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Database: PDB
Entry: 6EPP
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Original site: 6EPP 
HEADER    SIGNALING PROTEIN                       12-OCT-17   6EPP              
TITLE     RAS GUANINE EXCHANGE FACTOR SOS1 (REM-CDC25) IN COMPLEX WITH          
TITLE    2 KRAS(G12C) AND FRAGMENT SCREENING HIT F4                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GTPASE KRAS;                                               
COMPND   3 CHAIN: R;                                                            
COMPND   4 SYNONYM: K-RAS 2,KI-RAS,C-K-RAS,C-KI-RAS;                            
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 OTHER_DETAILS: N-TERMINAL G IS A CLONING ARTIFACT;                   
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: SON OF SEVENLESS HOMOLOG 1;                                
COMPND  10 CHAIN: S;                                                            
COMPND  11 SYNONYM: SOS-1;                                                      
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MUTATION: YES;                                                       
COMPND  14 OTHER_DETAILS: MUTATION K563G IS A CLONING ARTIFACT                  
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;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: SOS1;                                                          
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    GUANINE NUCLEOTIDE EXCHANGE FACTOR, GEF, FRAGMENT SCREEN, GTPASE,     
KEYWDS   2 SIGNALING PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.C.HILLIG,D.MOOSMAYER,A.HILPMANN,B.BADER,J.SCHROEDER,L.WORTMANN,     
AUTHOR   2 B.SAUTIER,J.KAHMANN,D.WEGENER,H.BRIEM,K.PETERSEN,V.BADOCK            
REVDAT   2   20-FEB-19 6EPP    1       JRNL                                     
REVDAT   1   06-FEB-19 6EPP    0                                                
JRNL        AUTH   R.C.HILLIG,B.SAUTIER,J.SCHROEDER,D.MOOSMAYER,A.HILPMANN,     
JRNL        AUTH 2 C.M.STEGMANN,N.D.WERBECK,H.BRIEM,U.BOEMER,J.WEISKE,V.BADOCK, 
JRNL        AUTH 3 J.MASTOURI,K.PETERSEN,G.SIEMEISTER,J.D.KAHMANN,D.WEGENER,    
JRNL        AUTH 4 N.BOHNKE,K.EIS,K.GRAHAM,L.WORTMANN,F.VON NUSSBAUM,B.BADER    
JRNL        TITL   DISCOVERY OF POTENT SOS1 INHIBITORS THAT BLOCK RAS           
JRNL        TITL 2 ACTIVATION VIA DISRUPTION OF THE RAS-SOS1 INTERACTION.       
JRNL        REF    PROC. NATL. ACAD. SCI.        V. 116  2551 2019              
JRNL        REF  2 U.S.A.                                                       
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   30683722                                                     
JRNL        DOI    10.1073/PNAS.1812963116                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.43                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 42657                          
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) : 0.178                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.201                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2165                            
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3090                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.97                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2910                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 168                          
REMARK   3   BIN FREE R VALUE                    : 0.3210                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5163                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 22                                      
REMARK   3   SOLVENT ATOMS            : 299                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 47.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 54.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.51000                                             
REMARK   3    B22 (A**2) : -0.51000                                             
REMARK   3    B33 (A**2) : 1.03000                                              
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): 0.225         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.176         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.132         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.549        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.955                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5355 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5022 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7241 ; 1.517 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11663 ; 1.011 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   635 ; 5.723 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   269 ;35.531 ;23.792       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   989 ;17.970 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    45 ;17.596 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   789 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5843 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1090 ; 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):  2528 ; 3.435 ; 3.331       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2527 ; 3.431 ; 3.328       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3161 ; 5.576 ; 7.451       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3162 ; 5.576 ; 7.457       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2827 ; 4.502 ; 3.894       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2828 ; 4.501 ; 3.896       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  4079 ; 7.216 ; 8.425       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 21984 ;11.066 ;63.255       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 21983 ;11.064 ;63.249       
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  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   R     1        R   167                          
REMARK   3    ORIGIN FOR THE GROUP (A): 178.7690 141.1150 262.1990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0947 T22:   0.1225                                     
REMARK   3      T33:   0.0124 T12:  -0.0422                                     
REMARK   3      T13:   0.0115 T23:   0.0030                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3259 L22:   3.5503                                     
REMARK   3      L33:   1.8640 L12:   0.2640                                     
REMARK   3      L13:  -0.0938 L23:  -0.5982                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0084 S12:   0.0509 S13:  -0.0059                       
REMARK   3      S21:  -0.0458 S22:  -0.0665 S23:  -0.1845                       
REMARK   3      S31:  -0.0798 S32:   0.2903 S33:   0.0748                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   S   568        S   743                          
REMARK   3    ORIGIN FOR THE GROUP (A): 162.6360 118.7880 226.1600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2841 T22:   0.2725                                     
REMARK   3      T33:   0.0330 T12:   0.0707                                     
REMARK   3      T13:   0.0015 T23:  -0.0811                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0908 L22:   2.4258                                     
REMARK   3      L33:   3.0130 L12:   0.5748                                     
REMARK   3      L13:  -1.3531 L23:   0.6587                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1043 S12:   0.6725 S13:  -0.3096                       
REMARK   3      S21:  -0.5228 S22:  -0.1043 S23:  -0.0082                       
REMARK   3      S31:  -0.1148 S32:  -0.3178 S33:   0.2086                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   S   752        S  1044                          
REMARK   3    ORIGIN FOR THE GROUP (A): 172.3830 115.5220 268.1480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1254 T22:   0.1059                                     
REMARK   3      T33:   0.0214 T12:   0.0374                                     
REMARK   3      T13:   0.0143 T23:  -0.0059                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8094 L22:   1.0007                                     
REMARK   3      L33:   2.2566 L12:  -0.0627                                     
REMARK   3      L13:   0.2663 L23:  -0.4388                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0269 S12:  -0.0725 S13:  -0.1037                       
REMARK   3      S21:   0.0062 S22:   0.0123 S23:  -0.0512                       
REMARK   3      S31:   0.2363 S32:   0.0385 S33:   0.0146                       
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 6EPP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-OCT-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200006898.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-JUL-14                          
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               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9762                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44844                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.430                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 9.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: 1BKD                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: DROPS MADE FROM KRAS SOS1 COMPLEX        
REMARK 280  (14.4 MG/ML IN 5 MM TRIS PH 7.5, 100MM NACL) AND RESERVOIR          
REMARK 280  SOLUTION (2.9 TO 3.4 M SODIUM FORMATE, 100 MM MES PH 6.5).          
REMARK 280  FRAGMENT SOAKED AT 25 MM FOR THREE DAYS AT 277 K USING A 500 MM     
REMARK 280  FRAGMENT STOCK SOLUTION IN DMSO. CRYO BUFFER 0.1 M MES PH 6.5,      
REMARK 280  3.5 M SODIUM FORMATE, 20 GLYCEROL, 25 MM FRAGMENT, VAPOR            
REMARK 280  DIFFUSION, HANGING DROP                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z                                                 
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       74.99000            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       74.99000            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      100.18500            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       74.99000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       74.99000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000      100.18500            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       74.99000            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       74.99000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000      100.18500            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       74.99000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       74.99000            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000      100.18500            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       74.99000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       74.99000            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000      100.18500            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       74.99000            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       74.99000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      100.18500            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       74.99000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       74.99000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000      100.18500            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       74.99000            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       74.99000            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      100.18500            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: R, S                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY R     0                                                      
REMARK 465     LYS R   169                                                      
REMARK 465     GLY S   563                                                      
REMARK 465     GLU S   564                                                      
REMARK 465     THR S   656                                                      
REMARK 465     GLU S   657                                                      
REMARK 465     ALA S   658                                                      
REMARK 465     ASP S   659                                                      
REMARK 465     ARG S   660                                                      
REMARK 465     ILE S   661                                                      
REMARK 465     ALA S   662                                                      
REMARK 465     ILE S   663                                                      
REMARK 465     GLU S   664                                                      
REMARK 465     ASN S   665                                                      
REMARK 465     GLY S   666                                                      
REMARK 465     ASP S   667                                                      
REMARK 465     GLN S   668                                                      
REMARK 465     PRO S   669                                                      
REMARK 465     LEU S   670                                                      
REMARK 465     ARG S   744                                                      
REMARK 465     ASP S   745                                                      
REMARK 465     ASN S   746                                                      
REMARK 465     GLY S   747                                                      
REMARK 465     PRO S   748                                                      
REMARK 465     GLY S   749                                                      
REMARK 465     HIS S   750                                                      
REMARK 465     ASN S   751                                                      
REMARK 465     PRO S  1047                                                      
REMARK 465     GLY S  1048                                                      
REMARK 465     THR S  1049                                                      
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   NH1  ARG S   568     O    GLU S   654              2.12            
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    TYR R  32      124.67   -172.76                                   
REMARK 500    ALA R  59      128.57    -39.98                                   
REMARK 500    SER R 118      -96.99   -112.60                                   
REMARK 500    PRO R 121     -179.75    -67.55                                   
REMARK 500    ARG R 149      -10.42     68.79                                   
REMARK 500    GLN S 566     -158.09    -73.14                                   
REMARK 500    ARG S 568       91.79     58.69                                   
REMARK 500    LYS S 595      -33.19     71.93                                   
REMARK 500    ALA S 672      -88.37     79.59                                   
REMARK 500    THR S 753      148.20     54.13                                   
REMARK 500    HIS S 764     -101.58   -113.68                                   
REMARK 500    PRO S 924      154.23    -46.88                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL R 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BOQ S 1101                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6EPL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6EPM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6EPN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6EPO   RELATED DB: PDB                                   
DBREF  6EPP R    1   169  UNP    P01116   RASK_HUMAN       1    169             
DBREF  6EPP S  563  1049  UNP    Q07889   SOS1_HUMAN     563   1049             
SEQADV 6EPP GLY R    0  UNP  P01116              EXPRESSION TAG                 
SEQADV 6EPP CYS R   12  UNP  P01116    GLY    12 ENGINEERED MUTATION            
SEQADV 6EPP SER R  118  UNP  P01116    CYS   118 ENGINEERED MUTATION            
SEQADV 6EPP GLU R  126  UNP  P01116    ASP   126 ENGINEERED MUTATION            
SEQADV 6EPP SER R  127  UNP  P01116    THR   127 ENGINEERED MUTATION            
SEQADV 6EPP ARG R  128  UNP  P01116    LYS   128 ENGINEERED MUTATION            
SEQADV 6EPP GLY S  563  UNP  Q07889    LYS   563 CONFLICT                       
SEQRES   1 R  170  GLY MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA CYS          
SEQRES   2 R  170  GLY VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN          
SEQRES   3 R  170  ASN HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP          
SEQRES   4 R  170  SER TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS          
SEQRES   5 R  170  LEU LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR          
SEQRES   6 R  170  SER ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY          
SEQRES   7 R  170  PHE LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE          
SEQRES   8 R  170  GLU ASP ILE HIS HIS TYR ARG GLU GLN ILE LYS ARG VAL          
SEQRES   9 R  170  LYS ASP SER GLU ASP VAL PRO MET VAL LEU VAL GLY ASN          
SEQRES  10 R  170  LYS SER ASP LEU PRO SER ARG THR VAL GLU SER ARG GLN          
SEQRES  11 R  170  ALA GLN ASP LEU ALA ARG SER TYR GLY ILE PRO PHE ILE          
SEQRES  12 R  170  GLU THR SER ALA LYS THR ARG GLN GLY VAL ASP ASP ALA          
SEQRES  13 R  170  PHE TYR THR LEU VAL ARG GLU ILE ARG LYS HIS LYS GLU          
SEQRES  14 R  170  LYS                                                          
SEQRES   1 S  487  GLY GLU GLU GLN MET ARG LEU PRO SER ALA ASP VAL TYR          
SEQRES   2 S  487  ARG PHE ALA GLU PRO ASP SER GLU GLU ASN ILE ILE PHE          
SEQRES   3 S  487  GLU GLU ASN MET GLN PRO LYS ALA GLY ILE PRO ILE ILE          
SEQRES   4 S  487  LYS ALA GLY THR VAL ILE LYS LEU ILE GLU ARG LEU THR          
SEQRES   5 S  487  TYR HIS MET TYR ALA ASP PRO ASN PHE VAL ARG THR PHE          
SEQRES   6 S  487  LEU THR THR TYR ARG SER PHE CYS LYS PRO GLN GLU LEU          
SEQRES   7 S  487  LEU SER LEU ILE ILE GLU ARG PHE GLU ILE PRO GLU PRO          
SEQRES   8 S  487  GLU PRO THR GLU ALA ASP ARG ILE ALA ILE GLU ASN GLY          
SEQRES   9 S  487  ASP GLN PRO LEU SER ALA GLU LEU LYS ARG PHE ARG LYS          
SEQRES  10 S  487  GLU TYR ILE GLN PRO VAL GLN LEU ARG VAL LEU ASN VAL          
SEQRES  11 S  487  CYS ARG HIS TRP VAL GLU HIS HIS PHE TYR ASP PHE GLU          
SEQRES  12 S  487  ARG ASP ALA TYR LEU LEU GLN ARG MET GLU GLU PHE ILE          
SEQRES  13 S  487  GLY THR VAL ARG GLY LYS ALA MET LYS LYS TRP VAL GLU          
SEQRES  14 S  487  SER ILE THR LYS ILE ILE GLN ARG LYS LYS ILE ALA ARG          
SEQRES  15 S  487  ASP ASN GLY PRO GLY HIS ASN ILE THR PHE GLN SER SER          
SEQRES  16 S  487  PRO PRO THR VAL GLU TRP HIS ILE SER ARG PRO GLY HIS          
SEQRES  17 S  487  ILE GLU THR PHE ASP LEU LEU THR LEU HIS PRO ILE GLU          
SEQRES  18 S  487  ILE ALA ARG GLN LEU THR LEU LEU GLU SER ASP LEU TYR          
SEQRES  19 S  487  ARG ALA VAL GLN PRO SER GLU LEU VAL GLY SER VAL TRP          
SEQRES  20 S  487  THR LYS GLU ASP LYS GLU ILE ASN SER PRO ASN LEU LEU          
SEQRES  21 S  487  LYS MET ILE ARG HIS THR THR ASN LEU THR LEU TRP PHE          
SEQRES  22 S  487  GLU LYS CYS ILE VAL GLU THR GLU ASN LEU GLU GLU ARG          
SEQRES  23 S  487  VAL ALA VAL VAL SER ARG ILE ILE GLU ILE LEU GLN VAL          
SEQRES  24 S  487  PHE GLN GLU LEU ASN ASN PHE ASN GLY VAL LEU GLU VAL          
SEQRES  25 S  487  VAL SER ALA MET ASN SER SER PRO VAL TYR ARG LEU ASP          
SEQRES  26 S  487  HIS THR PHE GLU GLN ILE PRO SER ARG GLN LYS LYS ILE          
SEQRES  27 S  487  LEU GLU GLU ALA HIS GLU LEU SER GLU ASP HIS TYR LYS          
SEQRES  28 S  487  LYS TYR LEU ALA LYS LEU ARG SER ILE ASN PRO PRO CYS          
SEQRES  29 S  487  VAL PRO PHE PHE GLY ILE TYR LEU THR ASN ILE LEU LYS          
SEQRES  30 S  487  THR GLU GLU GLY ASN PRO GLU VAL LEU LYS ARG HIS GLY          
SEQRES  31 S  487  LYS GLU LEU ILE ASN PHE SER LYS ARG ARG LYS VAL ALA          
SEQRES  32 S  487  GLU ILE THR GLY GLU ILE GLN GLN TYR GLN ASN GLN PRO          
SEQRES  33 S  487  TYR CYS LEU ARG VAL GLU SER ASP ILE LYS ARG PHE PHE          
SEQRES  34 S  487  GLU ASN LEU ASN PRO MET GLY ASN SER MET GLU LYS GLU          
SEQRES  35 S  487  PHE THR ASP TYR LEU PHE ASN LYS SER LEU GLU ILE GLU          
SEQRES  36 S  487  PRO ARG ASN PRO LYS PRO LEU PRO ARG PHE PRO LYS LYS          
SEQRES  37 S  487  TYR SER TYR PRO LEU LYS SER PRO GLY VAL ARG PRO SER          
SEQRES  38 S  487  ASN PRO ARG PRO GLY THR                                      
HET    GOL  R 201       6                                                       
HET    BOQ  S1101      16                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     BOQ ETHYL 2-(AMINOMETHYL)-5-~{TERT}-BUTYL-FURAN-3-                   
HETNAM   2 BOQ  CARBOXYLATE                                                     
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  GOL    C3 H8 O3                                                     
FORMUL   4  BOQ    C12 H19 N O3                                                 
FORMUL   5  HOH   *299(H2 O)                                                    
HELIX    1 AA1 GLY R   15  GLN R   25  1                                  11    
HELIX    2 AA2 ILE R   36  SER R   39  5                                   4    
HELIX    3 AA3 TYR R   64  ALA R   66  5                                   3    
HELIX    4 AA4 MET R   67  THR R   74  1                                   8    
HELIX    5 AA5 ASN R   86  ASP R   92  1                                   7    
HELIX    6 AA6 ASP R   92  LYS R  104  1                                  13    
HELIX    7 AA7 GLU R  126  GLY R  138  1                                  13    
HELIX    8 AA8 GLY R  151  GLU R  168  1                                  18    
HELIX    9 AA9 TYR S  575  GLU S  579  5                                   5    
HELIX   10 AB1 THR S  605  THR S  614  1                                  10    
HELIX   11 AB2 ASP S  620  TYR S  631  1                                  12    
HELIX   12 AB3 ARG S  632  PHE S  634  5                                   3    
HELIX   13 AB4 LYS S  636  GLU S  649  1                                  14    
HELIX   14 AB5 ALA S  672  TYR S  681  1                                  10    
HELIX   15 AB6 TYR S  681  HIS S  700  1                                  20    
HELIX   16 AB7 PHE S  701  ASP S  707  1                                   7    
HELIX   17 AB8 ASP S  707  VAL S  721  1                                  15    
HELIX   18 AB9 GLY S  723  ILE S  742  1                                  20    
HELIX   19 AC1 HIS S  770  PHE S  774  5                                   5    
HELIX   20 AC2 HIS S  780  VAL S  799  1                                  20    
HELIX   21 AC3 GLN S  800  LYS S  811  5                                  12    
HELIX   22 AC4 ASP S  813  SER S  818  1                                   6    
HELIX   23 AC5 SER S  818  GLU S  841  1                                  24    
HELIX   24 AC6 ASN S  844  LEU S  865  1                                  22    
HELIX   25 AC7 ASN S  867  SER S  880  1                                  14    
HELIX   26 AC8 SER S  880  ARG S  885  1                                   6    
HELIX   27 AC9 LEU S  886  ILE S  893  1                                   8    
HELIX   28 AD1 PRO S  894  LEU S  907  1                                  14    
HELIX   29 AD2 SER S  908  ILE S  922  1                                  15    
HELIX   30 AD3 PHE S  930  GLY S  943  1                                  14    
HELIX   31 AD4 PHE S  958  TYR S  974  1                                  17    
HELIX   32 AD5 GLU S  984  ASN S  993  1                                  10    
HELIX   33 AD6 MET S 1001  GLU S 1017  1                                  17    
SHEET    1 AA1 6 ARG R  41  ILE R  46  0                                        
SHEET    2 AA1 6 GLU R  49  ASP R  57 -1  O  CYS R  51   N  VAL R  44           
SHEET    3 AA1 6 GLU R   3  GLY R  10  1  N  TYR R   4   O  LEU R  52           
SHEET    4 AA1 6 GLY R  77  ALA R  83  1  O  LEU R  79   N  VAL R   9           
SHEET    5 AA1 6 MET R 111  LYS R 117  1  O  ASN R 116   N  PHE R  82           
SHEET    6 AA1 6 PHE R 141  SER R 145  1  O  THR R 144   N  GLY R 115           
SHEET    1 AA2 4 ILE S 586  MET S 592  0                                        
SHEET    2 AA2 4 PRO S 599  GLY S 604 -1  O  ALA S 603   N  ILE S 587           
SHEET    3 AA2 4 LYS S 953  ASN S 957 -1  O  ILE S 956   N  GLY S 604           
SHEET    4 AA2 4 VAL S 947  ARG S 950 -1  N  ARG S 950   O  LYS S 953           
CISPEP   1 LEU R  120    PRO R  121          0         9.71                     
CISPEP   2 PRO S  924    PRO S  925          0         0.56                     
CISPEP   3 ASN S 1020    PRO S 1021          0        10.34                     
SITE     1 AC1  3 ARG R  68  HIS R  95  GLN R  99                               
SITE     1 AC2  5 VAL S 883  TYR S 884  ASP S 887  PHE S 890                    
SITE     2 AC2  5 HOH S1249                                                     
CRYST1  149.980  149.980  200.370  90.00  90.00  90.00 I 4 2 2      16          
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      0.006668  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006668  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004991        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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