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Database: PDB
Entry: 4O67
LinkDB: 4O67
Original site: 4O67 
HEADER    TRANSFERASE                             20-DEC-13   4O67              
TITLE     HUMAN CYCLIC GMP-AMP SYNTHASE (CGAS) IN COMPLEX WITH GAMP             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIC GMP-AMP SYNTHASE;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 161-522;                                      
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    IMMUNE RESPONSE, TRANSFERASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.ZHANG,Z.CHEN,X.W.ZHANG,Z.J.CHEN                                     
REVDAT   3   05-AUG-15 4O67    1       HETSYN                                   
REVDAT   2   05-MAR-14 4O67    1       JRNL                                     
REVDAT   1   05-FEB-14 4O67    0                                                
JRNL        AUTH   X.ZHANG,J.WU,F.DU,H.XU,L.SUN,Z.CHEN,C.A.BRAUTIGAM,X.ZHANG,   
JRNL        AUTH 2 Z.J.CHEN                                                     
JRNL        TITL   THE CYTOSOLIC DNA SENSOR CGAS FORMS AN OLIGOMERIC COMPLEX    
JRNL        TITL 2 WITH DNA AND UNDERGOES SWITCH-LIKE CONFORMATIONAL CHANGES IN 
JRNL        TITL 3 THE ACTIVATION LOOP.                                         
JRNL        REF    CELL REP                      V.   6   421 2014              
JRNL        REFN                   ESSN 2211-1247                               
JRNL        PMID   24462292                                                     
JRNL        DOI    10.1016/J.CELREP.2014.01.003                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.44 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.44                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.87                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 26593                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1327                            
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 37.8739 -  5.0796    0.98     2961   161  0.1807 0.2387        
REMARK   3     2  5.0796 -  4.0333    1.00     2862   152  0.1569 0.2668        
REMARK   3     3  4.0333 -  3.5239    1.00     2866   145  0.1796 0.2259        
REMARK   3     4  3.5239 -  3.2019    1.00     2798   152  0.2065 0.2759        
REMARK   3     5  3.2019 -  2.9725    1.00     2816   149  0.2351 0.3216        
REMARK   3     6  2.9725 -  2.7973    1.00     2808   147  0.2364 0.3315        
REMARK   3     7  2.7973 -  2.6572    1.00     2751   154  0.2491 0.3489        
REMARK   3     8  2.6572 -  2.5416    0.99     2818   133  0.2780 0.3951        
REMARK   3     9  2.5416 -  2.4437    0.92     2586   134  0.3036 0.3941        
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)     : 0.380            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.970           
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      :  0.010           5915                                  
REMARK   3   ANGLE     :  1.299           7944                                  
REMARK   3   CHIRALITY :  0.056            867                                  
REMARK   3   PLANARITY :  0.006            984                                  
REMARK   3   DIHEDRAL  : 15.202           2282                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resid 161 through 199 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.7347  44.4271 147.6493              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2987 T22:   0.3294                                     
REMARK   3      T33:   0.3639 T12:   0.0308                                     
REMARK   3      T13:   0.0141 T23:   0.0484                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0399 L22:   0.0231                                     
REMARK   3      L33:   0.1316 L12:  -0.4262                                     
REMARK   3      L13:  -0.2761 L23:  -0.0254                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1018 S12:  -0.2134 S13:  -0.0114                       
REMARK   3      S21:   0.2247 S22:  -0.2300 S23:   0.3813                       
REMARK   3      S31:   0.1359 S32:  -0.0610 S33:  -0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resid 200 through 272 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  16.8997  28.1716 137.4425              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4133 T22:   0.2840                                     
REMARK   3      T33:   0.3966 T12:   0.0083                                     
REMARK   3      T13:   0.0280 T23:  -0.0679                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1930 L22:   0.6216                                     
REMARK   3      L33:   0.2740 L12:   0.2956                                     
REMARK   3      L13:   0.0893 L23:   0.1659                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0623 S12:  -0.0530 S13:  -0.1370                       
REMARK   3      S21:  -0.1141 S22:   0.1609 S23:  -0.0959                       
REMARK   3      S31:   0.0108 S32:   0.0582 S33:  -0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resid 273 through 405 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  12.1735  39.0332 141.2603              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1977 T22:   0.1777                                     
REMARK   3      T33:   0.1751 T12:   0.0005                                     
REMARK   3      T13:   0.0038 T23:  -0.0252                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3326 L22:   0.7883                                     
REMARK   3      L33:   0.3911 L12:   0.1164                                     
REMARK   3      L13:  -0.0842 L23:   0.4263                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0440 S12:  -0.0205 S13:   0.0001                       
REMARK   3      S21:  -0.0363 S22:   0.0354 S23:   0.0615                       
REMARK   3      S31:   0.0279 S32:   0.0469 S33:  -0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resid 406 through 521 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   8.9141  57.4441 133.0457              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1736 T22:   0.1511                                     
REMARK   3      T33:   0.1725 T12:  -0.0051                                     
REMARK   3      T13:  -0.0012 T23:   0.0083                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7777 L22:   0.3228                                     
REMARK   3      L33:   0.6896 L12:   0.2268                                     
REMARK   3      L13:   0.1237 L23:   0.0468                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0508 S12:   0.1247 S13:   0.1476                       
REMARK   3      S21:  -0.0437 S22:   0.0852 S23:   0.0071                       
REMARK   3      S31:  -0.0262 S32:   0.0402 S33:   0.0000                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'B' and (resid 161 through 199 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.3981 103.4912 147.5072              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2263 T22:   0.3079                                     
REMARK   3      T33:   0.3323 T12:   0.0440                                     
REMARK   3      T13:   0.1026 T23:   0.0619                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4544 L22:   0.0378                                     
REMARK   3      L33:   0.3509 L12:  -0.1686                                     
REMARK   3      L13:   0.2878 L23:   0.0293                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0430 S12:   0.0209 S13:   0.0430                       
REMARK   3      S21:   0.4422 S22:  -0.2220 S23:   0.1955                       
REMARK   3      S31:   0.1046 S32:   0.0113 S33:   0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'B' and (resid 200 through 253 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.3146  90.6318 138.2808              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4349 T22:   0.3734                                     
REMARK   3      T33:   0.3950 T12:   0.0895                                     
REMARK   3      T13:   0.0485 T23:  -0.0596                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4114 L22:   0.6441                                     
REMARK   3      L33:   0.1652 L12:   0.4764                                     
REMARK   3      L13:  -0.0349 L23:  -0.0845                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1625 S12:   0.1785 S13:  -0.1529                       
REMARK   3      S21:   0.1565 S22:  -0.0606 S23:  -0.0229                       
REMARK   3      S31:   0.0338 S32:   0.1637 S33:  -0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'B' and (resid 254 through 405 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  13.4671  94.7896 140.3980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2367 T22:   0.2293                                     
REMARK   3      T33:   0.2016 T12:  -0.0086                                     
REMARK   3      T13:   0.0403 T23:  -0.0049                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7088 L22:   1.2805                                     
REMARK   3      L33:  -0.2920 L12:   0.1091                                     
REMARK   3      L13:  -0.0663 L23:   0.3131                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0751 S12:   0.2294 S13:  -0.0027                       
REMARK   3      S21:   0.0604 S22:  -0.0246 S23:   0.1479                       
REMARK   3      S31:   0.0291 S32:   0.1757 S33:   0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'B' and (resid 406 through 521 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   9.0418 115.6060 131.8826              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2299 T22:   0.2253                                     
REMARK   3      T33:   0.1826 T12:  -0.0041                                     
REMARK   3      T13:  -0.0234 T23:   0.0714                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9797 L22:  -0.0242                                     
REMARK   3      L33:   0.7868 L12:  -0.2087                                     
REMARK   3      L13:  -0.3689 L23:   0.1827                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0504 S12:   0.1264 S13:  -0.0295                       
REMARK   3      S21:  -0.0706 S22:   0.0261 S23:  -0.0267                       
REMARK   3      S31:  -0.1037 S32:  -0.0292 S33:  -0.0000                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4O67 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB084092.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-APR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E DW                     
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26688                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.440                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.44                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.47                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2% ISOPROPANOL, 0.01 M MGSO4, 0.1 M      
REMARK 280  TRIS-HCL, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       23.91100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.01250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       59.27100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       62.01250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.91100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       59.27100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A   160                                                      
REMARK 465     GLY A   212                                                      
REMARK 465     SER A   213                                                      
REMARK 465     TYR A   214                                                      
REMARK 465     TYR A   215                                                      
REMARK 465     GLU A   216                                                      
REMARK 465     HIS A   217                                                      
REMARK 465     VAL A   218                                                      
REMARK 465     PRO A   257                                                      
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     GLN A   371                                                      
REMARK 465     PHE A   522                                                      
REMARK 465     MET B   160                                                      
REMARK 465     THR B   211                                                      
REMARK 465     GLY B   212                                                      
REMARK 465     SER B   213                                                      
REMARK 465     TYR B   214                                                      
REMARK 465     TYR B   215                                                      
REMARK 465     GLU B   216                                                      
REMARK 465     HIS B   217                                                      
REMARK 465     PRO B   257                                                      
REMARK 465     LYS B   365                                                      
REMARK 465     GLU B   366                                                      
REMARK 465     GLY B   367                                                      
REMARK 465     ASN B   368                                                      
REMARK 465     GLY B   369                                                      
REMARK 465     PHE B   370                                                      
REMARK 465     PHE B   522                                                      
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   NZ   LYS B   164     O    GLU B   515              2.06            
REMARK 500   O    ASN B   260     OG   SER B   263              2.18            
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    SER A 175       37.22    -97.38                                   
REMARK 500    SER A 243     -134.92     54.67                                   
REMARK 500    ARG A 255      -43.92   -134.33                                   
REMARK 500    LYS A 315      -33.95   -137.27                                   
REMARK 500    TRP A 343      -67.82   -106.55                                   
REMARK 500    PRO A 361       48.39    -75.03                                   
REMARK 500    ASN A 389       74.47   -114.97                                   
REMARK 500    PHE A 424       41.41   -102.76                                   
REMARK 500    ASN A 449       75.80   -117.27                                   
REMARK 500    PHE A 516       75.49     51.49                                   
REMARK 500    SER B 175       33.83    -97.91                                   
REMARK 500    SER B 243     -135.96     53.64                                   
REMARK 500    LYS B 254       46.97   -104.81                                   
REMARK 500    PRO B 261        2.16    -60.84                                   
REMARK 500    LYS B 315      -32.70   -138.37                                   
REMARK 500    TRP B 343      -70.20   -106.64                                   
REMARK 500    PRO B 361       46.22    -77.70                                   
REMARK 500    GLU B 372       34.52    -84.82                                   
REMARK 500    ASN B 389       76.08   -111.21                                   
REMARK 500    PHE B 424       48.51   -103.02                                   
REMARK 500    ASN B 449       75.39   -119.37                                   
REMARK 500    PHE B 516       71.75     49.79                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1102  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 390   NE2                                                    
REMARK 620 2 CYS B 397   SG  114.0                                              
REMARK 620 3 CYS B 396   SG  111.6 123.3                                        
REMARK 620 4 CYS B 404   SG   95.1 108.1  99.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 602  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 390   NE2                                                    
REMARK 620 2 CYS A 397   SG  108.5                                              
REMARK 620 3 CYS A 404   SG  101.8 107.1                                        
REMARK 620 4 CYS A 396   SG  116.2 124.3  94.9                                  
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 1SY A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1SY B 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1102                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4O68   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4O69   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4O6A   RELATED DB: PDB                                   
DBREF  4O67 A  161   522  UNP    Q8N884   CGAS_HUMAN     161    522             
DBREF  4O67 B  161   522  UNP    Q8N884   CGAS_HUMAN     161    522             
SEQADV 4O67 MET A  160  UNP  Q8N884              EXPRESSION TAG                 
SEQADV 4O67 MET B  160  UNP  Q8N884              EXPRESSION TAG                 
SEQRES   1 A  363  MET GLY ALA SER LYS LEU ARG ALA VAL LEU GLU LYS LEU          
SEQRES   2 A  363  LYS LEU SER ARG ASP ASP ILE SER THR ALA ALA GLY MET          
SEQRES   3 A  363  VAL LYS GLY VAL VAL ASP HIS LEU LEU LEU ARG LEU LYS          
SEQRES   4 A  363  CYS ASP SER ALA PHE ARG GLY VAL GLY LEU LEU ASN THR          
SEQRES   5 A  363  GLY SER TYR TYR GLU HIS VAL LYS ILE SER ALA PRO ASN          
SEQRES   6 A  363  GLU PHE ASP VAL MET PHE LYS LEU GLU VAL PRO ARG ILE          
SEQRES   7 A  363  GLN LEU GLU GLU TYR SER ASN THR ARG ALA TYR TYR PHE          
SEQRES   8 A  363  VAL LYS PHE LYS ARG ASN PRO LYS GLU ASN PRO LEU SER          
SEQRES   9 A  363  GLN PHE LEU GLU GLY GLU ILE LEU SER ALA SER LYS MET          
SEQRES  10 A  363  LEU SER LYS PHE ARG LYS ILE ILE LYS GLU GLU ILE ASN          
SEQRES  11 A  363  ASP ILE LYS ASP THR ASP VAL ILE MET LYS ARG LYS ARG          
SEQRES  12 A  363  GLY GLY SER PRO ALA VAL THR LEU LEU ILE SER GLU LYS          
SEQRES  13 A  363  ILE SER VAL ASP ILE THR LEU ALA LEU GLU SER LYS SER          
SEQRES  14 A  363  SER TRP PRO ALA SER THR GLN GLU GLY LEU ARG ILE GLN          
SEQRES  15 A  363  ASN TRP LEU SER ALA LYS VAL ARG LYS GLN LEU ARG LEU          
SEQRES  16 A  363  LYS PRO PHE TYR LEU VAL PRO LYS HIS ALA LYS GLU GLY          
SEQRES  17 A  363  ASN GLY PHE GLN GLU GLU THR TRP ARG LEU SER PHE SER          
SEQRES  18 A  363  HIS ILE GLU LYS GLU ILE LEU ASN ASN HIS GLY LYS SER          
SEQRES  19 A  363  LYS THR CYS CYS GLU ASN LYS GLU GLU LYS CYS CYS ARG          
SEQRES  20 A  363  LYS ASP CYS LEU LYS LEU MET LYS TYR LEU LEU GLU GLN          
SEQRES  21 A  363  LEU LYS GLU ARG PHE LYS ASP LYS LYS HIS LEU ASP LYS          
SEQRES  22 A  363  PHE SER SER TYR HIS VAL LYS THR ALA PHE PHE HIS VAL          
SEQRES  23 A  363  CYS THR GLN ASN PRO GLN ASP SER GLN TRP ASP ARG LYS          
SEQRES  24 A  363  ASP LEU GLY LEU CYS PHE ASP ASN CYS VAL THR TYR PHE          
SEQRES  25 A  363  LEU GLN CYS LEU ARG THR GLU LYS LEU GLU ASN TYR PHE          
SEQRES  26 A  363  ILE PRO GLU PHE ASN LEU PHE SER SER ASN LEU ILE ASP          
SEQRES  27 A  363  LYS ARG SER LYS GLU PHE LEU THR LYS GLN ILE GLU TYR          
SEQRES  28 A  363  GLU ARG ASN ASN GLU PHE PRO VAL PHE ASP GLU PHE              
SEQRES   1 B  363  MET GLY ALA SER LYS LEU ARG ALA VAL LEU GLU LYS LEU          
SEQRES   2 B  363  LYS LEU SER ARG ASP ASP ILE SER THR ALA ALA GLY MET          
SEQRES   3 B  363  VAL LYS GLY VAL VAL ASP HIS LEU LEU LEU ARG LEU LYS          
SEQRES   4 B  363  CYS ASP SER ALA PHE ARG GLY VAL GLY LEU LEU ASN THR          
SEQRES   5 B  363  GLY SER TYR TYR GLU HIS VAL LYS ILE SER ALA PRO ASN          
SEQRES   6 B  363  GLU PHE ASP VAL MET PHE LYS LEU GLU VAL PRO ARG ILE          
SEQRES   7 B  363  GLN LEU GLU GLU TYR SER ASN THR ARG ALA TYR TYR PHE          
SEQRES   8 B  363  VAL LYS PHE LYS ARG ASN PRO LYS GLU ASN PRO LEU SER          
SEQRES   9 B  363  GLN PHE LEU GLU GLY GLU ILE LEU SER ALA SER LYS MET          
SEQRES  10 B  363  LEU SER LYS PHE ARG LYS ILE ILE LYS GLU GLU ILE ASN          
SEQRES  11 B  363  ASP ILE LYS ASP THR ASP VAL ILE MET LYS ARG LYS ARG          
SEQRES  12 B  363  GLY GLY SER PRO ALA VAL THR LEU LEU ILE SER GLU LYS          
SEQRES  13 B  363  ILE SER VAL ASP ILE THR LEU ALA LEU GLU SER LYS SER          
SEQRES  14 B  363  SER TRP PRO ALA SER THR GLN GLU GLY LEU ARG ILE GLN          
SEQRES  15 B  363  ASN TRP LEU SER ALA LYS VAL ARG LYS GLN LEU ARG LEU          
SEQRES  16 B  363  LYS PRO PHE TYR LEU VAL PRO LYS HIS ALA LYS GLU GLY          
SEQRES  17 B  363  ASN GLY PHE GLN GLU GLU THR TRP ARG LEU SER PHE SER          
SEQRES  18 B  363  HIS ILE GLU LYS GLU ILE LEU ASN ASN HIS GLY LYS SER          
SEQRES  19 B  363  LYS THR CYS CYS GLU ASN LYS GLU GLU LYS CYS CYS ARG          
SEQRES  20 B  363  LYS ASP CYS LEU LYS LEU MET LYS TYR LEU LEU GLU GLN          
SEQRES  21 B  363  LEU LYS GLU ARG PHE LYS ASP LYS LYS HIS LEU ASP LYS          
SEQRES  22 B  363  PHE SER SER TYR HIS VAL LYS THR ALA PHE PHE HIS VAL          
SEQRES  23 B  363  CYS THR GLN ASN PRO GLN ASP SER GLN TRP ASP ARG LYS          
SEQRES  24 B  363  ASP LEU GLY LEU CYS PHE ASP ASN CYS VAL THR TYR PHE          
SEQRES  25 B  363  LEU GLN CYS LEU ARG THR GLU LYS LEU GLU ASN TYR PHE          
SEQRES  26 B  363  ILE PRO GLU PHE ASN LEU PHE SER SER ASN LEU ILE ASP          
SEQRES  27 B  363  LYS ARG SER LYS GLU PHE LEU THR LYS GLN ILE GLU TYR          
SEQRES  28 B  363  GLU ARG ASN ASN GLU PHE PRO VAL PHE ASP GLU PHE              
HET    1SY  A 601      45                                                       
HET     ZN  A 602       1                                                       
HET    1SY  B1101      45                                                       
HET     ZN  B1102       1                                                       
HETNAM     1SY CGAMP                                                            
HETNAM      ZN ZINC ION                                                         
HETSYN     1SY 2',3' CGAMP, C-GMP-AMP, C[G(2',5')PA(3',5')P]                    
FORMUL   3  1SY    2(C20 H24 N10 O13 P2)                                        
FORMUL   4   ZN    2(ZN 2+)                                                     
FORMUL   7  HOH   *89(H2 O)                                                     
HELIX    1   1 GLY A  161  SER A  175  1                                  15    
HELIX    2   2 SER A  175  ASP A  200  1                                  26    
HELIX    3   3 LEU A  262  GLN A  264  5                                   3    
HELIX    4   4 SER A  272  ILE A  291  1                                  20    
HELIX    5   5 PRO A  331  GLN A  335  5                                   5    
HELIX    6   6 SER A  345  ARG A  353  1                                   9    
HELIX    7   7 PHE A  379  ASN A  389  1                                  11    
HELIX    8   8 CYS A  405  PHE A  424  1                                  20    
HELIX    9   9 SER A  434  ASN A  449  1                                  16    
HELIX   10  10 GLN A  451  LYS A  458  5                                   8    
HELIX   11  11 ASP A  459  GLU A  478  1                                  20    
HELIX   12  12 ASP A  497  ASN A  514  1                                  18    
HELIX   13  13 PHE A  516  ASP A  520  5                                   5    
HELIX   14  14 ALA B  162  SER B  175  1                                  14    
HELIX   15  15 SER B  175  ASP B  200  1                                  26    
HELIX   16  16 ASN B  260  GLN B  264  5                                   5    
HELIX   17  17 SER B  272  ILE B  291  1                                  20    
HELIX   18  18 PRO B  331  GLN B  335  5                                   5    
HELIX   19  19 SER B  345  ARG B  353  1                                   9    
HELIX   20  20 PHE B  379  ASN B  389  1                                  11    
HELIX   21  21 CYS B  405  PHE B  424  1                                  20    
HELIX   22  22 SER B  434  ASN B  449  1                                  16    
HELIX   23  23 GLN B  451  LYS B  458  5                                   8    
HELIX   24  24 ASP B  459  GLU B  478  1                                  20    
HELIX   25  25 ASP B  497  ASN B  514  1                                  18    
HELIX   26  26 PHE B  516  ASP B  520  5                                   5    
SHEET    1   A 7 VAL A 206  LEU A 208  0                                        
SHEET    2   A 7 GLU A 225  GLU A 233 -1  O  LYS A 231   N  GLY A 207           
SHEET    3   A 7 ILE A 316  SER A 326  1  O  THR A 321   N  PHE A 230           
SHEET    4   A 7 PHE A 357  VAL A 360 -1  O  LEU A 359   N  LEU A 324           
SHEET    5   A 7 TRP A 375  SER A 378 -1  O  ARG A 376   N  VAL A 360           
SHEET    6   A 7 TYR A 248  PHE A 253 -1  N  TYR A 249   O  TRP A 375           
SHEET    7   A 7 ILE A 237  GLU A 241 -1  N  GLN A 238   O  LYS A 252           
SHEET    1   B 5 ILE A 220  ALA A 222  0                                        
SHEET    2   B 5 GLU A 225  GLU A 233 -1  O  GLU A 225   N  ALA A 222           
SHEET    3   B 5 ILE A 316  SER A 326  1  O  THR A 321   N  PHE A 230           
SHEET    4   B 5 ALA A 307  ILE A 312 -1  N  ILE A 312   O  ILE A 316           
SHEET    5   B 5 VAL A 296  LYS A 299 -1  N  ILE A 297   O  LEU A 311           
SHEET    1   C 2 LEU A 266  GLU A 267  0                                        
SHEET    2   C 2 ILE A 270  LEU A 271 -1  O  ILE A 270   N  GLU A 267           
SHEET    1   D 7 ILE B 237  GLU B 241  0                                        
SHEET    2   D 7 TYR B 248  PHE B 253 -1  O  LYS B 252   N  GLN B 238           
SHEET    3   D 7 TRP B 375  SER B 378 -1  O  TRP B 375   N  TYR B 249           
SHEET    4   D 7 PHE B 357  VAL B 360 -1  N  VAL B 360   O  ARG B 376           
SHEET    5   D 7 ILE B 316  SER B 326 -1  N  LEU B 324   O  LEU B 359           
SHEET    6   D 7 GLU B 225  GLU B 233  1  N  PHE B 226   O  SER B 317           
SHEET    7   D 7 VAL B 206  LEU B 208 -1  N  GLY B 207   O  LYS B 231           
SHEET    1   E 3 VAL B 206  LEU B 208  0                                        
SHEET    2   E 3 GLU B 225  GLU B 233 -1  O  LYS B 231   N  GLY B 207           
SHEET    3   E 3 ILE B 220  ALA B 222 -1  N  ALA B 222   O  GLU B 225           
SHEET    1   F 4 PHE B 357  VAL B 360  0                                        
SHEET    2   F 4 ILE B 316  SER B 326 -1  N  LEU B 324   O  LEU B 359           
SHEET    3   F 4 ALA B 307  ILE B 312 -1  N  ILE B 312   O  ILE B 316           
SHEET    4   F 4 VAL B 296  LYS B 299 -1  N  ILE B 297   O  LEU B 311           
SHEET    1   G 4 ILE B 237  GLU B 241  0                                        
SHEET    2   G 4 TYR B 248  PHE B 253 -1  O  LYS B 252   N  GLN B 238           
SHEET    3   G 4 ILE B 270  LEU B 271 -1  O  LEU B 271   N  VAL B 251           
SHEET    4   G 4 LEU B 266  GLU B 267 -1  N  GLU B 267   O  ILE B 270           
LINK         NE2 HIS B 390                ZN    ZN B1102     1555   1555  2.05  
LINK         NE2 HIS A 390                ZN    ZN A 602     1555   1555  2.06  
LINK         SG  CYS B 397                ZN    ZN B1102     1555   1555  2.17  
LINK         SG  CYS A 397                ZN    ZN A 602     1555   1555  2.25  
LINK         SG  CYS A 404                ZN    ZN A 602     1555   1555  2.29  
LINK         SG  CYS A 396                ZN    ZN A 602     1555   1555  2.35  
LINK         SG  CYS B 396                ZN    ZN B1102     1555   1555  2.41  
LINK         SG  CYS B 404                ZN    ZN B1102     1555   1555  2.44  
SITE     1 AC1 11 ASP A 227  LYS A 301  ARG A 302  SER A 305                    
SITE     2 AC1 11 PRO A 306  ASP A 319  LYS A 362  ARG A 376                    
SITE     3 AC1 11 SER A 434  TYR A 436  HOH A 708                               
SITE     1 AC2  4 HIS A 390  CYS A 396  CYS A 397  CYS A 404                    
SITE     1 AC3 12 ASP B 227  LYS B 301  ARG B 302  GLY B 303                    
SITE     2 AC3 12 SER B 305  ASP B 319  LYS B 362  ARG B 376                    
SITE     3 AC3 12 SER B 434  TYR B 436  LEU B 490  HOH B1220                    
SITE     1 AC4  4 HIS B 390  CYS B 396  CYS B 397  CYS B 404                    
CRYST1   47.822  118.542  124.025  90.00  90.00  90.00 P 21 21 21    8          
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      0.020911  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008436  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008063        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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