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Database: PDB
Entry: 5VDT
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Original site: 5VDT 
HEADER    TRANSFERASE                             03-APR-17   5VDT              
TITLE     HUMAN CYCLIC GMP-AMP SYNTHASE (CGAS) IN COMPLEX WITH 3',3'-CGAMP      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIC GMP-AMP SYNTHASE;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 161-522;                                      
COMPND   5 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 5VDT    1       JRNL                                     
REVDAT   2   04-OCT-17 5VDT    1       JRNL                                     
REVDAT   1   27-SEP-17 5VDT    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.    2.58 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) : 2.58                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 55.31                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 26697                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1333                            
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 55.3185 -  5.5484    1.00     2674   151  0.1758 0.1984        
REMARK   3     2  5.5484 -  4.4045    1.00     2584   147  0.1614 0.1752        
REMARK   3     3  4.4045 -  3.8479    0.99     2559   130  0.1781 0.2198        
REMARK   3     4  3.8479 -  3.4962    0.91     2319   139  0.1887 0.2506        
REMARK   3     5  3.4962 -  3.2456    0.97     2513   113  0.2280 0.2543        
REMARK   3     6  3.2456 -  3.0543    1.00     2536   140  0.2293 0.2694        
REMARK   3     7  3.0543 -  2.9013    1.00     2589   122  0.2533 0.3457        
REMARK   3     8  2.9013 -  2.7750    1.00     2532   149  0.2658 0.3093        
REMARK   3     9  2.7750 -  2.6682    0.99     2516   121  0.2681 0.3324        
REMARK   3    10  2.6682 -  2.5761    0.99     2542   121  0.3046 0.3455        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.500           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 48.07                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 64.39                          
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      :  0.003           5909                                  
REMARK   3   ANGLE     :  0.647           7972                                  
REMARK   3   CHIRALITY :  0.034            879                                  
REMARK   3   PLANARITY :  0.002            996                                  
REMARK   3   DIHEDRAL  : 13.056           2190                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 160 THROUGH 199 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -28.5075  -2.4526 -23.6531              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5686 T22:   0.4169                                     
REMARK   3      T33:   0.3844 T12:   0.0320                                     
REMARK   3      T13:  -0.0446 T23:   0.0930                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4809 L22:   3.5633                                     
REMARK   3      L33:   0.9154 L12:   2.0481                                     
REMARK   3      L13:  -0.7020 L23:   0.5756                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1198 S12:  -0.6133 S13:  -0.8044                       
REMARK   3      S21:  -0.0330 S22:  -0.1050 S23:  -0.4627                       
REMARK   3      S31:   0.1151 S32:   0.0527 S33:   0.2156                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 200 THROUGH 272 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -15.4758  16.9119 -17.5287              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4119 T22:   0.6775                                     
REMARK   3      T33:   0.6543 T12:  -0.0913                                     
REMARK   3      T13:  -0.0863 T23:   0.1049                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0519 L22:   4.4437                                     
REMARK   3      L33:   3.5028 L12:  -2.0251                                     
REMARK   3      L13:  -0.9014 L23:   0.4718                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0667 S12:  -0.4910 S13:   0.2618                       
REMARK   3      S21:   0.4195 S22:  -0.0676 S23:  -0.9517                       
REMARK   3      S31:  -0.2031 S32:   0.6708 S33:   0.0822                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 273 THROUGH 405 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -24.3978  13.0504 -18.3663              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3517 T22:   0.4215                                     
REMARK   3      T33:   0.3863 T12:   0.0008                                     
REMARK   3      T13:  -0.0885 T23:   0.0245                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1912 L22:   2.4197                                     
REMARK   3      L33:   3.8025 L12:  -0.0983                                     
REMARK   3      L13:  -2.1166 L23:  -0.1093                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1236 S12:   0.0166 S13:  -0.0039                       
REMARK   3      S21:   0.0033 S22:  -0.0767 S23:  -0.4783                       
REMARK   3      S31:  -0.1305 S32:   0.3188 S33:  -0.0657                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 406 THROUGH 521 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -42.6902  15.4016 -26.1149              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2853 T22:   0.2305                                     
REMARK   3      T33:   0.2460 T12:   0.0395                                     
REMARK   3      T13:   0.0185 T23:  -0.0170                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6223 L22:   3.0179                                     
REMARK   3      L33:   5.9114 L12:   0.4096                                     
REMARK   3      L13:   0.8028 L23:  -0.3574                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0517 S12:   0.1405 S13:  -0.0920                       
REMARK   3      S21:  -0.2359 S22:   0.0627 S23:   0.0381                       
REMARK   3      S31:  -0.0299 S32:   0.1062 S33:  -0.0001                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 160 THROUGH 199 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -29.2872  19.1875  23.8093              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5656 T22:   0.6448                                     
REMARK   3      T33:   0.8633 T12:  -0.0460                                     
REMARK   3      T13:   0.0270 T23:   0.2156                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6864 L22:   3.5012                                     
REMARK   3      L33:   1.0865 L12:  -3.0470                                     
REMARK   3      L13:  -1.1950 L23:   1.1723                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5167 S12:  -0.1374 S13:   1.2385                       
REMARK   3      S21:   0.2285 S22:  -0.3454 S23:  -1.0808                       
REMARK   3      S31:  -0.4363 S32:   0.5598 S33:  -0.1969                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 200 THROUGH 272 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.9115  -2.4062  17.2145              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4824 T22:   0.9541                                     
REMARK   3      T33:   0.7329 T12:   0.1555                                     
REMARK   3      T13:   0.0773 T23:   0.2087                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0432 L22:   6.5814                                     
REMARK   3      L33:   1.0206 L12:   1.2480                                     
REMARK   3      L13:   0.7040 L23:  -0.0223                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1183 S12:   0.5462 S13:  -0.0352                       
REMARK   3      S21:  -0.1039 S22:  -0.0135 S23:  -1.0891                       
REMARK   3      S31:   0.2002 S32:   0.5891 S33:   0.0642                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 273 THROUGH 388 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -21.6349   1.9418  20.3476              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3986 T22:   0.6558                                     
REMARK   3      T33:   0.5290 T12:  -0.0186                                     
REMARK   3      T13:   0.0153 T23:   0.0957                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0407 L22:   3.6289                                     
REMARK   3      L33:   4.1033 L12:   0.3937                                     
REMARK   3      L13:   2.1629 L23:   0.1364                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1257 S12:  -0.3610 S13:   0.2427                       
REMARK   3      S21:   0.3548 S22:  -0.3841 S23:  -0.8103                       
REMARK   3      S31:   0.2202 S32:   0.4702 S33:   0.1358                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 389 THROUGH 521 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -43.2787   2.0604  23.7127              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2949 T22:   0.3110                                     
REMARK   3      T33:   0.3104 T12:  -0.0003                                     
REMARK   3      T13:  -0.0218 T23:  -0.0103                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4486 L22:   1.5857                                     
REMARK   3      L33:   6.0693 L12:   0.1880                                     
REMARK   3      L13:  -1.2477 L23:  -0.1148                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0589 S12:  -0.0413 S13:   0.0906                       
REMARK   3      S21:   0.0653 S22:   0.0427 S23:   0.0340                       
REMARK   3      S31:  -0.0366 S32:  -0.0687 S33:  -0.0877                       
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  : 3354                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5VDT 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_1000227271.                                   
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   : 26726                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.576                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 55.306                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : 0.18700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.58                     
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) : 0.55800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: 4O67                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51                     
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      106.94800            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.98750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      106.94800            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.98750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ILE A   220                                                      
REMARK 465     SER A   221                                                      
REMARK 465     PHE A   522                                                      
REMARK 465     SER B   213                                                      
REMARK 465     TYR B   214                                                      
REMARK 465     TYR B   215                                                      
REMARK 465     GLU B   216                                                      
REMARK 465     HIS B   217                                                      
REMARK 465     VAL B   218                                                      
REMARK 465     LYS B   219                                                      
REMARK 465     ILE B   220                                                      
REMARK 465     SER B   221                                                      
REMARK 465     PHE B   522                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 173    CG   CD   CE   NZ                                   
REMARK 470     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     LYS A 219    CG   CD   CE   NZ                                   
REMARK 470     GLU A 225    CG   CD   OE1  OE2                                  
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     ASP A 290    CG   OD1  OD2                                       
REMARK 470     ASP A 293    CG   OD1  OD2                                       
REMARK 470     THR A 294    OG1  CG2                                            
REMARK 470     ASP A 295    CG   OD1  OD2                                       
REMARK 470     ARG A 302    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 400    CG   CD   CE   NZ                                   
REMARK 470     GLU A 401    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 425    CE   NZ                                             
REMARK 470     LYS A 428    CG   CD   CE   NZ                                   
REMARK 470     ARG A 499    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 521    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 173    CG   CD   CE   NZ                                   
REMARK 470     ASN B 210    CG   OD1  ND2                                       
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     LYS B 292    CG   CD   CE   NZ                                   
REMARK 470     ASP B 293    CG   OD1  OD2                                       
REMARK 470     ASP B 295    CG   OD1  OD2                                       
REMARK 470     ARG B 302    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 365    CG   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 418    CD   OE1  OE2                                       
REMARK 470     LYS B 425    CG   CD   CE   NZ                                   
REMARK 470     ASP B 426    CG   OD1  OD2                                       
REMARK 470     LYS B 428    CG   CD   CE   NZ                                   
REMARK 470     ARG B 499    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU B 521    CG   CD   OE1  OE2                                  
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A  418   CD                                                  
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    TYR A 215       38.35     38.70                                   
REMARK 500    HIS A 217      115.89   -161.73                                   
REMARK 500    ARG A 246       -8.45     70.02                                   
REMARK 500    ASP A 293       12.14    -67.99                                   
REMARK 500    LYS A 315      -29.25   -143.17                                   
REMARK 500    SER A 345      153.91     83.27                                   
REMARK 500    PRO A 361       77.19    -69.92                                   
REMARK 500    GLU A 372        3.39     55.76                                   
REMARK 500    PHE A 424       42.10   -107.71                                   
REMARK 500    ARG B 246       -8.85     69.83                                   
REMARK 500    ASP B 293       10.69     54.13                                   
REMARK 500    LYS B 315      -28.39   -143.90                                   
REMARK 500    TRP B 343      -63.60   -109.94                                   
REMARK 500    SER B 345      154.50     83.12                                   
REMARK 500    PHE B 424       42.26   -107.09                                   
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  120.7                                              
REMARK 620 3 CYS A 397   SG  110.3 121.6                                        
REMARK 620 4 CYS A 404   SG  101.4  97.3  98.7                                  
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  115.8                                              
REMARK 620 3 CYS B 397   SG  106.8 127.1                                        
REMARK 620 4 CYS B 404   SG   97.2 102.6 101.4                                  
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 4BW 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 4BW 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: 5VDS   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  5VDT A  161   522  UNP    Q8N884   CGAS_HUMAN     161    522             
DBREF  5VDT B  161   522  UNP    Q8N884   CGAS_HUMAN     161    522             
SEQADV 5VDT MET A  160  UNP  Q8N884              EXPRESSION TAG                 
SEQADV 5VDT 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    4BW  A 602      45                                                       
HET     ZN  B 601       1                                                       
HET    4BW  B 602      45                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     4BW 2-AMINO-9-[(2R,3R,3AS,5R,7AR,9R,10R,10AS,12R,14AR)-9-            
HETNAM   2 4BW  (6-AMINO-9H-PURIN-9-YL)-3,5,10,12-TETRAHYDROXY-5,12-            
HETNAM   3 4BW  DIOXIDOOCTAHYDRO-2H,7H-DIFURO[3,2-D:3',2'-J][1,3,7,9,           
HETNAM   4 4BW  2,8]TETRAOXADIPHOSPHACYCLODODECIN-2-YL]-1,9-DIHYDRO-            
HETNAM   5 4BW  6H-PURIN-6-ONE                                                  
HETSYN     4BW 3',3' CGAMP, C-GMP-AMP, C[G(3',5')PA(3',5')P]                    
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  4BW    2(C20 H24 N10 O13 P2)                                        
FORMUL   7  HOH   *146(H2 O)                                                    
HELIX    1 AA1 GLY A  161  LEU A  172  1                                  12    
HELIX    2 AA2 SER A  175  LYS A  198  1                                  24    
HELIX    3 AA3 LEU A  262  GLN A  264  5                                   3    
HELIX    4 AA4 SER A  272  GLU A  287  1                                  16    
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  389  1                                  11    
HELIX    9 AA9 ASN A  399  LYS A  403  5                                   5    
HELIX   10 AB1 CYS A  405  PHE A  424  1                                  20    
HELIX   11 AB2 SER A  434  ASN A  449  1                                  16    
HELIX   12 AB3 GLN A  451  LYS A  458  5                                   8    
HELIX   13 AB4 ASP A  459  GLU A  478  1                                  20    
HELIX   14 AB5 ASP A  497  ASN A  514  1                                  18    
HELIX   15 AB6 GLU A  515  ASP A  520  5                                   6    
HELIX   16 AB7 GLY B  161  LYS B  173  1                                  13    
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  GLU B  287  1                                  16    
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  389  1                                  11    
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 SER B  434  ASN B  449  1                                  16    
HELIX   27 AC9 GLN B  451  LYS B  458  5                                   8    
HELIX   28 AD1 ASP B  459  GLU B  478  1                                  20    
HELIX   29 AD2 ASP B  497  ASN B  514  1                                  18    
HELIX   30 AD3 GLU B  515  ASP B  520  5                                   6    
SHEET    1 AA1 7 VAL A 206  LEU A 209  0                                        
SHEET    2 AA1 7 GLU A 225  GLU A 233 -1  O  MET A 229   N  LEU A 209           
SHEET    3 AA1 7 ILE A 316  SER A 326  1  O  SER A 317   N  PHE A 226           
SHEET    4 AA1 7 PHE A 357  VAL A 360 -1  O  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  MET A 229   N  LEU A 209           
SHEET    3 AA2 5 ILE A 316  SER A 326  1  O  SER A 317   N  PHE A 226           
SHEET    4 AA2 5 ALA A 307  ILE A 312 -1  N  ILE A 312   O  ILE A 316           
SHEET    5 AA2 5 VAL A 296  MET A 298 -1  N  ILE A 297   O  LEU A 311           
SHEET    1 AA3 2 LEU A 266  GLU A 267  0                                        
SHEET    2 AA3 2 ILE A 270  LEU A 271 -1  O  ILE A 270   N  GLU A 267           
SHEET    1 AA4 2 LYS A 365  GLU A 366  0                                        
SHEET    2 AA4 2 GLY A 369  PHE A 370 -1  O  GLY A 369   N  GLU A 366           
SHEET    1 AA5 7 VAL B 206  LEU B 209  0                                        
SHEET    2 AA5 7 GLU B 225  GLU B 233 -1  O  MET B 229   N  LEU B 209           
SHEET    3 AA5 7 ILE B 316  SER B 326  1  O  SER B 317   N  PHE B 226           
SHEET    4 AA5 7 PHE B 357  VAL B 360 -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  MET B 229   N  LEU B 209           
SHEET    3 AA6 5 ILE B 316  SER B 326  1  O  SER B 317   N  PHE B 226           
SHEET    4 AA6 5 ALA B 307  ILE B 312 -1  N  ILE B 312   O  ILE B 316           
SHEET    5 AA6 5 VAL B 296  MET B 298 -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  O  ILE B 270   N  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  2.20  
LINK         SG  CYS A 396                ZN    ZN A 601     1555   1555  2.44  
LINK         SG  CYS A 397                ZN    ZN A 601     1555   1555  2.29  
LINK         SG  CYS A 404                ZN    ZN A 601     1555   1555  2.42  
LINK         NE2 HIS B 390                ZN    ZN B 601     1555   1555  2.14  
LINK         SG  CYS B 396                ZN    ZN B 601     1555   1555  2.36  
LINK         SG  CYS B 397                ZN    ZN B 601     1555   1555  2.32  
LINK         SG  CYS B 404                ZN    ZN B 601     1555   1555  2.40  
SITE     1 AC1  4 HIS A 390  CYS A 396  CYS A 397  CYS A 404                    
SITE     1 AC2 18 ASP A 227  MET A 229  GLY A 304  SER A 305                    
SITE     2 AC2 18 PRO A 306  ALA A 307  THR A 321  LYS A 362                    
SITE     3 AC2 18 ARG A 376  SER A 378  SER A 380  SER A 434                    
SITE     4 AC2 18 TYR A 436  HOH A 712  HOH A 741  HOH A 760                    
SITE     5 AC2 18 HOH A 761  HOH A 763                                          
SITE     1 AC3  4 HIS B 390  CYS B 396  CYS B 397  CYS B 404                    
SITE     1 AC4 15 ASP B 227  MET B 229  GLY B 304  PRO B 306                    
SITE     2 AC4 15 ALA B 307  THR B 321  LYS B 362  ARG B 376                    
SITE     3 AC4 15 SER B 378  SER B 380  SER B 434  TYR B 436                    
SITE     4 AC4 15 HOH B 727  HOH B 738  HOH B 748                               
CRYST1  213.896   47.975   88.274  90.00 110.07  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      0.004675  0.000000  0.001708        0.00000                         
SCALE2      0.000000  0.020844  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012060        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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