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Database: PDB
Entry: 5VDP
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Original site: 5VDP 
HEADER    TRANSFERASE                             03-APR-17   5VDP              
TITLE     HUMAN CYCLIC GMP-AMP SYNTHASE (CGAS) IN COMPLEX WITH 2',3'-CGAMP      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIC GMP-AMP SYNTHASE;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 161-521;                                      
COMPND   5 SYNONYM: H-CGAS,2'3'-CGAMP SYNTHASE,MAB-21 DOMAIN-CONTAINING PROTEIN 
COMPND   6 1;                                                                   
COMPND   7 EC: 2.7.7.86;                                                        
COMPND   8 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: MB21D1, C6ORF150;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSFERASE, STING, CGAMP                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.J.BYRNES,J.D.HALL                                                   
REVDAT   3   06-DEC-17 5VDP    1       JRNL                                     
REVDAT   2   04-OCT-17 5VDP    1       JRNL                                     
REVDAT   1   27-SEP-17 5VDP    0                                                
JRNL        AUTH   J.HALL,E.C.RALPH,S.SHANKER,H.WANG,L.J.BYRNES,R.HORST,J.WONG, 
JRNL        AUTH 2 A.BRAULT,D.DUMLAO,J.F.SMITH,L.A.DAKIN,D.C.SCHMITT,           
JRNL        AUTH 3 J.TRUJILLO,F.VINCENT,M.GRIFFOR,A.E.AULABAUGH                 
JRNL        TITL   THE CATALYTIC MECHANISM OF CYCLIC GMP-AMP SYNTHASE (CGAS)    
JRNL        TITL 2 AND IMPLICATIONS FOR INNATE IMMUNITY AND INHIBITION.         
JRNL        REF    PROTEIN SCI.                  V.  26  2367 2017              
JRNL        REFN                   ESSN 1469-896X                               
JRNL        PMID   28940468                                                     
JRNL        DOI    10.1002/PRO.3304                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX DEV_1999                                      
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.45                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 35983                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.970                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1787                            
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 32.4494 -  5.3998    0.98     2806   153  0.1586 0.1849        
REMARK   3     2  5.3998 -  4.2891    0.98     2659   154  0.1462 0.1878        
REMARK   3     3  4.2891 -  3.7479    0.98     2728   129  0.1644 0.2129        
REMARK   3     4  3.7479 -  3.4056    0.98     2643   162  0.1902 0.2389        
REMARK   3     5  3.4056 -  3.1617    0.99     2684   132  0.2249 0.2673        
REMARK   3     6  3.1617 -  2.9754    1.00     2700   137  0.2326 0.3036        
REMARK   3     7  2.9754 -  2.8265    0.99     2706   138  0.2460 0.3341        
REMARK   3     8  2.8265 -  2.7035    1.00     2681   140  0.2406 0.2550        
REMARK   3     9  2.7035 -  2.5995    1.00     2662   140  0.2355 0.3290        
REMARK   3    10  2.5995 -  2.5098    0.99     2669   135  0.2527 0.3249        
REMARK   3    11  2.5098 -  2.4314    1.00     2708   136  0.2570 0.3091        
REMARK   3    12  2.4314 -  2.3619    1.00     2689   134  0.2701 0.3413        
REMARK   3    13  2.3619 -  2.2997    0.70     1861    97  0.2936 0.3409        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.020           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.82                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.10                          
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      :  0.007           5995                                  
REMARK   3   ANGLE     :  1.004           8098                                  
REMARK   3   CHIRALITY :  0.045            888                                  
REMARK   3   PLANARITY :  0.005           1014                                  
REMARK   3   DIHEDRAL  : 14.696           2210                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 11                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 160 THROUGH 199 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.2338  47.5828  58.7262              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4354 T22:   0.4637                                     
REMARK   3      T33:   0.4217 T12:  -0.0357                                     
REMARK   3      T13:   0.0822 T23:  -0.1421                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9913 L22:   2.0900                                     
REMARK   3      L33:   0.2715 L12:   0.7803                                     
REMARK   3      L13:   0.0820 L23:  -0.6634                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4652 S12:   0.1496 S13:   0.8743                       
REMARK   3      S21:   0.1022 S22:  -0.2625 S23:   0.4823                       
REMARK   3      S31:  -0.1275 S32:  -0.1353 S33:  -0.1710                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 200 THROUGH 233 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.1437  39.8184  61.6551              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4333 T22:   0.6621                                     
REMARK   3      T33:   0.6470 T12:  -0.0691                                     
REMARK   3      T13:   0.0238 T23:  -0.1789                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6482 L22:   2.7780                                     
REMARK   3      L33:   6.8602 L12:   2.3892                                     
REMARK   3      L13:  -5.0794 L23:  -3.1950                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5512 S12:  -0.2135 S13:   0.5620                       
REMARK   3      S21:   0.1361 S22:  -0.6318 S23:   0.3661                       
REMARK   3      S31:  -0.1113 S32:   0.4596 S33:  -0.0089                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 234 THROUGH 272 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -19.0568  19.3238  67.0909              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5041 T22:   0.7117                                     
REMARK   3      T33:   0.6897 T12:  -0.1522                                     
REMARK   3      T13:   0.1935 T23:  -0.0858                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2018 L22:   4.7874                                     
REMARK   3      L33:   3.6918 L12:  -0.3353                                     
REMARK   3      L13:   3.4053 L23:  -0.9268                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3652 S12:  -0.7712 S13:  -0.7270                       
REMARK   3      S21:   0.6792 S22:   0.2410 S23:   1.2135                       
REMARK   3      S31:   0.2980 S32:  -0.9472 S33:   0.1980                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 273 THROUGH 315 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -16.6338  37.6376  51.5194              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3525 T22:   0.4013                                     
REMARK   3      T33:   0.5888 T12:   0.0734                                     
REMARK   3      T13:  -0.0785 T23:  -0.1174                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1903 L22:   7.2897                                     
REMARK   3      L33:   4.1335 L12:   2.5817                                     
REMARK   3      L13:  -1.1084 L23:  -2.8619                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1609 S12:   0.3581 S13:   0.3757                       
REMARK   3      S21:  -0.5305 S22:  -0.0604 S23:   1.2432                       
REMARK   3      S31:  -0.1573 S32:  -0.3552 S33:  -0.0233                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 316 THROUGH 521 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   6.8478  29.7127  62.0402              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3019 T22:   0.2910                                     
REMARK   3      T33:   0.2336 T12:  -0.0180                                     
REMARK   3      T13:  -0.0047 T23:  -0.0132                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2784 L22:   1.4533                                     
REMARK   3      L33:   1.6932 L12:   0.0900                                     
REMARK   3      L13:  -0.3771 L23:   0.3106                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0634 S12:  -0.0737 S13:  -0.0184                       
REMARK   3      S21:   0.0977 S22:  -0.1337 S23:   0.1004                       
REMARK   3      S31:   0.0788 S32:   0.0028 S33:   0.0892                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 160 THROUGH 199 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.0271  26.1921 106.2494              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4442 T22:   0.3349                                     
REMARK   3      T33:   0.1850 T12:  -0.0060                                     
REMARK   3      T13:  -0.0283 T23:  -0.0212                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3747 L22:   2.4587                                     
REMARK   3      L33:   0.5483 L12:   0.6020                                     
REMARK   3      L13:  -0.0748 L23:   0.4522                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2805 S12:   0.2916 S13:  -0.9830                       
REMARK   3      S21:   0.0507 S22:  -0.2027 S23:   0.1332                       
REMARK   3      S31:   0.3237 S32:  -0.0255 S33:  -0.0623                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 200 THROUGH 224 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.9130  32.8784 103.4499              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4408 T22:   0.4200                                     
REMARK   3      T33:   0.4587 T12:   0.0038                                     
REMARK   3      T13:  -0.0257 T23:  -0.0906                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4844 L22:   6.7235                                     
REMARK   3      L33:   6.2573 L12:  -5.9199                                     
REMARK   3      L13:   4.4730 L23:  -3.9143                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2658 S12:   0.6731 S13:  -0.0994                       
REMARK   3      S21:   0.0883 S22:  -0.4636 S23:   0.1359                       
REMARK   3      S31:  -0.0564 S32:   0.6481 S33:   0.1157                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 225 THROUGH 248 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -11.9704  48.8950  99.4817              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3339 T22:   0.3494                                     
REMARK   3      T33:   0.3272 T12:   0.0586                                     
REMARK   3      T13:  -0.0591 T23:  -0.0386                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3574 L22:   4.3712                                     
REMARK   3      L33:   1.6458 L12:   1.8953                                     
REMARK   3      L13:  -0.3197 L23:   0.0737                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0103 S12:   0.5919 S13:   0.2144                       
REMARK   3      S21:  -0.6157 S22:  -0.1963 S23:   0.5557                       
REMARK   3      S31:  -0.0626 S32:  -0.1310 S33:   0.1615                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 249 THROUGH 272 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -24.4362  52.9594  98.7190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5890 T22:   0.5779                                     
REMARK   3      T33:   0.8325 T12:   0.0778                                     
REMARK   3      T13:  -0.2280 T23:   0.0656                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3911 L22:   4.1510                                     
REMARK   3      L33:   6.2763 L12:  -0.7287                                     
REMARK   3      L13:  -2.5382 L23:  -2.7658                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2698 S12:   0.7223 S13:   0.6909                       
REMARK   3      S21:  -0.8908 S22:   0.4779 S23:   1.8788                       
REMARK   3      S31:  -0.3335 S32:  -1.4166 S33:  -0.0280                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 273 THROUGH 405 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.4667  41.6437 100.9795              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2914 T22:   0.2413                                     
REMARK   3      T33:   0.2239 T12:  -0.0088                                     
REMARK   3      T13:  -0.0764 T23:  -0.0297                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8789 L22:   1.7822                                     
REMARK   3      L33:   2.1323 L12:   0.2011                                     
REMARK   3      L13:  -0.8974 L23:   0.2281                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0852 S12:  -0.0095 S13:   0.0592                       
REMARK   3      S21:  -0.0932 S22:  -0.0971 S23:   0.2189                       
REMARK   3      S31:  -0.0735 S32:   0.0196 S33:  -0.0002                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 406 THROUGH 521 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  12.2156  44.4098 108.6867              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2231 T22:   0.1991                                     
REMARK   3      T33:   0.1709 T12:  -0.0298                                     
REMARK   3      T13:  -0.0063 T23:  -0.0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4784 L22:   3.2128                                     
REMARK   3      L33:   3.1636 L12:  -0.0989                                     
REMARK   3      L13:   0.6634 L23:   0.0888                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0306 S12:  -0.0515 S13:  -0.0217                       
REMARK   3      S21:  -0.0189 S22:  -0.0693 S23:   0.0368                       
REMARK   3      S31:  -0.0810 S32:   0.1271 S33:   0.0924                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND SEGID                           
REMARK   3     SELECTION          : CHAIN B AND SEGID                           
REMARK   3     ATOM PAIRS NUMBER  : 3372                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5VDP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000227212.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JUL-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 173                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : AIMLESS                            
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37195                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.446                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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: REFMAC                                                
REMARK 200 STARTING MODEL: 4O67                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.19                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18-20% PEG 3350, 0.2 M AMMONIUM          
REMARK 280  CITRATE PH 7, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      107.94300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.36650            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      107.94300            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.36650            
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                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ILE A   220                                                      
REMARK 465     SER A   221                                                      
REMARK 465     PHE A   522                                                      
REMARK 465     ILE B   220                                                      
REMARK 465     SER B   221                                                      
REMARK 465     PHE B   522                                                      
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     LYS A 173    CG   CD   CE   NZ                                   
REMARK 470     ASP A 177    CG   OD1  OD2                                       
REMARK 470     ASP A 178    CG   OD1  OD2                                       
REMARK 470     ARG A 204    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 211    OG1  CG2                                            
REMARK 470     TYR A 214    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A 219    CG   CD   CE   NZ                                   
REMARK 470     LYS A 254    CG   CD   CE   NZ                                   
REMARK 470     LYS A 258    CG   CD   CE   NZ                                   
REMARK 470     GLU A 259    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 287    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 289    CG   OD1  ND2                                       
REMARK 470     LYS A 292    CG   CD   CE   NZ                                   
REMARK 470     ASP A 293    CG   OD1  OD2                                       
REMARK 470     THR A 294    OG1  CG2                                            
REMARK 470     ASP A 295    CG   OD1  OD2                                       
REMARK 470     ARG A 302    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 314    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 315    CG   CD   CE   NZ                                   
REMARK 470     ARG A 339    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 400    CG   CD   CE   NZ                                   
REMARK 470     GLU A 401    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 425    CG   CD   CE   NZ                                   
REMARK 470     LYS A 428    CG   CD   CE   NZ                                   
REMARK 470     GLU A 521    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 173    CG   CD   CE   NZ                                   
REMARK 470     THR B 211    OG1  CG2                                            
REMARK 470     TYR B 214    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU B 216    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 219    CG   CD   CE   NZ                                   
REMARK 470     LYS B 254    CG   CD   CE   NZ                                   
REMARK 470     ARG B 255    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B 256    CG   OD1  ND2                                       
REMARK 470     LYS B 258    CG   CD   CE   NZ                                   
REMARK 470     GLU B 259    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 262    CG   CD1  CD2                                       
REMARK 470     LYS B 292    CG   CD   CE   NZ                                   
REMARK 470     ASP B 293    CG   OD1  OD2                                       
REMARK 470     ASP B 295    CG   OD1  OD2                                       
REMARK 470     ARG B 302    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 351    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 365    CG   CD   CE   NZ                                   
REMARK 470     LYS B 384    CG   CD   CE   NZ                                   
REMARK 470     LYS B 400    CG   CD   CE   NZ                                   
REMARK 470     GLU B 401    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 425    CG   CD   CE   NZ                                   
REMARK 470     ASP B 426    CG   OD1  OD2                                       
REMARK 470     LYS B 428    CG   CD   CE   NZ                                   
REMARK 470     GLU B 521    CG   CD   OE1  OE2                                  
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU B  418   CD                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B   701     O    HOH B   710              1.79            
REMARK 500   NH1  ARG B   166     O    HOH B   701              1.97            
REMARK 500   O2   SO4 B   602     O    HOH B   702              2.00            
REMARK 500   OE1  GLU B   398     O    HOH B   703              2.03            
REMARK 500   O3   SO4 B   602     O    HOH B   704              2.12            
REMARK 500   OG   SER B   378     O    HOH B   705              2.13            
REMARK 500   O44  1SY B   604     O    HOH B   706              2.14            
REMARK 500   OD2  ASP B   459     O    HOH B   707              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A 223       42.97    -96.50                                   
REMARK 500    SER A 243       40.78     39.27                                   
REMARK 500    ARG A 246      -23.46     77.01                                   
REMARK 500    ASP A 293      -12.01     75.11                                   
REMARK 500    ARG A 300      151.23    -49.45                                   
REMARK 500    GLU A 314       18.32     59.01                                   
REMARK 500    LYS A 315      -36.89   -132.17                                   
REMARK 500    TRP A 343      -66.42   -108.21                                   
REMARK 500    SER A 345      153.84    101.37                                   
REMARK 500    ASN A 449       76.82   -115.67                                   
REMARK 500    ASN B 210       63.51     39.60                                   
REMARK 500    PRO B 223       40.10    -95.48                                   
REMARK 500    PRO B 235      170.33    -58.03                                   
REMARK 500    ARG B 246      -24.38     76.33                                   
REMARK 500    ASP B 293      -10.86     75.48                                   
REMARK 500    GLU B 314       16.82     59.96                                   
REMARK 500    LYS B 315      -37.50   -133.89                                   
REMARK 500    TRP B 343      -67.34   -108.46                                   
REMARK 500    SER B 345      148.72    108.70                                   
REMARK 500    ASN B 368       -1.05     77.57                                   
REMARK 500    ASN B 449       75.52   -117.13                                   
REMARK 500    ASP B 520       66.71     60.71                                   
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 A 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 390   NE2                                                    
REMARK 620 2 CYS A 396   SG  112.4                                              
REMARK 620 3 CYS A 397   SG  103.4 129.3                                        
REMARK 620 4 CYS A 404   SG   96.7 100.2 110.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 390   NE2                                                    
REMARK 620 2 CYS B 396   SG  112.3                                              
REMARK 620 3 CYS B 397   SG  104.8 131.4                                        
REMARK 620 4 CYS B 404   SG   98.8  95.3 109.0                                  
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 SO4 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1SY A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1SY B 604                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5VDO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VDQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VDR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VDS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VDT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VDU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VDV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VDW   RELATED DB: PDB                                   
DBREF  5VDP A  161   522  UNP    Q8N884   CGAS_HUMAN     161    522             
DBREF  5VDP B  161   522  UNP    Q8N884   CGAS_HUMAN     161    522             
SEQADV 5VDP MET A  160  UNP  Q8N884              EXPRESSION TAG                 
SEQADV 5VDP 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     ZN  A 601       1                                                       
HET    SO4  A 602       5                                                       
HET    SO4  A 603       5                                                       
HET    SO4  A 604       5                                                       
HET    1SY  A 605      66                                                       
HET     ZN  B 601       1                                                       
HET    SO4  B 602       5                                                       
HET    SO4  B 603       5                                                       
HET    1SY  B 604      66                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM     1SY CGAMP                                                            
HETSYN     1SY 2',3' CGAMP, C-GMP-AMP, C[G(2',5')PA(3',5')P]                    
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  SO4    5(O4 S 2-)                                                   
FORMUL   7  1SY    2(C20 H24 N10 O13 P2)                                        
FORMUL  12  HOH   *129(H2 O)                                                    
HELIX    1 AA1 GLY A  161  LYS A  173  1                                  13    
HELIX    2 AA2 SER A  175  LYS A  198  1                                  24    
HELIX    3 AA3 CYS A  199  ARG A  204  5                                   6    
HELIX    4 AA4 ASN A  260  GLN A  264  5                                   5    
HELIX    5 AA5 SER A  272  ILE A  288  1                                  17    
HELIX    6 AA6 PRO A  331  GLN A  335  5                                   5    
HELIX    7 AA7 SER A  345  LYS A  355  1                                  11    
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 SER A  434  ASN A  449  1                                  16    
HELIX   12 AB3 GLN A  451  LYS A  458  5                                   8    
HELIX   13 AB4 ASP A  459  GLU A  478  1                                  20    
HELIX   14 AB5 ASP A  497  ASN A  513  1                                  17    
HELIX   15 AB6 ASN A  514  GLU A  515  5                                   2    
HELIX   16 AB7 PHE A  516  ASP A  520  5                                   5    
HELIX   17 AB8 GLY B  161  LYS B  173  1                                  13    
HELIX   18 AB9 SER B  175  LYS B  198  1                                  24    
HELIX   19 AC1 CYS B  199  ARG B  204  5                                   6    
HELIX   20 AC2 LEU B  262  GLN B  264  5                                   3    
HELIX   21 AC3 SER B  272  ILE B  288  1                                  17    
HELIX   22 AC4 PRO B  331  GLN B  335  5                                   5    
HELIX   23 AC5 SER B  345  ARG B  353  1                                   9    
HELIX   24 AC6 PHE B  379  ASN B  389  1                                  11    
HELIX   25 AC7 ASN B  399  LYS B  403  5                                   5    
HELIX   26 AC8 CYS B  405  PHE B  424  1                                  20    
HELIX   27 AC9 SER B  434  ASN B  449  1                                  16    
HELIX   28 AD1 GLN B  451  LYS B  458  5                                   8    
HELIX   29 AD2 ASP B  459  GLU B  478  1                                  20    
HELIX   30 AD3 ASP B  497  ASN B  514  1                                  18    
HELIX   31 AD4 GLU B  515  ASP B  520  5                                   6    
SHEET    1 AA1 7 VAL A 206  LEU A 209  0                                        
SHEET    2 AA1 7 GLU A 225  GLU A 233 -1  O  MET A 229   N  LEU A 209           
SHEET    3 AA1 7 ILE A 316  SER A 326  1  O  SER A 317   N  PHE A 226           
SHEET    4 AA1 7 PHE A 357  VAL A 360 -1  O  LEU A 359   N  LEU A 324           
SHEET    5 AA1 7 TRP A 375  SER A 378 -1  O  ARG A 376   N  VAL A 360           
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  GLN A 238   O  LYS A 252           
SHEET    1 AA2 5 VAL A 206  LEU A 209  0                                        
SHEET    2 AA2 5 GLU A 225  GLU A 233 -1  O  MET A 229   N  LEU A 209           
SHEET    3 AA2 5 ILE A 316  SER A 326  1  O  SER A 317   N  PHE A 226           
SHEET    4 AA2 5 ALA A 307  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           
SHEET    1 AA4 2 ALA A 364  GLU A 366  0                                        
SHEET    2 AA4 2 GLY A 369  GLN A 371 -1  O  GLN A 371   N  ALA A 364           
SHEET    1 AA5 8 VAL B 206  LEU B 209  0                                        
SHEET    2 AA5 8 GLU B 225  GLU B 233 -1  O  MET B 229   N  LEU B 209           
SHEET    3 AA5 8 ILE B 316  SER B 326  1  O  ASP B 319   N  VAL B 228           
SHEET    4 AA5 8 PHE B 357  VAL B 360 -1  O  LEU B 359   N  LEU B 324           
SHEET    5 AA5 8 TRP B 375  SER B 378 -1  O  ARG B 376   N  VAL B 360           
SHEET    6 AA5 8 TYR B 248  PHE B 253 -1  N  TYR B 249   O  TRP B 375           
SHEET    7 AA5 8 ILE B 270  LEU B 271 -1  O  LEU B 271   N  VAL B 251           
SHEET    8 AA5 8 LEU B 266  GLU B 267 -1  N  GLU B 267   O  ILE B 270           
SHEET    1 AA6 7 ILE B 237  GLU B 241  0                                        
SHEET    2 AA6 7 TYR B 248  PHE B 253 -1  O  LYS B 252   N  GLN B 238           
SHEET    3 AA6 7 TRP B 375  SER B 378 -1  O  TRP B 375   N  TYR B 249           
SHEET    4 AA6 7 PHE B 357  VAL B 360 -1  N  VAL B 360   O  ARG B 376           
SHEET    5 AA6 7 ILE B 316  SER B 326 -1  N  LEU B 324   O  LEU B 359           
SHEET    6 AA6 7 ALA B 307  ILE B 312 -1  N  ILE B 312   O  ILE B 316           
SHEET    7 AA6 7 VAL B 296  MET B 298 -1  N  ILE B 297   O  LEU B 311           
SHEET    1 AA7 2 ALA B 364  LYS B 365  0                                        
SHEET    2 AA7 2 PHE B 370  GLN B 371 -1  O  GLN B 371   N  ALA B 364           
LINK         NZ  LYS A 285                 O4  SO4 A 604     1555   1555  1.30  
LINK         NE2 HIS A 390                ZN    ZN A 601     1555   1555  2.16  
LINK         SG  CYS A 396                ZN    ZN A 601     1555   1555  2.33  
LINK         SG  CYS A 397                ZN    ZN A 601     1555   1555  2.15  
LINK         SG  CYS A 404                ZN    ZN A 601     1555   1555  2.40  
LINK         NE2 HIS B 390                ZN    ZN B 601     1555   1555  2.15  
LINK         SG  CYS B 396                ZN    ZN B 601     1555   1555  2.37  
LINK         SG  CYS B 397                ZN    ZN B 601     1555   1555  2.16  
LINK         SG  CYS B 404                ZN    ZN B 601     1555   1555  2.55  
SITE     1 AC1  4 HIS A 390  CYS A 396  CYS A 397  CYS A 404                    
SITE     1 AC2  6 SER A 175  ARG A 176  ASP A 177  ASN A 489                    
SITE     2 AC2  6 SER A 492  HOH A 738                                          
SITE     1 AC3  2 GLN A 335  ARG A 353                                          
SITE     1 AC4  4 ARG A 281  LYS A 285  ARG A 300  LYS A 301                    
SITE     1 AC5 15 ASP A 227  GLY A 303  GLY A 304  SER A 305                    
SITE     2 AC5 15 PRO A 306  ASP A 319  LYS A 362  ARG A 376                    
SITE     3 AC5 15 SER A 380  SER A 434  TYR A 436  LEU A 490                    
SITE     4 AC5 15 HOH A 719  HOH A 728  HOH A 744                               
SITE     1 AC6  4 HIS B 390  CYS B 396  CYS B 397  CYS B 404                    
SITE     1 AC7  7 ARG B 281  LYS B 285  ARG B 300  LYS B 301                    
SITE     2 AC7  7 HOH B 702  HOH B 704  HOH B 739                               
SITE     1 AC8  3 SER B 175  ARG B 176  ASN B 489                               
SITE     1 AC9 16 ASP B 227  GLY B 304  SER B 305  PRO B 306                    
SITE     2 AC9 16 ASP B 319  LYS B 362  ARG B 376  SER B 380                    
SITE     3 AC9 16 SER B 434  TYR B 436  LEU B 490  HOH B 705                    
SITE     4 AC9 16 HOH B 706  HOH B 714  HOH B 719  HOH B 737                    
CRYST1  215.886   46.733   88.165  90.00 110.45  90.00 C 1 2 1       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      0.004632  0.000000  0.001728        0.00000                         
SCALE2      0.000000  0.021398  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012106        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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