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Database: PDB
Entry: 5VQ0
LinkDB: 5VQ0
Original site: 5VQ0 
HEADER    HYDROLASE                               06-MAY-17   5VQ0              
TITLE     CRYSTAL STRUCTURE OF HUMAN KRAS G12A MUTANT IN COMPLEX WITH GDP (EDTA 
TITLE    2 SOAKED)                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GTPASE KRAS;                                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 1-169;                                            
COMPND   5 SYNONYM: K-RAS 2,KI-RAS,C-K-RAS,C-KI-RAS;                            
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: KRAS, KRAS2, RASK2;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ONCOGENIC MUTANT, HYDROLASE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.XU,B.LONG,G.BORIS,S.NI,M.A.KENNEDY                                  
REVDAT   2   20-DEC-17 5VQ0    1       JRNL                                     
REVDAT   1   06-DEC-17 5VQ0    0                                                
JRNL        AUTH   S.XU,B.N.LONG,G.H.BORIS,A.CHEN,S.NI,M.A.KENNEDY              
JRNL        TITL   STRUCTURAL INSIGHT INTO THE REARRANGEMENT OF THE SWITCH I    
JRNL        TITL 2 REGION IN GTP-BOUND G12A K-RAS.                              
JRNL        REF    ACTA CRYSTALLOGR D STRUCT     V.  73   970 2017              
JRNL        REF  2 BIOL                                                         
JRNL        REFN                   ISSN 2059-7983                               
JRNL        PMID   29199977                                                     
JRNL        DOI    10.1107/S2059798317015418                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 66.48                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 15807                          
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) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 781                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1125                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.35                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2160                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 85                           
REMARK   3   BIN FREE R VALUE                    : 0.2880                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2547                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 64                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.94                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.54000                                             
REMARK   3    B22 (A**2) : -1.54000                                             
REMARK   3    B33 (A**2) : 5.00000                                              
REMARK   3    B12 (A**2) : -0.77000                                             
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): 0.372         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.265         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.193         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.964         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.912                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.881                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2669 ; 0.015 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2460 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3614 ; 2.376 ; 1.983       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5710 ; 0.998 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   320 ; 6.227 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   127 ;38.038 ;24.331       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   478 ;14.370 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;16.458 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   408 ; 0.093 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2914 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   532 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     169      1                      
REMARK   3           1     B      1       B     169      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      1    A (A**2):   1283 ; 0.840 ; 0.500           
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 U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 5VQ0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000227835.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-APR-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 31-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97931                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.22                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16807                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 66.480                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.04600                            
REMARK 200  R SYM                      (I) : 0.04600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.15000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.01700                            
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: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 MOL/L SODIUM ACETATE, 0.1 MOL/L      
REMARK 280  TRIS PH 8.5, 26% PEG 3,350, VAPOR DIFFUSION, HANGING DROP,          
REMARK 280  TEMPERATURE 295K                                                    
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       46.38300            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       26.77924            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       39.47167            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       46.38300            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       26.77924            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       39.47167            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       46.38300            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       26.77924            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       39.47167            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       53.55848            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       78.94333            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       53.55848            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       78.94333            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       53.55848            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       78.94333            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     HIS A     0                                                      
REMARK 465     GLN A    61                                                      
REMARK 465     GLU A    62                                                      
REMARK 465     GLU A    63                                                      
REMARK 465     TYR A    64                                                      
REMARK 465     SER A    65                                                      
REMARK 465     ALA A    66                                                      
REMARK 465     MET A    67                                                      
REMARK 465     ARG A    68                                                      
REMARK 465     ASP A    69                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     GLN B    61                                                      
REMARK 465     GLU B    62                                                      
REMARK 465     GLU B    63                                                      
REMARK 465     TYR B    64                                                      
REMARK 465     SER B    65                                                      
REMARK 465     ALA B    66                                                      
REMARK 465     MET B    67                                                      
REMARK 465     ARG B    68                                                      
REMARK 465     ASP B    69                                                      
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     ASP A 126    OD2                                                 
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    GLN A    70     OG1  THR A    74              2.13            
REMARK 500   O    GLN B    70     OG1  THR B    74              2.14            
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    ASP A 108       78.51   -115.55                                   
REMARK 500    SER A 122       46.65    -78.72                                   
REMARK 500    ASP B  33      109.54    -45.73                                   
REMARK 500    SER B 122       48.33    -78.60                                   
REMARK 500    ARG B 149       -1.62     81.68                                   
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 201  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A  17   OG                                                     
REMARK 620 2 GDP A 202   O2B  82.0                                              
REMARK 620 3 HOH A 319   O    88.7 160.6                                        
REMARK 620 4 HOH A 302   O   147.6  97.5  81.3                                  
REMARK 620 5 HOH A 303   O    69.6  86.8  74.0  78.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 201  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B  17   OG                                                     
REMARK 620 2 HOH B 319   O    86.6                                              
REMARK 620 3 GDP B 202   O2B  81.9 156.4                                        
REMARK 620 4 HOH B 301   O    67.3  73.3  83.3                                  
REMARK 620 5 HOH B 303   O   144.4  82.9  94.6  77.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP B 202                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5VP7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VPI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VPY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VPZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VQ1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VQ2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VQ8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VQ6   RELATED DB: PDB                                   
DBREF  5VQ0 A    1   169  UNP    P01116   RASK_HUMAN       1    169             
DBREF  5VQ0 B    1   169  UNP    P01116   RASK_HUMAN       1    169             
SEQADV 5VQ0 HIS A    0  UNP  P01116              EXPRESSION TAG                 
SEQADV 5VQ0 ALA A   12  UNP  P01116    GLY    12 ENGINEERED MUTATION            
SEQADV 5VQ0 SER A  118  UNP  P01116    CYS   118 ENGINEERED MUTATION            
SEQADV 5VQ0 HIS B    0  UNP  P01116              EXPRESSION TAG                 
SEQADV 5VQ0 ALA B   12  UNP  P01116    GLY    12 ENGINEERED MUTATION            
SEQADV 5VQ0 SER B  118  UNP  P01116    CYS   118 ENGINEERED MUTATION            
SEQRES   1 A  170  HIS MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA ALA          
SEQRES   2 A  170  GLY VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN          
SEQRES   3 A  170  ASN HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP          
SEQRES   4 A  170  SER TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS          
SEQRES   5 A  170  LEU LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR          
SEQRES   6 A  170  SER ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY          
SEQRES   7 A  170  PHE LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE          
SEQRES   8 A  170  GLU ASP ILE HIS HIS TYR ARG GLU GLN ILE LYS ARG VAL          
SEQRES   9 A  170  LYS ASP SER GLU ASP VAL PRO MET VAL LEU VAL GLY ASN          
SEQRES  10 A  170  LYS SER ASP LEU PRO SER ARG THR VAL ASP THR LYS GLN          
SEQRES  11 A  170  ALA GLN ASP LEU ALA ARG SER TYR GLY ILE PRO PHE ILE          
SEQRES  12 A  170  GLU THR SER ALA LYS THR ARG GLN GLY VAL ASP ASP ALA          
SEQRES  13 A  170  PHE TYR THR LEU VAL ARG GLU ILE ARG LYS HIS LYS GLU          
SEQRES  14 A  170  LYS                                                          
SEQRES   1 B  170  HIS MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA ALA          
SEQRES   2 B  170  GLY VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN          
SEQRES   3 B  170  ASN HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP          
SEQRES   4 B  170  SER TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS          
SEQRES   5 B  170  LEU LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR          
SEQRES   6 B  170  SER ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY          
SEQRES   7 B  170  PHE LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE          
SEQRES   8 B  170  GLU ASP ILE HIS HIS TYR ARG GLU GLN ILE LYS ARG VAL          
SEQRES   9 B  170  LYS ASP SER GLU ASP VAL PRO MET VAL LEU VAL GLY ASN          
SEQRES  10 B  170  LYS SER ASP LEU PRO SER ARG THR VAL ASP THR LYS GLN          
SEQRES  11 B  170  ALA GLN ASP LEU ALA ARG SER TYR GLY ILE PRO PHE ILE          
SEQRES  12 B  170  GLU THR SER ALA LYS THR ARG GLN GLY VAL ASP ASP ALA          
SEQRES  13 B  170  PHE TYR THR LEU VAL ARG GLU ILE ARG LYS HIS LYS GLU          
SEQRES  14 B  170  LYS                                                          
HET     MG  A 201       1                                                       
HET    GDP  A 202      28                                                       
HET     MG  B 201       1                                                       
HET    GDP  B 202      28                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   4  GDP    2(C10 H15 N5 O11 P2)                                         
FORMUL   7  HOH   *64(H2 O)                                                     
HELIX    1 AA1 GLY A   15  ASN A   26  1                                  12    
HELIX    2 AA2 TYR A   71  GLY A   75  1                                   5    
HELIX    3 AA3 ASN A   86  ASP A   92  1                                   7    
HELIX    4 AA4 ASP A   92  ASP A  105  1                                  14    
HELIX    5 AA5 ASP A  126  GLY A  138  1                                  13    
HELIX    6 AA6 GLY A  151  LYS A  167  1                                  17    
HELIX    7 AA7 GLY B   15  ASN B   26  1                                  12    
HELIX    8 AA8 TYR B   71  GLY B   75  1                                   5    
HELIX    9 AA9 ASN B   86  ASP B   92  1                                   7    
HELIX   10 AB1 ASP B   92  ASP B  105  1                                  14    
HELIX   11 AB2 ASP B  126  GLY B  138  1                                  13    
HELIX   12 AB3 GLY B  151  LYS B  167  1                                  17    
SHEET    1 AA1 6 ASP A  38  ILE A  46  0                                        
SHEET    2 AA1 6 GLU A  49  ASP A  57 -1  O  LEU A  53   N  LYS A  42           
SHEET    3 AA1 6 THR A   2  VAL A   9  1  N  LEU A   6   O  ASP A  54           
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           
SHEET    1 AA2 6 ASP B  38  ILE B  46  0                                        
SHEET    2 AA2 6 GLU B  49  ASP B  57 -1  O  LEU B  53   N  LYS B  42           
SHEET    3 AA2 6 THR B   2  VAL B   9  1  N  LEU B   6   O  ASP B  54           
SHEET    4 AA2 6 GLY B  77  ALA B  83  1  O  VAL B  81   N  VAL B   9           
SHEET    5 AA2 6 MET B 111  ASN B 116  1  O  ASN B 116   N  PHE B  82           
SHEET    6 AA2 6 PHE B 141  GLU B 143  1  O  ILE B 142   N  LEU B 113           
LINK         OG  SER A  17                MG    MG A 201     1555   1555  2.28  
LINK         OG  SER B  17                MG    MG B 201     1555   1555  2.30  
LINK        MG    MG A 201                 O2B GDP A 202     1555   1555  2.08  
LINK        MG    MG A 201                 O   HOH A 319     1555   1555  2.15  
LINK        MG    MG A 201                 O   HOH A 302     1555   1555  2.12  
LINK        MG    MG A 201                 O   HOH A 303     1555   1555  2.11  
LINK        MG    MG B 201                 O   HOH B 319     1555   1555  2.07  
LINK        MG    MG B 201                 O2B GDP B 202     1555   1555  2.08  
LINK        MG    MG B 201                 O   HOH B 301     1555   1555  2.13  
LINK        MG    MG B 201                 O   HOH B 303     1555   1555  2.15  
SITE     1 AC1  5 SER A  17  GDP A 202  HOH A 302  HOH A 303                    
SITE     2 AC1  5 HOH A 319                                                     
SITE     1 AC2 19 GLY A  13  VAL A  14  GLY A  15  LYS A  16                    
SITE     2 AC2 19 SER A  17  ALA A  18  PHE A  28  VAL A  29                    
SITE     3 AC2 19 ASP A  30  ASN A 116  LYS A 117  ASP A 119                    
SITE     4 AC2 19 LEU A 120  SER A 145  ALA A 146  LYS A 147                    
SITE     5 AC2 19  MG A 201  HOH A 302  HOH A 303                               
SITE     1 AC3  5 SER B  17  GDP B 202  HOH B 301  HOH B 303                    
SITE     2 AC3  5 HOH B 319                                                     
SITE     1 AC4 19 GLY B  13  VAL B  14  GLY B  15  LYS B  16                    
SITE     2 AC4 19 SER B  17  ALA B  18  PHE B  28  VAL B  29                    
SITE     3 AC4 19 ASP B  30  ASN B 116  LYS B 117  ASP B 119                    
SITE     4 AC4 19 LEU B 120  SER B 145  ALA B 146  LYS B 147                    
SITE     5 AC4 19  MG B 201  HOH B 301  HOH B 303                               
CRYST1   92.766   92.766  118.415  90.00  90.00 120.00 H 3          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      0.010780  0.006224  0.000000        0.00000                         
SCALE2      0.000000  0.012447  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008445        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2  1.000000 -0.000166 -0.000136        0.00188    1                    
MTRIX2   2 -0.000166 -1.000000  0.000009      -53.55845    1                    
MTRIX3   2 -0.000136 -0.000009 -1.000000       -0.01779    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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