GenomeNet

Database: PDB
Entry: 5VDS
LinkDB: 5VDS
Original site: 5VDS 
HEADER    TRANSFERASE                             03-APR-17   5VDS              
TITLE     HUMAN CYCLIC GMP-AMP SYNTHASE (CGAS) IN COMPLEX WITH 3',3'-CDUMP      
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   4   26-FEB-20 5VDS    1       REMARK                                   
REVDAT   3   06-DEC-17 5VDS    1       JRNL                                     
REVDAT   2   04-OCT-17 5VDS    1       JRNL                                     
REVDAT   1   27-SEP-17 5VDS    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.    2.77 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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.77                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 58.17                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 22373                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1132                            
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 58.1778 -  5.5310    1.00     2756   149  0.1907 0.1926        
REMARK   3     2  5.5310 -  4.3906    1.00     2663   149  0.1721 0.1908        
REMARK   3     3  4.3906 -  3.8357    1.00     2667   144  0.1824 0.2606        
REMARK   3     4  3.8357 -  3.4851    1.00     2623   147  0.2029 0.2454        
REMARK   3     5  3.4851 -  3.2353    1.00     2631   136  0.2268 0.2913        
REMARK   3     6  3.2353 -  3.0446    1.00     2645   129  0.2323 0.3003        
REMARK   3     7  3.0446 -  2.8921    1.00     2631   140  0.2580 0.3182        
REMARK   3     8  2.8921 -  2.7662    1.00     2625   138  0.2797 0.3135        
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)     : 0.340            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.480           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.14                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.54                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           5530                                  
REMARK   3   ANGLE     :  0.536           7712                                  
REMARK   3   CHIRALITY :  0.028            861                                  
REMARK   3   PLANARITY :  0.002            953                                  
REMARK   3   DIHEDRAL  : 11.832           2128                                  
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): -29.1152  20.3154  22.6281              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4352 T22:   0.5069                                     
REMARK   3      T33:   0.9828 T12:  -0.1321                                     
REMARK   3      T13:  -0.0506 T23:   0.0320                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1984 L22:   0.0413                                     
REMARK   3      L33:   0.3418 L12:   0.2750                                     
REMARK   3      L13:  -1.0113 L23:   0.0316                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0621 S12:  -0.3032 S13:   1.6646                       
REMARK   3      S21:   0.1317 S22:  -0.0739 S23:  -0.3818                       
REMARK   3      S31:  -0.4201 S32:   0.5145 S33:  -0.1422                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 200 THROUGH 224 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -21.5316  13.5365  19.8851              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5247 T22:   1.2414                                     
REMARK   3      T33:   1.1481 T12:   0.0457                                     
REMARK   3      T13:  -0.0965 T23:   0.2168                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1385 L22:   0.1180                                     
REMARK   3      L33:   4.5071 L12:  -0.5903                                     
REMARK   3      L13:  -4.8097 L23:   0.5365                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2590 S12:   1.1201 S13:   0.7844                       
REMARK   3      S21:   0.2347 S22:   0.1533 S23:  -0.0628                       
REMARK   3      S31:  -0.6659 S32:  -0.9543 S33:  -0.0053                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 225 THROUGH 288 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -11.2362  -0.2683  17.9972              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2787 T22:   0.8854                                     
REMARK   3      T33:   0.9747 T12:   0.0573                                     
REMARK   3      T13:  -0.1211 T23:   0.1386                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0979 L22:   1.3501                                     
REMARK   3      L33:   1.3875 L12:  -0.0375                                     
REMARK   3      L13:   0.2891 L23:  -0.0503                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1311 S12:   0.1042 S13:   0.1820                       
REMARK   3      S21:   0.1730 S22:   0.2143 S23:  -0.7713                       
REMARK   3      S31:  -0.0826 S32:   0.7516 S33:  -0.0523                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 289 THROUGH 326 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -16.2300  13.2887  27.0892              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5777 T22:   0.7251                                     
REMARK   3      T33:   0.6126 T12:  -0.2053                                     
REMARK   3      T13:  -0.1205 T23:  -0.0435                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5306 L22:   4.0921                                     
REMARK   3      L33:   2.4347 L12:  -1.2113                                     
REMARK   3      L13:  -1.2341 L23:   0.4277                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1131 S12:  -0.6133 S13:   0.4272                       
REMARK   3      S21:   1.2467 S22:   0.0230 S23:  -0.6433                       
REMARK   3      S31:  -0.2840 S32:   0.7686 S33:  -0.0573                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 327 THROUGH 405 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -31.2508   2.2162   9.6077              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1772 T22:   0.1929                                     
REMARK   3      T33:   0.3009 T12:  -0.0441                                     
REMARK   3      T13:   0.0289 T23:  -0.0072                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2727 L22:   2.5574                                     
REMARK   3      L33:   3.2438 L12:  -1.7027                                     
REMARK   3      L13:   1.0395 L23:  -1.0530                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0216 S12:  -0.0760 S13:   0.2363                       
REMARK   3      S21:  -0.0471 S22:  -0.0907 S23:  -0.4928                       
REMARK   3      S31:  -0.0717 S32:   0.3487 S33:   0.0436                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 406 THROUGH 434 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -38.3909   6.1735  31.0153              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2464 T22:   0.2153                                     
REMARK   3      T33:   0.2328 T12:  -0.0535                                     
REMARK   3      T13:  -0.0516 T23:  -0.0223                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0763 L22:   4.6075                                     
REMARK   3      L33:   4.5248 L12:   0.2382                                     
REMARK   3      L13:  -0.7407 L23:   2.2563                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2057 S12:  -0.5887 S13:   0.0537                       
REMARK   3      S21:   0.7387 S22:   0.0372 S23:  -0.5775                       
REMARK   3      S31:  -0.0803 S32:   0.5585 S33:   0.1838                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 435 THROUGH 521 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -42.9115  -0.5308  24.4283              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1636 T22:   0.1246                                     
REMARK   3      T33:   0.1658 T12:  -0.0388                                     
REMARK   3      T13:  -0.0391 T23:   0.0029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2823 L22:   2.8793                                     
REMARK   3      L33:   4.4574 L12:  -0.3187                                     
REMARK   3      L13:  -0.1382 L23:  -0.1129                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0640 S12:  -0.3483 S13:  -0.0257                       
REMARK   3      S21:   0.1457 S22:   0.0513 S23:  -0.2040                       
REMARK   3      S31:   0.1145 S32:   0.0770 S33:  -0.0739                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 160 THROUGH 199 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -31.0410  -1.5008 -23.3951              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6177 T22:   0.2774                                     
REMARK   3      T33:   0.3737 T12:   0.0266                                     
REMARK   3      T13:  -0.0138 T23:   0.0976                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2160 L22:   2.7646                                     
REMARK   3      L33:   1.4858 L12:   2.7867                                     
REMARK   3      L13:   1.0613 L23:   1.2160                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3127 S12:  -0.2877 S13:  -1.7250                       
REMARK   3      S21:   0.1823 S22:  -0.1076 S23:  -0.3772                       
REMARK   3      S31:   0.4692 S32:   0.2798 S33:  -0.2076                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 200 THROUGH 272 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -18.7264  17.3026 -18.9652              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2542 T22:   0.5444                                     
REMARK   3      T33:   0.7141 T12:  -0.0503                                     
REMARK   3      T13:  -0.0609 T23:   0.0773                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7783 L22:   1.8848                                     
REMARK   3      L33:   1.3178 L12:   0.9998                                     
REMARK   3      L13:  -0.7088 L23:   0.1832                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1066 S12:  -0.0749 S13:   0.3128                       
REMARK   3      S21:   0.0844 S22:  -0.0836 S23:  -0.5339                       
REMARK   3      S31:   0.0331 S32:   0.4021 S33:  -0.0288                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 273 THROUGH 361 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -22.0334  13.5942 -19.3595              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1995 T22:   0.3669                                     
REMARK   3      T33:   0.3251 T12:   0.0523                                     
REMARK   3      T13:  -0.0724 T23:   0.0524                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7588 L22:   2.6567                                     
REMARK   3      L33:   2.3310 L12:   0.1706                                     
REMARK   3      L13:  -0.5642 L23:   0.2395                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1873 S12:   0.1573 S13:   0.2261                       
REMARK   3      S21:  -0.1808 S22:   0.1079 S23:  -0.5324                       
REMARK   3      S31:   0.0578 S32:   0.5604 S33:  -0.3184                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 362 THROUGH 521 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -42.4608  15.0352 -23.2069              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1974 T22:   0.1185                                     
REMARK   3      T33:   0.2142 T12:   0.0249                                     
REMARK   3      T13:   0.0552 T23:   0.0161                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7821 L22:   1.1318                                     
REMARK   3      L33:   2.7905 L12:  -0.1997                                     
REMARK   3      L13:   0.5325 L23:   0.0204                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0499 S12:   0.1690 S13:   0.0166                       
REMARK   3      S21:  -0.2063 S22:  -0.0671 S23:  -0.1953                       
REMARK   3      S31:   0.0889 S32:  -0.0192 S33:  -0.0107                       
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                                     
REMARK   3     SELECTION          : CHAIN B                                     
REMARK   3     ATOM PAIRS NUMBER  : 3212                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5VDS 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_1000227270.                                   
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   : 22387                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.766                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 58.165                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 8.800                              
REMARK 200  R MERGE                    (I) : 0.23400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.77                     
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) : 0.76400                            
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   (%): 51.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
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      107.72500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.20400            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      107.72500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.20400            
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     ARG A   255                                                      
REMARK 465     ASN A   256                                                      
REMARK 465     PRO A   257                                                      
REMARK 465     ILE A   291                                                      
REMARK 465     LYS A   292                                                      
REMARK 465     ASP A   293                                                      
REMARK 465     THR A   294                                                      
REMARK 465     LYS A   301                                                      
REMARK 465     ARG A   302                                                      
REMARK 465     GLY A   303                                                      
REMARK 465     GLY A   304                                                      
REMARK 465     SER A   305                                                      
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     ARG B   255                                                      
REMARK 465     ASN B   256                                                      
REMARK 465     PRO B   257                                                      
REMARK 465     LYS B   258                                                      
REMARK 465     LYS B   292                                                      
REMARK 465     ASP B   293                                                      
REMARK 465     THR B   294                                                      
REMARK 465     LYS B   301                                                      
REMARK 465     ARG B   302                                                      
REMARK 465     GLY B   303                                                      
REMARK 465     GLY B   304                                                      
REMARK 465     SER B   305                                                      
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     GLN B   371                                                      
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     LEU A 174    CG   CD1  CD2                                       
REMARK 470     ARG A 176    CG   CD   NE   CZ   NH1  NH2                        
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     GLU A 216    CG   CD   OE1  OE2                                  
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     ASN A 289    CG   OD1  ND2                                       
REMARK 470     ASP A 290    CG   OD1  OD2                                       
REMARK 470     ASP A 295    CG   OD1  OD2                                       
REMARK 470     ARG A 300    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     LYS A 350    CD   CE   NZ                                        
REMARK 470     LYS A 365    CG   CD   CE   NZ                                   
REMARK 470     GLU A 372    CG   CD   OE1  OE2                                  
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 427    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    CE   NZ                                             
REMARK 470     LYS B 254    CG   CD   CE   NZ                                   
REMARK 470     GLU B 259    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 295    CG   OD1  OD2                                       
REMARK 470     ARG B 300    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 350    CD   CE   NZ                                        
REMARK 470     GLU B 385    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 400    CG   CD   CE   NZ                                   
REMARK 470     GLU B 401    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 422    CD   OE1  OE2                                       
REMARK 470     LYS B 425    CE   NZ                                             
REMARK 470     ASP B 426    CG   OD1  OD2                                       
REMARK 470     LYS B 428    CG   CD   CE   NZ                                   
REMARK 470     LEU B 462    CG   CD1  CD2                                       
REMARK 470     GLU B 521    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A 203       43.10    -97.66                                   
REMARK 500    ASN A 210       74.21     50.74                                   
REMARK 500    THR A 211       76.49   -105.99                                   
REMARK 500    SER A 213        6.60     57.99                                   
REMARK 500    ARG A 236       79.86     56.15                                   
REMARK 500    ARG A 246      -14.18     65.25                                   
REMARK 500    LYS A 315      -56.61   -143.44                                   
REMARK 500    TRP A 343      -68.24    -98.96                                   
REMARK 500    SER A 345      156.69     76.69                                   
REMARK 500    PHE A 516       70.03     53.04                                   
REMARK 500    PHE B 203       42.91    -97.83                                   
REMARK 500    ASN B 210       68.32    -67.45                                   
REMARK 500    THR B 211     -162.46   -113.40                                   
REMARK 500    HIS B 217       18.79     57.92                                   
REMARK 500    LYS B 219      107.58    -46.23                                   
REMARK 500    LYS B 219      108.37    -47.29                                   
REMARK 500    ALA B 222       83.11     55.57                                   
REMARK 500    ARG B 236       79.41     55.18                                   
REMARK 500    ARG B 246      -14.02     66.24                                   
REMARK 500    LYS B 315      -57.42   -143.08                                   
REMARK 500    TRP B 343      -67.70    -98.98                                   
REMARK 500    SER B 345      157.60     76.55                                   
REMARK 500    PHE B 516       71.46     53.86                                   
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  117.5                                              
REMARK 620 3 CYS A 397   SG  103.9 126.2                                        
REMARK 620 4 CYS A 404   SG   94.3 105.1 104.4                                  
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  120.1                                              
REMARK 620 3 CYS B 397   SG  103.5 122.7                                        
REMARK 620 4 CYS B 404   SG  101.1  99.7 106.5                                  
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 9BJ A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9BJ B 602                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5VDO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VDP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VDQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VDR   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  5VDS A  161   522  UNP    Q8N884   CGAS_HUMAN     161    522             
DBREF  5VDS B  161   522  UNP    Q8N884   CGAS_HUMAN     161    522             
SEQADV 5VDS MET A  160  UNP  Q8N884              EXPRESSION TAG                 
SEQADV 5VDS 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    9BJ  A 602      40                                                       
HET     ZN  B 601       1                                                       
HET    9BJ  B 602      40                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     9BJ 3',3'-CDUMP                                                      
HETSYN     9BJ 1-{(2R,6R,8R,10AR,12R,13R,13AS)-6-[(1R,2R)-2-(2,4-               
HETSYN   2 9BJ  DIOXO-3,4-DIHYDROPYRIMIDIN-1(2H)-YL)-1,2-                       
HETSYN   3 9BJ  DIHYDROXYETHYL]-2,8,13-TRIHYDROXY-2,8-DIOXOHEXAHYDRO-           
HETSYN   4 9BJ  2H,4H,8H,10H-2LAMBDA~5~,8LAMBDA~5~-FURO[3,2-D][1,3,7,           
HETSYN   5 9BJ  9,2,8]TETRAOXADIPHOSPHACYCLODODECIN-12-YL}PYRIMIDINE-           
HETSYN   6 9BJ  2,4(1H,3H)-DIONE                                                
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  9BJ    2(C18 H24 N4 O16 P2)                                         
FORMUL   7  HOH   *90(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 LEU A  262  GLN A  264  5                                   3    
HELIX    4 AA4 SER A  272  ILE A  288  1                                  17    
HELIX    5 AA5 PRO A  331  GLN A  335  5                                   5    
HELIX    6 AA6 LEU A  344  LEU A  354  1                                  11    
HELIX    7 AA7 PHE A  379  ASN A  389  1                                  11    
HELIX    8 AA8 ASN A  399  LYS A  403  5                                   5    
HELIX    9 AA9 CYS A  405  PHE A  424  1                                  20    
HELIX   10 AB1 SER A  434  ASN A  449  1                                  16    
HELIX   11 AB2 GLN A  451  LYS A  458  5                                   8    
HELIX   12 AB3 ASP A  459  THR A  477  1                                  19    
HELIX   13 AB4 ASP A  497  ASN A  514  1                                  18    
HELIX   14 AB5 GLU A  515  ASP A  520  5                                   6    
HELIX   15 AB6 GLY B  161  LYS B  173  1                                  13    
HELIX   16 AB7 SER B  175  LYS B  198  1                                  24    
HELIX   17 AB8 LEU B  262  GLN B  264  5                                   3    
HELIX   18 AB9 SER B  272  ILE B  288  1                                  17    
HELIX   19 AC1 ASN B  289  ILE B  291  5                                   3    
HELIX   20 AC2 PRO B  331  GLN B  335  5                                   5    
HELIX   21 AC3 LEU B  344  LEU B  354  1                                  11    
HELIX   22 AC4 PHE B  379  ASN B  389  1                                  11    
HELIX   23 AC5 ASN B  399  LYS B  403  5                                   5    
HELIX   24 AC6 CYS B  405  PHE B  424  1                                  20    
HELIX   25 AC7 SER B  434  ASN B  449  1                                  16    
HELIX   26 AC8 GLN B  451  LYS B  458  5                                   8    
HELIX   27 AC9 ASP B  459  GLU B  478  1                                  20    
HELIX   28 AD1 ASP B  497  ASN B  514  1                                  18    
HELIX   29 AD2 GLU B  515  ASP B  520  5                                   6    
SHEET    1 AA1 7 VAL A 206  LEU A 208  0                                        
SHEET    2 AA1 7 GLU A 225  GLU A 233 -1  O  LYS A 231   N  GLY A 207           
SHEET    3 AA1 7 ILE A 316  SER A 326  1  O  SER A 317   N  PHE A 226           
SHEET    4 AA1 7 PHE A 357  PRO A 361 -1  O  PHE A 357   N  SER A 326           
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  GLU A 240   O  PHE A 250           
SHEET    1 AA2 5 VAL A 206  LEU A 208  0                                        
SHEET    2 AA2 5 GLU A 225  GLU A 233 -1  O  LYS A 231   N  GLY A 207           
SHEET    3 AA2 5 ILE A 316  SER A 326  1  O  SER A 317   N  PHE A 226           
SHEET    4 AA2 5 VAL A 308  ILE A 312 -1  N  ILE A 312   O  ILE A 316           
SHEET    5 AA2 5 VAL A 296  MET A 298 -1  N  ILE A 297   O  LEU A 311           
SHEET    1 AA3 2 LEU A 266  GLU A 267  0                                        
SHEET    2 AA3 2 ILE A 270  LEU A 271 -1  O  ILE A 270   N  GLU A 267           
SHEET    1 AA4 7 VAL B 206  LEU B 209  0                                        
SHEET    2 AA4 7 GLU B 225  GLU B 233 -1  O  MET B 229   N  LEU B 209           
SHEET    3 AA4 7 ILE B 316  SER B 326  1  O  SER B 317   N  PHE B 226           
SHEET    4 AA4 7 PHE B 357  PRO B 361 -1  O  PHE B 357   N  SER B 326           
SHEET    5 AA4 7 TRP B 375  SER B 378 -1  O  ARG B 376   N  VAL B 360           
SHEET    6 AA4 7 TYR B 248  PHE B 253 -1  N  TYR B 249   O  TRP B 375           
SHEET    7 AA4 7 ILE B 237  GLU B 241 -1  N  GLU B 240   O  PHE B 250           
SHEET    1 AA5 5 VAL B 206  LEU B 209  0                                        
SHEET    2 AA5 5 GLU B 225  GLU B 233 -1  O  MET B 229   N  LEU B 209           
SHEET    3 AA5 5 ILE B 316  SER B 326  1  O  SER B 317   N  PHE B 226           
SHEET    4 AA5 5 VAL B 308  ILE B 312 -1  N  ILE B 312   O  ILE B 316           
SHEET    5 AA5 5 VAL B 296  MET B 298 -1  N  ILE B 297   O  LEU B 311           
SHEET    1 AA6 2 LEU B 266  GLU B 267  0                                        
SHEET    2 AA6 2 ILE B 270  LEU B 271 -1  O  ILE B 270   N  GLU B 267           
LINK         NE2 HIS A 390                ZN    ZN A 601     1555   1555  2.20  
LINK         SG  CYS A 396                ZN    ZN A 601     1555   1555  2.41  
LINK         SG  CYS A 397                ZN    ZN A 601     1555   1555  2.33  
LINK         SG  CYS A 404                ZN    ZN A 601     1555   1555  2.33  
LINK         NE2 HIS B 390                ZN    ZN B 601     1555   1555  2.22  
LINK         SG  CYS B 396                ZN    ZN B 601     1555   1555  2.48  
LINK         SG  CYS B 397                ZN    ZN B 601     1555   1555  2.35  
LINK         SG  CYS B 404                ZN    ZN B 601     1555   1555  2.30  
SITE     1 AC1  4 HIS A 390  CYS A 396  CYS A 397  CYS A 404                    
SITE     1 AC2 12 ALA A 307  THR A 321  VAL A 360  LYS A 362                    
SITE     2 AC2 12 ARG A 376  SER A 434  TYR A 436  ASN A 482                    
SITE     3 AC2 12 PHE A 488  HOH A 712  HOH A 713  HOH A 716                    
SITE     1 AC3  4 HIS B 390  CYS B 396  CYS B 397  CYS B 404                    
SITE     1 AC4 14 THR B 321  LYS B 362  ARG B 376  SER B 378                    
SITE     2 AC4 14 SER B 434  TYR B 436  ASN B 482  PHE B 488                    
SITE     3 AC4 14 LEU B 490  HOH B 704  HOH B 706  HOH B 722                    
SITE     4 AC4 14 HOH B 736  HOH B 743                                          
CRYST1  215.450   48.408   86.086  90.00 104.81  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      0.004641  0.000000  0.001228        0.00000                         
SCALE2      0.000000  0.020658  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012016        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system