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Database: PDB
Entry: 6GOD
LinkDB: 6GOD
Original site: 6GOD 
HEADER    ONCOPROTEIN                             01-JUN-18   6GOD              
TITLE     KRAS FULL LENGTH WILD-TYPE GPPNHP                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GTPASE KRAS;                                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: K-RAS 2,KI-RAS,C-K-RAS,C-KI-RAS;                            
COMPND   5 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: KRAS, KRAS2, RASK2;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    KRAS FULL LENGHT, ONCOPROTEIN                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.CRUZ-MIGONI,C.E.QUEVEDO,S.B.CARR,M.T.EHEBAUER,S.V.E.PHILLIPS,       
AUTHOR   2 T.H.RABBITTS                                                         
REVDAT   2   20-FEB-19 6GOD    1       JRNL                                     
REVDAT   1   06-FEB-19 6GOD    0                                                
JRNL        AUTH   A.CRUZ-MIGONI,P.CANNING,C.E.QUEVEDO,C.J.R.BATAILLE,N.BERY,   
JRNL        AUTH 2 A.MILLER,A.J.RUSSELL,S.E.V.PHILLIPS,S.B.CARR,T.H.RABBITTS    
JRNL        TITL   STRUCTURE-BASED DEVELOPMENT OF NEW RAS-EFFECTOR INHIBITORS   
JRNL        TITL 2 FROM A COMBINATION OF ACTIVE AND INACTIVE RAS-BINDING        
JRNL        TITL 3 COMPOUNDS.                                                   
JRNL        REF    PROC. NATL. ACAD. SCI.        V. 116  2545 2019              
JRNL        REF  2 U.S.A.                                                       
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   30683716                                                     
JRNL        DOI    10.1073/PNAS.1811360116                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.71 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0189                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.71                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 51.11                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 17971                          
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) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 992                             
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) : 1.71                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.75                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1362                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.66                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2680                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 93                           
REMARK   3   BIN FREE R VALUE                    : 0.2960                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1366                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 97                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.92                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : -0.01000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.114         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.117         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.090         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.738         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1440 ; 0.018 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1303 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1951 ; 1.876 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3031 ; 1.046 ; 2.991       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   175 ; 5.865 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    69 ;39.709 ;24.493       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   256 ;15.274 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;14.259 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   219 ; 0.118 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1591 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   283 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):   697 ; 3.075 ; 3.006       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   696 ; 3.074 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   873 ; 4.384 ; 4.494       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):   874 ; 4.382 ; 4.501       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   743 ; 4.128 ; 3.593       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):   743 ; 4.126 ; 3.593       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  1079 ; 6.280 ; 5.175       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  1598 ; 7.791 ;37.064       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  1586 ; 7.753 ;36.857       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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 6GOD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-JUN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200009168.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-APR-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : MASSIF-1                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.966                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 2M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : XIA2                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18963                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 51.110                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.05100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
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: 4DST                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRISCL, 0.2 M NAOAC AND 30-35 %    
REMARK 280  PEG 4000, PH 8.0, VAPOR DIFFUSION, SITTING DROP, 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       39.38000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       22.73605            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       25.72667            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       39.38000            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       22.73605            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       25.72667            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       39.38000            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       22.73605            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       25.72667            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       45.47211            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       51.45333            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       45.47211            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       51.45333            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       45.47211            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       51.45333            
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 TOTAL BURIED SURFACE AREA: 1360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8390 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 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 390  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     LYS A 169    CD   CE   NZ                                        
REMARK 470     LYS A 172    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   O    HOH A   304     O    HOH A   374              2.15            
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   340     O    HOH A   340     2455     1.17            
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    TYR A  32   CB  -  CG  -  CD2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ASP A  92   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 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    ILE A  36      -64.02    -99.33                                   
REMARK 500    SER A 122       34.86    -76.23                                   
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 204  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A  10   O                                                      
REMARK 620 2 ALA A  59   O   106.6                                              
REMARK 620 3 GLY A  60   O    94.1  88.0                                        
REMARK 620 4 TYR A  96   OH   83.1 169.4  87.1                                  
REMARK 620 5 HOH A 319   O   164.2  88.9  89.3  81.7                            
REMARK 620 6 HOH A 341   O    87.9  87.0 175.0  97.7  90.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 201  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A  17   OG                                                     
REMARK 620 2 THR A  35   OG1  83.1                                              
REMARK 620 3 HOH A 326   O    86.8  90.0                                        
REMARK 620 4 GNP A 202   O2G 172.3  90.0  89.9                                  
REMARK 620 5 GNP A 202   O1B  93.0 175.5  87.6  93.8                            
REMARK 620 6 HOH A 332   O    90.4  88.1 176.7  92.8  94.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GNP A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 204                  
DBREF  6GOD A    2   172  UNP    P01116   RASK_HUMAN       2    172             
SEQADV 6GOD SER A    1  UNP  P01116              EXPRESSION TAG                 
SEQRES   1 A  172  SER THR GLU TYR LYS LEU VAL VAL VAL GLY ALA GLY GLY          
SEQRES   2 A  172  VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN ASN          
SEQRES   3 A  172  HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP SER          
SEQRES   4 A  172  TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS LEU          
SEQRES   5 A  172  LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR SER          
SEQRES   6 A  172  ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY PHE          
SEQRES   7 A  172  LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE GLU          
SEQRES   8 A  172  ASP ILE HIS HIS TYR ARG GLU GLN ILE LYS ARG VAL LYS          
SEQRES   9 A  172  ASP SER GLU ASP VAL PRO MET VAL LEU VAL GLY ASN LYS          
SEQRES  10 A  172  CYS ASP LEU PRO SER ARG THR VAL ASP THR LYS GLN ALA          
SEQRES  11 A  172  GLN ASP LEU ALA ARG SER TYR GLY ILE PRO PHE ILE GLU          
SEQRES  12 A  172  THR SER ALA LYS THR ARG GLN GLY VAL ASP ASP ALA PHE          
SEQRES  13 A  172  TYR THR LEU VAL ARG GLU ILE ARG LYS HIS LYS GLU LYS          
SEQRES  14 A  172  MET SER LYS                                                  
HET     MG  A 201       1                                                       
HET    GNP  A 202      32                                                       
HET    GOL  A 203       6                                                       
HET     MG  A 204       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2   MG    2(MG 2+)                                                     
FORMUL   3  GNP    C10 H17 N6 O13 P3                                            
FORMUL   4  GOL    C3 H8 O3                                                     
FORMUL   6  HOH   *97(H2 O)                                                     
HELIX    1 AA1 GLY A   15  ASN A   26  1                                  12    
HELIX    2 AA2 TYR A   64  GLY A   75  1                                  12    
HELIX    3 AA3 ASN A   86  ASP A  105  1                                  20    
HELIX    4 AA4 ASP A  126  GLY A  138  1                                  13    
HELIX    5 AA5 GLY A  151  LYS A  172  1                                  22    
SHEET    1 AA1 6 GLU A  37  ILE A  46  0                                        
SHEET    2 AA1 6 GLU A  49  THR A  58 -1  O  CYS A  51   N  VAL A  44           
SHEET    3 AA1 6 GLU A   3  VAL A   9  1  N  VAL A   8   O  LEU A  56           
SHEET    4 AA1 6 GLY A  77  ALA A  83  1  O  VAL A  81   N  VAL A   9           
SHEET    5 AA1 6 MET A 111  ASN A 116  1  O  ASN A 116   N  PHE A  82           
SHEET    6 AA1 6 PHE A 141  GLU A 143  1  O  ILE A 142   N  LEU A 113           
LINK         O   GLY A  10                MG    MG A 204     1555   1555  2.51  
LINK         OG  SER A  17                MG    MG A 201     1555   1555  2.05  
LINK         OG1 THR A  35                MG    MG A 201     1555   1555  2.04  
LINK         O   ALA A  59                MG    MG A 204     1555   1555  2.39  
LINK         O   GLY A  60                MG    MG A 204     1555   1555  2.46  
LINK         OH  TYR A  96                MG    MG A 204     1555   1555  2.36  
LINK        MG    MG A 201                 O   HOH A 326     1555   1555  2.17  
LINK        MG    MG A 201                 O2G GNP A 202     1555   1555  2.01  
LINK        MG    MG A 201                 O1B GNP A 202     1555   1555  2.07  
LINK        MG    MG A 201                 O   HOH A 332     1555   1555  1.94  
LINK        MG    MG A 204                 O   HOH A 319     1555   1555  2.28  
LINK        MG    MG A 204                 O   HOH A 341     1555   1555  2.37  
SITE     1 AC1  5 SER A  17  THR A  35  GNP A 202  HOH A 326                    
SITE     2 AC1  5 HOH A 332                                                     
SITE     1 AC2 26 GLY A  12  GLY A  13  VAL A  14  GLY A  15                    
SITE     2 AC2 26 LYS A  16  SER A  17  ALA A  18  PHE A  28                    
SITE     3 AC2 26 VAL A  29  ASP A  30  GLU A  31  TYR A  32                    
SITE     4 AC2 26 PRO A  34  THR A  35  GLY A  60  ASN A 116                    
SITE     5 AC2 26 LYS A 117  ASP A 119  SER A 145  ALA A 146                    
SITE     6 AC2 26 LYS A 147   MG A 201  HOH A 315  HOH A 326                    
SITE     7 AC2 26 HOH A 332  HOH A 343                                          
SITE     1 AC3  3 ARG A  68  ASP A  92  GLN A  99                               
SITE     1 AC4  6 GLY A  10  ALA A  59  GLY A  60  TYR A  96                    
SITE     2 AC4  6 HOH A 319  HOH A 341                                          
CRYST1   78.760   78.760   77.180  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      0.012697  0.007331  0.000000        0.00000                         
SCALE2      0.000000  0.014661  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012957        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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