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Database: PDB
Entry: 5VDU
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Original site: 5VDU 
HEADER    TRANSFERASE                             03-APR-17   5VDU              
TITLE     HUMAN CYCLIC GMP-AMP SYNTHASE (CGAS) IN COMPLEX WITH COMPOUND F2      
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 5VDU    1       JRNL                                     
REVDAT   2   04-OCT-17 5VDU    1       JRNL                                     
REVDAT   1   27-SEP-17 5VDU    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.    2.73 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) : 2.73                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 52.27                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 22914                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.630                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1061                            
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 52.2839 -  5.4556    0.97     2808   150  0.1928 0.2065        
REMARK   3     2  5.4556 -  4.3310    0.98     2724   141  0.1804 0.2256        
REMARK   3     3  4.3310 -  3.7837    0.96     2690   122  0.1984 0.2259        
REMARK   3     4  3.7837 -  3.4378    0.97     2674   111  0.2319 0.3010        
REMARK   3     5  3.4378 -  3.1914    0.99     2732   135  0.2588 0.2840        
REMARK   3     6  3.1914 -  3.0033    0.99     2701   138  0.2640 0.2781        
REMARK   3     7  3.0033 -  2.8529    0.99     2750   144  0.2821 0.3192        
REMARK   3     8  2.8529 -  2.7287    0.99     2774   120  0.3253 0.3669        
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)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.860           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 46.77                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 65.17                          
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           5708                                  
REMARK   3   ANGLE     :  0.665           7843                                  
REMARK   3   CHIRALITY :  0.030            870                                  
REMARK   3   PLANARITY :  0.003           1099                                  
REMARK   3   DIHEDRAL  : 12.390           2158                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 160 THROUGH 253 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -25.9808   7.7507 -21.1454              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4730 T22:   0.5260                                     
REMARK   3      T33:   0.2471 T12:   0.0775                                     
REMARK   3      T13:   0.0061 T23:   0.0881                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4115 L22:   2.0702                                     
REMARK   3      L33:   1.5627 L12:   0.2144                                     
REMARK   3      L13:   0.6271 L23:   0.5036                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2359 S12:   0.1582 S13:  -0.2167                       
REMARK   3      S21:  -0.0466 S22:  -0.2151 S23:  -0.3047                       
REMARK   3      S31:   0.3093 S32:   0.5628 S33:  -0.0125                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 254 THROUGH 307 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.7022  13.0036 -25.7450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3416 T22:   0.9648                                     
REMARK   3      T33:   0.6214 T12:   0.0850                                     
REMARK   3      T13:   0.1477 T23:   0.2306                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2532 L22:   5.4672                                     
REMARK   3      L33:   6.0262 L12:   2.1631                                     
REMARK   3      L13:   2.9859 L23:   4.1804                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1960 S12:   0.4877 S13:  -0.2579                       
REMARK   3      S21:  -0.1549 S22:  -0.0727 S23:  -1.2920                       
REMARK   3      S31:   0.3577 S32:   1.1049 S33:  -0.3941                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 308 THROUGH 405 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -30.4012  14.0892 -14.4197              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2778 T22:   0.3309                                     
REMARK   3      T33:   0.2511 T12:   0.0335                                     
REMARK   3      T13:  -0.0648 T23:   0.0383                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8223 L22:   0.9351                                     
REMARK   3      L33:   4.0211 L12:   0.0731                                     
REMARK   3      L13:  -0.9586 L23:   0.0232                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0263 S12:   0.0700 S13:   0.0614                       
REMARK   3      S21:   0.1600 S22:  -0.0886 S23:   0.0241                       
REMARK   3      S31:  -0.0612 S32:   0.4724 S33:   0.0034                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 406 THROUGH 520 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -44.9360  15.1102 -26.1604              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2918 T22:   0.1984                                     
REMARK   3      T33:   0.1977 T12:   0.0068                                     
REMARK   3      T13:   0.0508 T23:  -0.0264                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2891 L22:   2.7578                                     
REMARK   3      L33:   4.1799 L12:  -0.3785                                     
REMARK   3      L13:   0.4888 L23:  -0.4942                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0180 S12:   0.2872 S13:  -0.0345                       
REMARK   3      S21:  -0.2052 S22:   0.0274 S23:  -0.1350                       
REMARK   3      S31:   0.0603 S32:   0.0533 S33:  -0.0456                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 160 THROUGH 224 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -26.9618  16.5740  21.0780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5655 T22:   0.6324                                     
REMARK   3      T33:   0.7218 T12:  -0.1203                                     
REMARK   3      T13:   0.0632 T23:   0.0273                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.7604 L22:   0.4829                                     
REMARK   3      L33:   0.8890 L12:  -0.7321                                     
REMARK   3      L13:  -1.5390 L23:   0.1123                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1305 S12:   0.0995 S13:   0.6468                       
REMARK   3      S21:  -0.1747 S22:  -0.1599 S23:  -0.3550                       
REMARK   3      S31:  -0.3696 S32:   0.3737 S33:  -0.0499                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 225 THROUGH 272 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -12.8807  -4.4310  15.4286              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3777 T22:   0.7226                                     
REMARK   3      T33:   0.6769 T12:   0.1527                                     
REMARK   3      T13:   0.0730 T23:   0.0167                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7056 L22:   6.9019                                     
REMARK   3      L33:   2.8923 L12:   2.1719                                     
REMARK   3      L13:   0.5983 L23:  -1.8265                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0157 S12:   0.6331 S13:  -0.5137                       
REMARK   3      S21:  -0.0948 S22:  -0.0822 S23:  -1.0107                       
REMARK   3      S31:   0.2044 S32:   0.9202 S33:   0.0890                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 273 THROUGH 326 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -12.6930  11.4318  26.7653              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5811 T22:   0.8041                                     
REMARK   3      T33:   0.7547 T12:  -0.1883                                     
REMARK   3      T13:  -0.1017 T23:  -0.0399                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9268 L22:   7.1062                                     
REMARK   3      L33:   2.7281 L12:  -3.4115                                     
REMARK   3      L13:  -2.0416 L23:   4.0388                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1502 S12:  -0.3016 S13:   0.9863                       
REMARK   3      S21:   0.5870 S22:   0.4295 S23:  -1.0757                       
REMARK   3      S31:  -0.5803 S32:   1.1737 S33:  -0.0261                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 327 THROUGH 405 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -31.1224   0.5937  10.5015              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3249 T22:   0.2362                                     
REMARK   3      T33:   0.2724 T12:  -0.0567                                     
REMARK   3      T13:   0.0564 T23:   0.0078                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7900 L22:   2.9667                                     
REMARK   3      L33:   4.2941 L12:  -1.9586                                     
REMARK   3      L13:   0.7056 L23:  -0.4210                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0008 S12:  -0.0578 S13:   0.1071                       
REMARK   3      S21:  -0.1023 S22:   0.0309 S23:  -0.2974                       
REMARK   3      S31:   0.1004 S32:   0.4772 S33:  -0.1097                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 406 THROUGH 434 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -38.6169   5.5425  31.1124              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3345 T22:   0.3229                                     
REMARK   3      T33:   0.2821 T12:  -0.1059                                     
REMARK   3      T13:  -0.0689 T23:  -0.0239                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3191 L22:   4.3551                                     
REMARK   3      L33:   3.8834 L12:   0.6003                                     
REMARK   3      L13:  -1.4169 L23:   3.0351                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0555 S12:  -0.9111 S13:   0.0550                       
REMARK   3      S21:   0.8965 S22:  -0.0011 S23:  -0.4758                       
REMARK   3      S31:  -0.6387 S32:   0.4804 S33:   0.0221                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 435 THROUGH 520 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -43.2939  -1.4004  24.0481              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2791 T22:   0.1697                                     
REMARK   3      T33:   0.2293 T12:  -0.0287                                     
REMARK   3      T13:  -0.0118 T23:  -0.0026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8296 L22:   2.3111                                     
REMARK   3      L33:   5.6434 L12:  -0.0538                                     
REMARK   3      L13:  -1.2143 L23:  -0.2326                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0229 S12:  -0.2006 S13:  -0.0874                       
REMARK   3      S21:  -0.0080 S22:   0.0281 S23:  -0.0201                       
REMARK   3      S31:   0.1087 S32:   0.1833 S33:  -0.0735                       
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  : 3326                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5VDU 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_1000227272.                                   
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 0.5.12                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22940                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.729                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 52.274                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.11900                            
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) : 2.73                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.69200                            
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   (%): 52.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
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      108.20750            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.00950            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      108.20750            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.00950            
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     GLU A   521                                                      
REMARK 465     PHE A   522                                                      
REMARK 465     GLU B   521                                                      
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     ARG A 176    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 187    CG   CD   CE   NZ                                   
REMARK 470     HIS A 192    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU A 195    CG   CD1  CD2                                       
REMARK 470     ARG A 196    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 198    CG   CD   CE   NZ                                   
REMARK 470     ARG A 236    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 240    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 252    CE   NZ                                             
REMARK 470     LYS A 254    CG   CD   CE   NZ                                   
REMARK 470     ARG A 255    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 256    CG   OD1  ND2                                       
REMARK 470     LYS A 258    CG   CD   CE   NZ                                   
REMARK 470     GLU A 259    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 266    CG   CD1  CD2                                       
REMARK 470     GLU A 267    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 269    CD   OE1  OE2                                       
REMARK 470     LEU A 277    CG   CD1  CD2                                       
REMARK 470     ARG A 281    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 282    CG   CD   CE   NZ                                   
REMARK 470     LYS A 285    CG   CD   CE   NZ                                   
REMARK 470     GLU A 286    CG   CD   OE1  OE2                                  
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     MET A 298    CG   SD   CE                                        
REMARK 470     LYS A 299    CG   CD   CE   NZ                                   
REMARK 470     ARG A 300    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 301    CG   CD   CE   NZ                                   
REMARK 470     ARG A 302    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 305    OG                                                  
REMARK 470     LYS A 315    CG   CD   CE   NZ                                   
REMARK 470     ASP A 319    CG   OD1  OD2                                       
REMARK 470     LYS A 365    CG   CD   CE   NZ                                   
REMARK 470     GLU A 366    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 368    CG   OD1  ND2                                       
REMARK 470     PHE A 370    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A 372    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 373    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 400    CG   CD   CE   NZ                                   
REMARK 470     GLU A 422    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 426    CG   OD1  OD2                                       
REMARK 470     LYS A 428    CG   CD   CE   NZ                                   
REMARK 470     LYS A 432    CG   CD   CE   NZ                                   
REMARK 470     ARG A 499    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 176    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 178    CG   OD1  OD2                                       
REMARK 470     ILE B 179    CG1  CG2  CD1                                       
REMARK 470     MET B 185    CG   SD   CE                                        
REMARK 470     LYS B 187    CG   CD   CE   NZ                                   
REMARK 470     LEU B 195    CG   CD1  CD2                                       
REMARK 470     LYS B 198    CG   CD   CE   NZ                                   
REMARK 470     ARG B 204    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 221    OG                                                  
REMARK 470     ARG B 236    CG   CD   NE   CZ   NH1  NH2                        
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 266    CG   CD1  CD2                                       
REMARK 470     GLU B 267    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 269    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 275    CG   CD   CE   NZ                                   
REMARK 470     LYS B 279    CG   CD   CE   NZ                                   
REMARK 470     ARG B 281    NE   CZ   NH1  NH2                                  
REMARK 470     LYS B 282    CG   CD   CE   NZ                                   
REMARK 470     LYS B 285    CG   CD   CE   NZ                                   
REMARK 470     GLU B 287    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 292    CG   CD   CE   NZ                                   
REMARK 470     ASP B 293    CG   OD1  OD2                                       
REMARK 470     THR B 294    OG1  CG2                                            
REMARK 470     MET B 298    CG   SD   CE                                        
REMARK 470     ARG B 300    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 301    CG   CD   CE   NZ                                   
REMARK 470     ARG B 302    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 305    OG                                                  
REMARK 470     GLU B 314    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 315    CG   CD   CE   NZ                                   
REMARK 470     ASP B 319    CG   OD1  OD2                                       
REMARK 470     LYS B 365    CG   CD   CE   NZ                                   
REMARK 470     GLU B 366    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 368    CG   OD1  ND2                                       
REMARK 470     GLU B 372    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 373    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 400    CG   CD   CE   NZ                                   
REMARK 470     ASP B 426    CG   OD1  OD2                                       
REMARK 470     LYS B 428    CG   CD   CE   NZ                                   
REMARK 470     ASP B 431    CG   OD1  OD2                                       
REMARK 470     LYS B 432    CG   CD   CE   NZ                                   
REMARK 470     ARG B 499    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A 203       42.74   -104.26                                   
REMARK 500    ALA A 222       65.33   -152.70                                   
REMARK 500    ARG A 246      -14.19     67.15                                   
REMARK 500    ARG A 302      -67.81   -137.49                                   
REMARK 500    PRO A 306       95.48    -67.88                                   
REMARK 500    SER A 313     -135.51     53.56                                   
REMARK 500    LYS A 315      -55.89   -135.54                                   
REMARK 500    TRP A 343      -66.15   -105.00                                   
REMARK 500    SER A 345      157.69     87.90                                   
REMARK 500    ASN A 389       69.83   -157.42                                   
REMARK 500    PHE B 203       43.03   -103.92                                   
REMARK 500    ALA B 222       65.74   -153.05                                   
REMARK 500    SER B 243     -118.10     54.97                                   
REMARK 500    ARG B 246      -11.20     64.66                                   
REMARK 500    ARG B 302      -67.97   -137.53                                   
REMARK 500    PRO B 306       96.21    -67.57                                   
REMARK 500    SER B 313     -134.72     53.44                                   
REMARK 500    LYS B 315      -56.52   -135.94                                   
REMARK 500    TRP B 343      -66.84   -104.52                                   
REMARK 500    SER B 345      156.65     87.57                                   
REMARK 500    ASN B 389       69.03   -157.18                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 726        DISTANCE =  6.13 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 390   NE2                                                    
REMARK 620 2 CYS A 396   SG  119.5                                              
REMARK 620 3 CYS A 397   SG  106.1 121.9                                        
REMARK 620 4 CYS A 404   SG   90.6 109.5 103.8                                  
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  117.2                                              
REMARK 620 3 CYS B 397   SG  101.1 125.7                                        
REMARK 620 4 CYS B 404   SG   94.6 110.0 103.2                                  
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 9BS 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 9BS B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9BS B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9BS B 604                 
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: 5VDS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VDT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VDV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VDW   RELATED DB: PDB                                   
DBREF  5VDU A  161   522  UNP    Q8N884   CGAS_HUMAN     161    522             
DBREF  5VDU B  161   522  UNP    Q8N884   CGAS_HUMAN     161    522             
SEQADV 5VDU MET A  160  UNP  Q8N884              EXPRESSION TAG                 
SEQADV 5VDU 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    9BS  A 602      36                                                       
HET     ZN  B 601       1                                                       
HET    9BS  B 602      36                                                       
HET    9BS  B 603      12                                                       
HET    9BS  B 604      12                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     9BS 2-(PYRIDIN-2-YL)PYRIMIDINE                                       
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  9BS    4(C9 H7 N3)                                                  
FORMUL   9  HOH   *52(H2 O)                                                     
HELIX    1 AA1 GLY A  161  LEU A  174  1                                  14    
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  291  1                                  20    
HELIX    5 AA5 PRO A  331  GLN A  335  5                                   5    
HELIX    6 AA6 ILE A  340  SER A  345  1                                   6    
HELIX    7 AA7 SER A  345  ARG A  353  1                                   9    
HELIX    8 AA8 PHE A  379  ASN A  388  1                                  10    
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  THR A  477  1                                  19    
HELIX   14 AB5 ASP A  497  ASN A  514  1                                  18    
HELIX   15 AB6 GLU A  515  ASP A  520  5                                   6    
HELIX   16 AB7 GLY B  161  LEU B  174  1                                  14    
HELIX   17 AB8 SER B  175  LYS B  198  1                                  24    
HELIX   18 AB9 LEU B  262  GLN B  264  5                                   3    
HELIX   19 AC1 SER B  272  ILE B  291  1                                  20    
HELIX   20 AC2 PRO B  331  GLN B  335  5                                   5    
HELIX   21 AC3 ILE B  340  SER B  345  1                                   6    
HELIX   22 AC4 SER B  345  ARG B  353  1                                   9    
HELIX   23 AC5 PHE B  379  ASN B  388  1                                  10    
HELIX   24 AC6 ASN B  399  LYS B  403  5                                   5    
HELIX   25 AC7 CYS B  405  PHE B  424  1                                  20    
HELIX   26 AC8 HIS B  429  PHE B  433  5                                   5    
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  THR B  477  1                                  19    
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  LYS A 231   N  GLY A 207           
SHEET    3 AA1 7 ILE A 316  SER A 326  1  O  ASP A 319   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  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  LYS A 231   N  GLY A 207           
SHEET    3 AA2 5 ILE A 316  SER A 326  1  O  ASP A 319   N  PHE A 226           
SHEET    4 AA2 5 VAL A 308  ILE A 312 -1  N  LEU A 310   O  VAL A 318           
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  N  ILE A 270   O  GLU A 267           
SHEET    1 AA4 2 ALA A 364  LYS A 365  0                                        
SHEET    2 AA4 2 PHE A 370  GLN A 371 -1  O  GLN A 371   N  ALA A 364           
SHEET    1 AA5 7 VAL B 206  LEU B 209  0                                        
SHEET    2 AA5 7 GLU B 225  GLU B 233 -1  O  LYS B 231   N  GLY B 207           
SHEET    3 AA5 7 ILE B 316  SER B 326  1  O  GLU B 325   N  LEU B 232           
SHEET    4 AA5 7 PHE B 357  PRO B 361 -1  O  PHE B 357   N  SER B 326           
SHEET    5 AA5 7 TRP B 375  SER B 378 -1  O  ARG B 376   N  VAL B 360           
SHEET    6 AA5 7 TYR B 248  PHE B 253 -1  N  TYR B 249   O  TRP B 375           
SHEET    7 AA5 7 ILE B 237  GLU B 241 -1  N  GLN B 238   O  LYS B 252           
SHEET    1 AA6 5 VAL B 206  LEU B 209  0                                        
SHEET    2 AA6 5 GLU B 225  GLU B 233 -1  O  LYS B 231   N  GLY B 207           
SHEET    3 AA6 5 ILE B 316  SER B 326  1  O  GLU B 325   N  LEU B 232           
SHEET    4 AA6 5 VAL B 308  ILE B 312 -1  N  LEU B 310   O  VAL B 318           
SHEET    5 AA6 5 VAL B 296  ILE B 297 -1  N  ILE B 297   O  LEU B 311           
SHEET    1 AA7 2 LEU B 266  GLU B 267  0                                        
SHEET    2 AA7 2 ILE B 270  LEU B 271 -1  N  ILE B 270   O  GLU B 267           
SHEET    1 AA8 2 ALA B 364  LYS B 365  0                                        
SHEET    2 AA8 2 PHE B 370  GLN B 371 -1  O  GLN B 371   N  ALA B 364           
LINK         NE2 HIS A 390                ZN    ZN A 601     1555   1555  2.16  
LINK         SG  CYS A 396                ZN    ZN A 601     1555   1555  2.43  
LINK         SG  CYS A 397                ZN    ZN A 601     1555   1555  2.35  
LINK         SG  CYS A 404                ZN    ZN A 601     1555   1555  2.32  
LINK         NE2 HIS B 390                ZN    ZN B 601     1555   1555  2.15  
LINK         SG  CYS B 396                ZN    ZN B 601     1555   1555  2.39  
LINK         SG  CYS B 397                ZN    ZN B 601     1555   1555  2.32  
LINK         SG  CYS B 404                ZN    ZN B 601     1555   1555  2.37  
SITE     1 AC1  4 HIS A 390  CYS A 396  CYS A 397  CYS A 404                    
SITE     1 AC2  7 ARG A 376  LEU A 377  TYR A 436  HIS A 437                    
SITE     2 AC2  7 ASN A 482  PHE A 488  LEU A 490                               
SITE     1 AC3  4 HIS B 390  CYS B 396  CYS B 397  CYS B 404                    
SITE     1 AC4  5 ARG B 376  LEU B 377  SER B 434  TYR B 436                    
SITE     2 AC4  5 ASN B 482                                                     
SITE     1 AC5  4 LYS B 506  GLN B 507  TYR B 510  9BS B 604                    
SITE     1 AC6  5 LEU A 311  GLU A 314  LYS B 506  GLN B 507                    
SITE     2 AC6  5 9BS B 603                                                     
CRYST1  216.415   48.019   86.466  90.00 104.94  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      0.004621  0.000000  0.001233        0.00000                         
SCALE2      0.000000  0.020825  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011970        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system