       
HET    DTT  A 207       8                                                       
HET    GNP  A 208      32                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE                                   
HETNAM     GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER                      
HETSYN     DTT 1,4-DITHIOTHREITOL                                               
FORMUL   2   CA    3(CA 2+)                                                     
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   5  DTT    2(C4 H10 O2 S2)                                              
FORMUL   9  GNP    C10 H17 N6 O13 P3                                            
FORMUL  10  HOH   *180(H2 O)                                                    
HELIX    1   1 GLY A   15  ASN A   26  1                                  12    
HELIX    2   2 GLN A   61  SER A   65  5                                   5    
HELIX    3   3 MET A   67  ARG A   73  1                                   7    
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  ARG A  164  1                                  14    
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  GLY A  10  1  N  LEU A   6   O  LEU A  56           
SHEET    4   A 6 GLY A  77  ALA A  83  1  O  VAL A  81   N  VAL A   9           
SHEET    5   A 6 MET A 111  ASN A 116  1  O  ASN A 116   N  PHE A  82           
SHEET    6   A 6 TYR A 141  GLU A 143  1  O  ILE A 142   N  LEU A 113           
LINK        MG    MG A 202                 O2G GNP A 208     1555   1555  2.05  
LINK        MG    MG A 202                 O2B GNP A 208     1555   1555  2.09  
LINK         OG  SER A  17                MG    MG A 202     1555   1555  2.11  
LINK        MG    MG A 202                 O   HOH A 437     1555   1555  2.11  
LINK         OG1 THR A  35                MG    MG A 202     1555   1555  2.14  
LINK        MG    MG A 202                 O   HOH A 301     1555   1555  2.16  
LINK        MG    MG A 203                 O   HOH A 357     1555   1555  2.26  
LINK         O   GLY A 138                CA    CA A 206     1555   1555  2.29  
LINK         O   ARG A 102                CA    CA A 205     1555   1555  2.33  
LINK         O   PHE A  28                CA    CA A 201     1555   1555  2.35  
LINK        MG    MG A 203                 O   HOH A 336     1555   1555  2.36  
LINK         OD2 ASP A  30                CA    CA A 201     1555   1555  2.40  
LINK        CA    CA A 201                 O   HOH A 307     1555   1555  2.43  
LINK        CA    CA A 206                 O   HOH A 417     1555   1555  2.48  
LINK        CA    CA A 201                 O   HOH A 442     1555   1555  2.48  
LINK        CA    CA A 206                 O   HOH A 469     1555   1555  2.57  
LINK        CA    CA A 206                 O   HOH A 461     1555   1555  2.57  
LINK         OD2 ASP A 105                CA    CA A 205     1555   1555  2.58  
LINK        CA    CA A 206                 O   HOH A 459     1555   1555  2.66  
LINK        CA    CA A 206                 O   HOH A 446     1555   1555  2.69  
SITE     1 AC1  6 PHE A  28  ASP A  30  GLU A  31  ASP A  33                    
SITE     2 AC1  6 HOH A 307  HOH A 442                                          
SITE     1 AC2  5 SER A  17  THR A  35  GNP A 208  HOH A 301                    
SITE     2 AC2  5 HOH A 437                                                     
SITE     1 AC3  2 HOH A 336  HOH A 357                                          
SITE     1 AC4  3 ARG A  68  GLN A  95  TYR A  96                               
SITE     1 AC5  2 ARG A 102  ASP A 105                                          
SITE     1 AC6  7 GLY A 138  HOH A 341  HOH A 417  HOH A 446                    
SITE     2 AC6  7 HOH A 459  HOH A 461  HOH A 469                               
SITE     1 AC7  3 TYR A  32  PRO A  34  GLN A  61                               
SITE     1 AC8 31 GLY A  12  GLY A  13  VAL A  14  GLY A  15                    
SITE     2 AC8 31 LYS A  16  SER A  17  ALA A  18  PHE A  28                    
SITE     3 AC8 31 VAL A  29  ASP A  30  GLU A  31  TYR A  32                    
SITE     4 AC8 31 PRO A  34  THR A  35  GLY A  60  GLN A  61                    
SITE     5 AC8 31 ASN A 116  LYS A 117  ASP A 119  LEU A 120                    
SITE     6 AC8 31 SER A 145  ALA A 146  LYS A 147   MG A 202                    
SITE     7 AC8 31 HOH A 301  HOH A 303  HOH A 323  HOH A 330                    
SITE     8 AC8 31 HOH A 377  HOH A 434  HOH A 437                               
CRYST1   88.207   88.207  134.142  90.00  90.00 120.00 H 3 2        18          
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      0.011337  0.006545  0.000000        0.00000                         
SCALE2      0.000000  0.013091  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007455        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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