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Database: PDB
Entry: 6CTA
LinkDB: 6CTA
Original site: 6CTA 
HEADER    TRANSFERASE/DNA                         22-MAR-18   6CTA              
TITLE     STRUCTURE OF THE HUMAN CGAS-DNA COMPLEX WITH ATP                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIC GMP-AMP SYNTHASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: H-CGAS,2'3'-CGAMP SYNTHASE,MAB-21 DOMAIN-CONTAINING PROTEIN 
COMPND   5 1;                                                                   
COMPND   6 EC: 2.7.7.86;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: DNA (5'-D(P*CP*GP*TP*CP*TP*TP*CP*GP*GP*CP*AP*AP*T)-3');    
COMPND  11 CHAIN: B;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: DNA (5'-D(*AP*AP*AP*TP*TP*GP*CP*CP*GP*AP*AP*GP*AP*CP*GP*A)-
COMPND  15 3');                                                                 
COMPND  16 CHAIN: C;                                                            
COMPND  17 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CGAS, C6ORF150, MB21D1;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  11 ORGANISM_TAXID: 32630;                                               
SOURCE  12 MOL_ID: 3;                                                           
SOURCE  13 SYNTHETIC: YES;                                                      
SOURCE  14 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  15 ORGANISM_TAXID: 32630                                                
KEYWDS    CGAS, STING, INNATE IMMUNITY, TRANSFERASE, TRANSFERASE-DNA COMPLEX    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.ZHOU,A.T.WHITELEY,C.C.DE OLIVEIRA MANN,B.R.MOREHOUSE,J.J.MEKALANOS, 
AUTHOR   2 P.J.KRANZUSCH                                                        
REVDAT   3   17-APR-19 6CTA    1       REMARK                                   
REVDAT   2   01-AUG-18 6CTA    1       JRNL                                     
REVDAT   1   18-JUL-18 6CTA    0                                                
JRNL        AUTH   W.ZHOU,A.T.WHITELEY,C.C.DE OLIVEIRA MANN,B.R.MOREHOUSE,      
JRNL        AUTH 2 R.P.NOWAK,E.S.FISCHER,N.S.GRAY,J.J.MEKALANOS,P.J.KRANZUSCH   
JRNL        TITL   STRUCTURE OF THE HUMAN CGAS-DNA COMPLEX REVEALS ENHANCED     
JRNL        TITL 2 CONTROL OF IMMUNE SURVEILLANCE.                              
JRNL        REF    CELL                          V. 174   300 2018              
JRNL        REFN                   ISSN 1097-4172                               
JRNL        PMID   30007416                                                     
JRNL        DOI    10.1016/J.CELL.2018.06.026                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.78 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.13_2998: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.78                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.83                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 18163                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.214                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1817                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 48.8416 -  6.5293    1.00     1429   159  0.2240 0.2374        
REMARK   3     2  6.5293 -  5.1843    1.00     1319   147  0.2050 0.2208        
REMARK   3     3  5.1843 -  4.5295    1.00     1282   141  0.1675 0.2008        
REMARK   3     4  4.5295 -  4.1156    1.00     1281   143  0.1749 0.2237        
REMARK   3     5  4.1156 -  3.8208    1.00     1263   141  0.1815 0.2399        
REMARK   3     6  3.8208 -  3.5956    1.00     1266   140  0.1972 0.2335        
REMARK   3     7  3.5956 -  3.4156    1.00     1247   139  0.2071 0.2478        
REMARK   3     8  3.4156 -  3.2669    1.00     1254   139  0.2488 0.3157        
REMARK   3     9  3.2669 -  3.1412    1.00     1237   138  0.2499 0.2809        
REMARK   3    10  3.1412 -  3.0328    1.00     1232   136  0.2635 0.3293        
REMARK   3    11  3.0328 -  2.9380    1.00     1239   139  0.2596 0.2909        
REMARK   3    12  2.9380 -  2.8540    1.00     1241   138  0.2914 0.2989        
REMARK   3    13  2.8540 -  2.7789    0.86     1056   117  0.3250 0.4136        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.400           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           3576                                  
REMARK   3   ANGLE     :  0.543           4932                                  
REMARK   3   CHIRALITY :  0.035            540                                  
REMARK   3   PLANARITY :  0.004            517                                  
REMARK   3   DIHEDRAL  : 19.252           2063                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 161 THROUGH 233 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  16.4124 -33.1831   0.2004              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5271 T22:   0.6612                                     
REMARK   3      T33:   0.5363 T12:   0.0063                                     
REMARK   3      T13:  -0.0202 T23:   0.0797                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7991 L22:   0.4444                                     
REMARK   3      L33:   0.1973 L12:   0.3508                                     
REMARK   3      L13:   0.4735 L23:   0.2936                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3301 S12:   0.2896 S13:   0.2404                       
REMARK   3      S21:   0.3434 S22:  -0.2472 S23:   0.2323                       
REMARK   3      S31:  -0.1883 S32:  -0.2716 S33:   0.0004                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 234 THROUGH 272 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  17.3587 -61.4657  -2.9521              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6052 T22:   0.6568                                     
REMARK   3      T33:   0.7861 T12:  -0.1055                                     
REMARK   3      T13:  -0.0471 T23:  -0.1939                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1062 L22:   0.7861                                     
REMARK   3      L33:   0.4245 L12:  -0.0313                                     
REMARK   3      L13:   0.1875 L23:  -0.0133                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4876 S12:   0.1114 S13:  -1.1363                       
REMARK   3      S21:   0.1161 S22:  -0.2101 S23:  -0.0513                       
REMARK   3      S31:   0.1846 S32:  -0.0043 S33:   0.0021                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 273 THROUGH 388 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  19.3014 -46.0992  -0.9915              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3911 T22:   0.5786                                     
REMARK   3      T33:   0.4059 T12:   0.0172                                     
REMARK   3      T13:  -0.0114 T23:  -0.0133                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8576 L22:   0.5988                                     
REMARK   3      L33:   0.4153 L12:   0.0636                                     
REMARK   3      L13:  -0.2536 L23:   0.0905                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0617 S12:   0.2190 S13:  -0.2277                       
REMARK   3      S21:  -0.0714 S22:  -0.0343 S23:   0.0046                       
REMARK   3      S31:   0.2464 S32:  -0.1725 S33:   0.0001                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 389 THROUGH 434 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  33.5160 -30.8280  -2.4296              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3854 T22:   0.5542                                     
REMARK   3      T33:   0.4487 T12:   0.0450                                     
REMARK   3      T13:  -0.0166 T23:   0.0688                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2947 L22:   1.2950                                     
REMARK   3      L33:   0.4795 L12:   0.3085                                     
REMARK   3      L13:  -0.3456 L23:  -0.0320                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0510 S12:   0.1698 S13:   0.2734                       
REMARK   3      S21:   0.0010 S22:  -0.0582 S23:   0.1521                       
REMARK   3      S31:  -0.1781 S32:   0.1183 S33:  -0.0001                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 435 THROUGH 521 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  40.1336 -36.8655  -5.7978              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4125 T22:   0.5841                                     
REMARK   3      T33:   0.4507 T12:   0.0009                                     
REMARK   3      T13:   0.0707 T23:   0.0252                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8504 L22:   0.8773                                     
REMARK   3      L33:   1.4642 L12:   0.2031                                     
REMARK   3      L13:   0.1635 L23:  -0.1705                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1054 S12:   0.1489 S13:   0.0646                       
REMARK   3      S21:  -0.0592 S22:  -0.0486 S23:  -0.3336                       
REMARK   3      S31:  -0.0203 S32:   0.0512 S33:   0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 16 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  14.4619 -29.0524  16.3111              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9803 T22:   1.3171                                     
REMARK   3      T33:   1.0784 T12:  -0.0995                                     
REMARK   3      T13:   0.0077 T23:  -0.0939                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1327 L22:   0.1783                                     
REMARK   3      L33:   0.4003 L12:  -0.1654                                     
REMARK   3      L13:   0.2382 L23:  -0.2883                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1479 S12:  -1.3942 S13:   0.8940                       
REMARK   3      S21:  -0.4854 S22:  -0.4020 S23:   0.7767                       
REMARK   3      S31:   0.1226 S32:  -0.5097 S33:  -0.0017                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 16 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  13.6419 -29.9980  14.2089              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1947 T22:   0.9719                                     
REMARK   3      T33:   1.2142 T12:  -0.0590                                     
REMARK   3      T13:  -0.1062 T23:  -0.0363                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5110 L22:   0.4834                                     
REMARK   3      L33:   1.1376 L12:  -0.6965                                     
REMARK   3      L13:   0.1326 L23:   0.4430                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4406 S12:  -0.9979 S13:   0.5007                       
REMARK   3      S21:  -0.6058 S22:  -0.7667 S23:   0.8430                       
REMARK   3      S31:  -0.1658 S32:  -0.1251 S33:  -0.0010                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6CTA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000233353.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-DEC-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
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                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97918                            
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          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18321                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.779                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.150                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 19.50                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.79                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 18.20                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
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: 4KM5                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.54                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES-NAOH PH 7.0, 1.4 M SODIUM    
REMARK 280  CITRATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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       78.92300            
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      157.84600            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      118.38450            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      197.30750            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       39.46150            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       78.92300            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      157.84600            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      197.30750            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      118.38450            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       39.46150            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3960 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20710 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 721  LIES ON A SPECIAL POSITION.                          
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     SER A   156                                                      
REMARK 465     ASP A   157                                                      
REMARK 465     ALA A   158                                                      
REMARK 465     ALA A   159                                                      
REMARK 465     PRO A   160                                                      
REMARK 465     ARG A   255                                                      
REMARK 465     ASN A   256                                                      
REMARK 465     PRO A   257                                                      
REMARK 465     LYS A   258                                                      
REMARK 465     GLU A   259                                                      
REMARK 465     LYS A   292                                                      
REMARK 465     ASP A   293                                                      
REMARK 465     THR A   294                                                      
REMARK 465     ARG A   300                                                      
REMARK 465     LYS A   301                                                      
REMARK 465     ARG A   302                                                      
REMARK 465     LYS A   365                                                      
REMARK 465     GLU A   366                                                      
REMARK 465     GLY A   367                                                      
REMARK 465     ASN A   368                                                      
REMARK 465     GLY A   369                                                      
REMARK 465     PHE A   370                                                      
REMARK 465     PHE A   522                                                      
REMARK 465      DT B     1                                                      
REMARK 465      DT B     2                                                      
REMARK 465      DT B     3                                                      
REMARK 465      DT B    17                                                      
REMARK 465      DA C    17                                                      
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      DA C   1    O5'                                                 
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    PHE A 203       42.78    -90.95                                   
REMARK 500    SER A 221      -67.99     66.67                                   
REMARK 500    SER A 243     -128.61     56.45                                   
REMARK 500    ARG A 246      -16.07     67.98                                   
REMARK 500    TRP A 343      -70.34   -111.62                                   
REMARK 500    SER A 345      150.55     95.90                                   
REMARK 500    PHE A 516       76.07     51.32                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 721        DISTANCE =  5.91 ANGSTROMS                       
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 602  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 225   OE1                                                    
REMARK 620 2 ASP A 227   OD2  99.1                                              
REMARK 620 3 ATP A 604   O2B 147.8  86.4                                        
REMARK 620 4 ATP A 604   O2G  80.2 139.4  75.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 603  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 227   OD1                                                    
REMARK 620 2 ASP A 319   OD2  74.0                                              
REMARK 620 3 ATP A 604   O1A  60.9 116.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 390   NE2                                                    
REMARK 620 2 CYS A 396   SG  116.1                                              
REMARK 620 3 CYS A 397   SG   97.4 126.8                                        
REMARK 620 4 CYS A 404   SG   99.1 109.4 104.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP A 604                 
DBREF  6CTA A  157   522  UNP    Q8N884   CGAS_HUMAN     157    522             
DBREF  6CTA B    1    17  PDB    6CTA     6CTA             1     17             
DBREF  6CTA C    1    17  PDB    6CTA     6CTA             1     17             
SEQADV 6CTA SER A  156  UNP  Q8N884              EXPRESSION TAG                 
SEQADV 6CTA ASN A  187  UNP  Q8N884    LYS   187 ENGINEERED MUTATION            
SEQADV 6CTA ARG A  195  UNP  Q8N884    LEU   195 ENGINEERED MUTATION            
SEQRES   1 A  367  SER ASP ALA ALA PRO GLY ALA SER LYS LEU ARG ALA VAL          
SEQRES   2 A  367  LEU GLU LYS LEU LYS LEU SER ARG ASP ASP ILE SER THR          
SEQRES   3 A  367  ALA ALA GLY MET VAL ASN GLY VAL VAL ASP HIS LEU LEU          
SEQRES   4 A  367  ARG ARG LEU LYS CYS ASP SER ALA PHE ARG GLY VAL GLY          
SEQRES   5 A  367  LEU LEU ASN THR GLY SER TYR TYR GLU HIS VAL LYS ILE          
SEQRES   6 A  367  SER ALA PRO ASN GLU PHE ASP VAL MET PHE LYS LEU GLU          
SEQRES   7 A  367  VAL PRO ARG ILE GLN LEU GLU GLU TYR SER ASN THR ARG          
SEQRES   8 A  367  ALA TYR TYR PHE VAL LYS PHE LYS ARG ASN PRO LYS GLU          
SEQRES   9 A  367  ASN PRO LEU SER GLN PHE LEU GLU GLY GLU ILE LEU SER          
SEQRES  10 A  367  ALA SER LYS MET LEU SER LYS PHE ARG LYS ILE ILE LYS          
SEQRES  11 A  367  GLU GLU ILE ASN ASP ILE LYS ASP THR ASP VAL ILE MET          
SEQRES  12 A  367  LYS ARG LYS ARG GLY GLY SER PRO ALA VAL THR LEU LEU          
SEQRES  13 A  367  ILE SER GLU LYS ILE SER VAL ASP ILE THR LEU ALA LEU          
SEQRES  14 A  367  GLU SER LYS SER SER TRP PRO ALA SER THR GLN GLU GLY          
SEQRES  15 A  367  LEU ARG ILE GLN ASN TRP LEU SER ALA LYS VAL ARG LYS          
SEQRES  16 A  367  GLN LEU ARG LEU LYS PRO PHE TYR LEU VAL PRO LYS HIS          
SEQRES  17 A  367  ALA LYS GLU GLY ASN GLY PHE GLN GLU GLU THR TRP ARG          
SEQRES  18 A  367  LEU SER PHE SER HIS ILE GLU LYS GLU ILE LEU ASN ASN          
SEQRES  19 A  367  HIS GLY LYS SER LYS THR CYS CYS GLU ASN LYS GLU GLU          
SEQRES  20 A  367  LYS CYS CYS ARG LYS ASP CYS LEU LYS LEU MET LYS TYR          
SEQRES  21 A  367  LEU LEU GLU GLN LEU LYS GLU ARG PHE LYS ASP LYS LYS          
SEQRES  22 A  367  HIS LEU ASP LYS PHE SER SER TYR HIS VAL LYS THR ALA          
SEQRES  23 A  367  PHE PHE HIS VAL CYS THR GLN ASN PRO GLN ASP SER GLN          
SEQRES  24 A  367  TRP ASP ARG LYS ASP LEU GLY LEU CYS PHE ASP ASN CYS          
SEQRES  25 A  367  VAL THR TYR PHE LEU GLN CYS LEU ARG THR GLU LYS LEU          
SEQRES  26 A  367  GLU ASN TYR PHE ILE PRO GLU PHE ASN LEU PHE SER SER          
SEQRES  27 A  367  ASN LEU ILE ASP LYS ARG SER LYS GLU PHE LEU THR LYS          
SEQRES  28 A  367  GLN ILE GLU TYR GLU ARG ASN ASN GLU PHE PRO VAL PHE          
SEQRES  29 A  367  ASP GLU PHE                                                  
SEQRES   1 B   17   DT  DT  DT  DC  DG  DT  DC  DT  DT  DC  DG  DG  DC          
SEQRES   2 B   17   DA  DA  DT  DT                                              
SEQRES   1 C   17   DA  DA  DA  DT  DT  DG  DC  DC  DG  DA  DA  DG  DA          
SEQRES   2 C   17   DC  DG  DA  DA                                              
HET     ZN  A 601       1                                                       
HET     MG  A 602       1                                                       
HET     MG  A 603       1                                                       
HET    ATP  A 604      31                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
FORMUL   4   ZN    ZN 2+                                                        
FORMUL   5   MG    2(MG 2+)                                                     
FORMUL   7  ATP    C10 H16 N5 O13 P3                                            
FORMUL   8  HOH   *21(H2 O)                                                     
HELIX    1 AA1 GLY A  161  LEU A  172  1                                  12    
HELIX    2 AA2 SER A  175  LYS A  198  1                                  24    
HELIX    3 AA3 GLY A  212  GLU A  216  1                                   5    
HELIX    4 AA4 ASN A  260  GLN A  264  5                                   5    
HELIX    5 AA5 SER A  272  ASN A  289  1                                  18    
HELIX    6 AA6 PRO A  331  GLN A  335  5                                   5    
HELIX    7 AA7 SER A  345  ARG A  353  1                                   9    
HELIX    8 AA8 PHE A  379  ASN A  389  1                                  11    
HELIX    9 AA9 ASN A  399  LYS A  403  5                                   5    
HELIX   10 AB1 CYS A  405  PHE A  424  1                                  20    
HELIX   11 AB2 LYS A  428  PHE A  433  5                                   6    
HELIX   12 AB3 SER A  434  ASN A  449  1                                  16    
HELIX   13 AB4 GLN A  451  LYS A  458  5                                   8    
HELIX   14 AB5 ASP A  459  GLU A  478  1                                  20    
HELIX   15 AB6 ASP A  497  ASN A  514  1                                  18    
HELIX   16 AB7 PHE A  516  GLU A  521  1                                   6    
SHEET    1 AA1 7 VAL A 206  THR A 211  0                                        
SHEET    2 AA1 7 GLU A 225  GLU A 233 -1  O  LYS A 231   N  GLY A 207           
SHEET    3 AA1 7 ILE A 316  SER A 326  1  O  GLU A 325   N  LEU A 232           
SHEET    4 AA1 7 PHE A 357  PRO A 361 -1  O  LEU A 359   N  LEU A 324           
SHEET    5 AA1 7 TRP A 375  SER A 378 -1  O  SER A 378   N  TYR A 358           
SHEET    6 AA1 7 TYR A 248  PHE A 253 -1  N  TYR A 249   O  TRP A 375           
SHEET    7 AA1 7 ILE A 237  GLU A 241 -1  N  GLU A 240   O  PHE A 250           
SHEET    1 AA2 5 VAL A 206  THR A 211  0                                        
SHEET    2 AA2 5 GLU A 225  GLU A 233 -1  O  LYS A 231   N  GLY A 207           
SHEET    3 AA2 5 ILE A 316  SER A 326  1  O  GLU A 325   N  LEU A 232           
SHEET    4 AA2 5 VAL A 308  ILE A 312 -1  N  ILE A 312   O  ILE A 316           
SHEET    5 AA2 5 VAL A 296  MET A 298 -1  N  ILE A 297   O  LEU A 311           
SHEET    1 AA3 2 LEU A 266  GLU A 267  0                                        
SHEET    2 AA3 2 ILE A 270  LEU A 271 -1  O  ILE A 270   N  GLU A 267           
LINK         OE1 GLU A 225                MG    MG A 602     1555   1555  1.95  
LINK         OD1 ASP A 227                MG    MG A 603     1555   1555  2.92  
LINK         OD2 ASP A 227                MG    MG A 602     1555   1555  1.94  
LINK         OD2 ASP A 319                MG    MG A 603     1555   1555  2.36  
LINK         NE2 HIS A 390                ZN    ZN A 601     1555   1555  2.07  
LINK         SG  CYS A 396                ZN    ZN A 601     1555   1555  2.36  
LINK         SG  CYS A 397                ZN    ZN A 601     1555   1555  2.32  
LINK         SG  CYS A 404                ZN    ZN A 601     1555   1555  2.35  
LINK        MG    MG A 602                 O2B ATP A 604     1555   1555  2.04  
LINK        MG    MG A 602                 O2G ATP A 604     1555   1555  2.26  
LINK        MG    MG A 603                 O1A ATP A 604     1555   1555  2.50  
CISPEP   1 SER A  305    PRO A  306          0         4.01                     
SITE     1 AC1  4 HIS A 390  CYS A 396  CYS A 397  CYS A 404                    
SITE     1 AC2  4 SER A 213  GLU A 225  ASP A 227  ATP A 604                    
SITE     1 AC3  4 GLU A 225  ASP A 227  ASP A 319  ATP A 604                    
SITE     1 AC4 14 GLY A 212  SER A 213  GLU A 225  ASP A 227                    
SITE     2 AC4 14 ARG A 376  SER A 380  GLU A 383  LYS A 414                    
SITE     3 AC4 14 SER A 435  TYR A 436  LYS A 439   MG A 602                    
SITE     4 AC4 14  MG A 603  HOH A 702                                          
CRYST1   99.782   99.782  236.769  90.00  90.00 120.00 P 61 2 2     12          
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      0.010022  0.005786  0.000000        0.00000                         
SCALE2      0.000000  0.011572  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004224        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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