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Database: PDB
Entry: 5YY1
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Original site: 5YY1 
HEADER    TRANSFERASE                             07-DEC-17   5YY1              
TITLE     CO-CRYSTAL STRUCTURE OF KRAS (G12C) COVALENTLY BOUND WITH QUINAZOLINE 
TITLE    2 BASED INHIBITOR JBI739                                               
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;                                                     
COMPND   6 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    KRAS, G12C, TRANSFERASE                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.SWAMINATHAN,M.K.THAKUR,S.KANDAN,A.GAUTAM,M.KANAVALLI,P.SIMHADRI,    
AUTHOR   2 R.GOSU                                                               
REVDAT   1   18-APR-18 5YY1    0                                                
JRNL        AUTH   S.SWAMINATHAN,M.K.THAKUR,S.KANDAN,A.GAUTAM,M.KANAVALLI,      
JRNL        AUTH 2 P.SIMHADRI,R.GOSU                                            
JRNL        TITL   CO-CRYSTAL STRUCTURE OF KRAS (G12C) COVALENTLY BOUND WITH    
JRNL        TITL 2 QUINAZOLINE BASED INHIBITOR JBI739                           
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.69 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 1.69                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.77                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 19773                          
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) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1067                            
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) : 1.69                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1012                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 68.69                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3190                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 50                           
REMARK   3   BIN FREE R VALUE                    : 0.4480                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1348                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 69                                      
REMARK   3   SOLVENT ATOMS            : 140                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.81                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.54000                                              
REMARK   3    B22 (A**2) : -0.28000                                             
REMARK   3    B33 (A**2) : -0.26000                                             
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): 0.117         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.115         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.075         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.216         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1451 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1270 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1964 ; 1.222 ; 2.018       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2957 ; 0.709 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   173 ; 4.864 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    66 ;37.029 ;24.242       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   252 ;13.431 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;16.814 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   215 ; 0.060 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1615 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   283 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   309 ; 0.200 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1304 ; 0.188 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   714 ; 0.191 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):   820 ; 0.079 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   101 ; 0.131 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     5 ; 0.099 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    28 ; 0.191 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.137 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   910 ; 0.628 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   351 ; 0.101 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1377 ; 0.930 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   687 ; 1.277 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   585 ; 1.931 ; 4.500       
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 : 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 5YY1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-DEC-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300006113.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-JUL-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54178                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000 V706                      
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000 V706                      
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21722                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.690                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : 0.09200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35900                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: 5F2E                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.94                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01M TRI-SODIUM CITRATE, 33% (W/V)      
REMARK 280  PEG 6000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       20.19550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       44.62100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       25.86500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       44.62100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.19550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       25.86500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: 870 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 8070 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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 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  31    CD   OE1  OE2                                       
REMARK 470     GLN A  70    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 107    CG   CD   OE1  OE2                                  
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    ALA A  59     -153.61   -162.11                                   
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   O3B  89.4                                              
REMARK 620 3 HOH A 324   O    94.3  86.2                                        
REMARK 620 4 HOH A 312   O    82.1  92.4 176.1                                  
REMARK 620 5 HOH A 341   O   174.7  89.6  90.9  92.7                            
REMARK 620 6 HOH A 377   O    89.8 174.3  88.2  93.1  91.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 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 94F A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 205                 
DBREF  5YY1 A    1   169  UNP    P01116   RASK_HUMAN       1    169             
SEQADV 5YY1 GLY A    0  UNP  P01116              EXPRESSION TAG                 
SEQADV 5YY1 CYS A   12  UNP  P01116    GLY    12 VARIANT                        
SEQADV 5YY1 SER A   51  UNP  P01116    CYS    51 ENGINEERED MUTATION            
SEQADV 5YY1 LEU A   80  UNP  P01116    CYS    80 ENGINEERED MUTATION            
SEQADV 5YY1 SER A  118  UNP  P01116    CYS   118 ENGINEERED MUTATION            
SEQRES   1 A  170  GLY MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA CYS          
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 SER          
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 LEU 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                                                          
HET     MG  A 201       1                                                       
HET    GDP  A 202      28                                                       
HET    94F  A 203      32                                                       
HET    EDO  A 204       4                                                       
HET    EDO  A 205       4                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM     94F 1-[4-[6-CHLORANYL-8-FLUORANYL-7-[2-(TRIFLUOROMETHYL)             
HETNAM   2 94F  PHENYL]QUINAZOLIN-4-YL]PIPERAZIN-1-YL]PROPAN-1-ONE              
HETNAM     EDO ETHANE-1,2-DIOL                                                  
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2   MG    MG 2+                                                        
FORMUL   3  GDP    C10 H15 N5 O11 P2                                            
FORMUL   4  94F    C22 H19 CL F4 N4 O                                           
FORMUL   5  EDO    2(C2 H6 O2)                                                  
FORMUL   7  HOH   *140(H2 O)                                                    
HELIX    1 AA1 GLY A   15  ASN A   26  1                                  12    
HELIX    2 AA2 SER A   65  THR A   74  1                                  10    
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  169  1                                  19    
SHEET    1 AA1 6 ASP A  38  ILE A  46  0                                        
SHEET    2 AA1 6 GLU A  49  ASP A  57 -1  O  ILE A  55   N  TYR A  40           
SHEET    3 AA1 6 THR A   2  VAL A   9  1  N  TYR A   4   O  ASP A  54           
SHEET    4 AA1 6 GLY A  77  ALA A  83  1  O  LEU A  79   N  VAL A   9           
SHEET    5 AA1 6 MET A 111  ASN A 116  1  O  VAL A 114   N  LEU A  80           
SHEET    6 AA1 6 PHE A 141  GLU A 143  1  O  ILE A 142   N  LEU A 113           
LINK         SG  CYS A  12                 C14 94F A 203     1555   1555  1.62  
LINK         OG  SER A  17                MG    MG A 201     1555   1555  2.18  
LINK        MG    MG A 201                 O3B GDP A 202     1555   1555  2.16  
LINK        MG    MG A 201                 O   HOH A 324     1555   1555  2.07  
LINK        MG    MG A 201                 O   HOH A 312     1555   1555  2.13  
LINK        MG    MG A 201                 O   HOH A 341     1555   1555  2.12  
LINK        MG    MG A 201                 O   HOH A 377     1555   1555  2.11  
SITE     1 AC1  6 SER A  17  GDP A 202  HOH A 312  HOH A 324                    
SITE     2 AC1  6 HOH A 341  HOH A 377                                          
SITE     1 AC2 25 GLY A  13  VAL A  14  GLY A  15  LYS A  16                    
SITE     2 AC2 25 SER A  17  ALA A  18  PHE A  28  VAL A  29                    
SITE     3 AC2 25 ASP A  30  ASN A 116  LYS A 117  ASP A 119                    
SITE     4 AC2 25 LEU A 120  SER A 145  ALA A 146  LYS A 147                    
SITE     5 AC2 25  MG A 201  HOH A 312  HOH A 324  HOH A 325                    
SITE     6 AC2 25 HOH A 341  HOH A 360  HOH A 390  HOH A 393                    
SITE     7 AC2 25 HOH A 402                                                     
SITE     1 AC3 19 VAL A   9  CYS A  12  LYS A  16  PRO A  34                    
SITE     2 AC3 19 ALA A  59  GLY A  60  GLN A  61  GLU A  62                    
SITE     3 AC3 19 TYR A  64  ARG A  68  ASP A  69  MET A  72                    
SITE     4 AC3 19 HIS A  95  TYR A  96  GLN A  99  ILE A 100                    
SITE     5 AC3 19 VAL A 103  EDO A 205  HOH A 341                               
SITE     1 AC4  5 GLY A 138  ILE A 139  PRO A 140  GLU A 162                    
SITE     2 AC4  5 LYS A 165                                                     
SITE     1 AC5  6 GLU A  62  HIS A  95  94F A 203  HOH A 305                    
SITE     2 AC5  6 HOH A 310  HOH A 335                                          
CRYST1   40.391   51.730   89.242  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.024758  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.019331  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011205        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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