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Database: PDB
Entry: 5VDO
LinkDB: 5VDO
Original site: 5VDO 
HEADER    TRANSFERASE                             03-APR-17   5VDO              
TITLE     HUMAN CYCLIC GMP-AMP SYNTHASE (CGAS) IN COMPLEX WITH 2',2'-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 5VDO    1       JRNL                                     
REVDAT   2   04-OCT-17 5VDO    1       JRNL                                     
REVDAT   1   27-SEP-17 5VDO    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.    3.22 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) : 3.22                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 55.72                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 14157                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.180                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 733                             
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 55.7264 -  5.5013    0.99     2773   155  0.1980 0.2420        
REMARK   3     2  5.5013 -  4.3671    1.00     2669   154  0.1860 0.2338        
REMARK   3     3  4.3671 -  3.8152    1.00     2689   133  0.1953 0.2683        
REMARK   3     4  3.8152 -  3.4664    1.00     2656   158  0.2204 0.2547        
REMARK   3     5  3.4664 -  3.2180    0.99     2637   133  0.2765 0.3780        
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)     : 0.460            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.140           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 75.42                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 104.9                          
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           5904                                  
REMARK   3   ANGLE     :  0.577           7966                                  
REMARK   3   CHIRALITY :  0.029            879                                  
REMARK   3   PLANARITY :  0.003            996                                  
REMARK   3   DIHEDRAL  : 12.582           2182                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 160 THROUGH 199 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -29.1731  -2.9216 -23.5480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1253 T22:   0.7581                                     
REMARK   3      T33:   0.6022 T12:   0.0291                                     
REMARK   3      T13:  -0.0936 T23:   0.2801                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8161 L22:   4.1640                                     
REMARK   3      L33:   5.4011 L12:   1.1550                                     
REMARK   3      L13:   4.3983 L23:   1.6316                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.8568 S12:   0.8612 S13:  -1.7220                       
REMARK   3      S21:  -0.0119 S22:  -1.0049 S23:  -0.7658                       
REMARK   3      S31:   0.8282 S32:   1.0871 S33:  -0.9315                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 200 THROUGH 224 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -22.0100   3.9920 -20.6852              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0900 T22:   1.8527                                     
REMARK   3      T33:   1.1369 T12:  -0.3209                                     
REMARK   3      T13:   0.2236 T23:   0.0465                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.4293 L22:   8.5180                                     
REMARK   3      L33:   5.2513 L12:   5.3978                                     
REMARK   3      L13:   6.5279 L23:   5.0687                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.2900 S12:  -1.3275 S13:   0.7480                       
REMARK   3      S21:  -0.7622 S22:  -0.1256 S23:   0.3315                       
REMARK   3      S31:   1.4716 S32:   0.8604 S33:   1.3930                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 225 THROUGH 298 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -12.2829  16.6646 -20.5952              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7126 T22:   1.7854                                     
REMARK   3      T33:   1.1665 T12:  -0.3416                                     
REMARK   3      T13:   0.0348 T23:   0.3024                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7226 L22:   9.2102                                     
REMARK   3      L33:   3.3972 L12:  -2.0994                                     
REMARK   3      L13:   0.1026 L23:   1.8816                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1880 S12:  -0.0203 S13:  -0.0693                       
REMARK   3      S21:  -0.3839 S22:   0.1047 S23:  -1.7912                       
REMARK   3      S31:  -0.4344 S32:   1.5740 S33:  -0.3817                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 299 THROUGH 334 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -20.2916  11.2474 -23.7312              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1134 T22:   0.9008                                     
REMARK   3      T33:   0.6469 T12:  -0.0361                                     
REMARK   3      T13:   0.0527 T23:   0.0917                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2771 L22:   4.4814                                     
REMARK   3      L33:   4.9509 L12:  -3.5185                                     
REMARK   3      L13:  -3.8438 L23:   4.4177                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0966 S12:   0.3093 S13:   0.1280                       
REMARK   3      S21:  -1.1047 S22:  -0.1983 S23:  -0.3795                       
REMARK   3      S31:  -0.3484 S32:   0.3142 S33:   0.1485                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 335 THROUGH 405 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -31.9657  15.4682 -12.1895              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6518 T22:   0.4792                                     
REMARK   3      T33:   0.4505 T12:  -0.1202                                     
REMARK   3      T13:   0.0116 T23:  -0.0469                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4508 L22:   4.9535                                     
REMARK   3      L33:   6.6563 L12:   1.0819                                     
REMARK   3      L13:  -2.2763 L23:  -1.6456                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0003 S12:  -0.2740 S13:  -0.3431                       
REMARK   3      S21:   0.1362 S22:  -0.2129 S23:  -0.6711                       
REMARK   3      S31:  -0.5049 S32:   0.6926 S33:   0.0962                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 406 THROUGH 521 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -43.3971  15.3168 -26.1616              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7016 T22:   0.3726                                     
REMARK   3      T33:   0.2692 T12:  -0.1059                                     
REMARK   3      T13:   0.0082 T23:   0.0214                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6154 L22:   3.4351                                     
REMARK   3      L33:   6.2804 L12:   0.4228                                     
REMARK   3      L13:   0.1255 L23:  -0.4622                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0082 S12:   0.5125 S13:   0.1292                       
REMARK   3      S21:  -0.3471 S22:   0.0744 S23:   0.0130                       
REMARK   3      S31:   0.0503 S32:   0.4579 S33:  -0.0899                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 160 THROUGH 272 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -20.0761   5.6595  19.4481              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7427 T22:   1.0777                                     
REMARK   3      T33:   0.8907 T12:  -0.0088                                     
REMARK   3      T13:   0.1455 T23:   0.2168                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7973 L22:   4.5167                                     
REMARK   3      L33:   5.1059 L12:   0.2177                                     
REMARK   3      L13:  -1.4577 L23:   1.0832                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2272 S12:   0.1218 S13:   0.5647                       
REMARK   3      S21:  -0.2526 S22:   0.0116 S23:  -1.7380                       
REMARK   3      S31:  -0.5175 S32:   1.7035 S33:  -0.3177                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 273 THROUGH 325 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.9976   9.7277  29.5226              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0284 T22:   2.0633                                     
REMARK   3      T33:   1.3598 T12:  -0.0998                                     
REMARK   3      T13:  -0.2282 T23:  -0.0728                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.4369 L22:   5.4867                                     
REMARK   3      L33:   8.3042 L12:  -6.2010                                     
REMARK   3      L13:  -3.0562 L23:   4.8062                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2886 S12:  -1.8864 S13:   0.6516                       
REMARK   3      S21:   1.0098 S22:   1.0053 S23:  -1.7003                       
REMARK   3      S31:  -0.1731 S32:   1.6411 S33:  -0.7041                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 326 THROUGH 521 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -38.5364  -0.1955  20.4228              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5842 T22:   0.3393                                     
REMARK   3      T33:   0.3813 T12:   0.0657                                     
REMARK   3      T13:  -0.0036 T23:   0.0008                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4930 L22:   3.5062                                     
REMARK   3      L33:   6.4068 L12:  -0.2581                                     
REMARK   3      L13:  -0.0934 L23:  -1.2758                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0465 S12:  -0.2161 S13:  -0.1163                       
REMARK   3      S21:   0.1340 S22:  -0.0128 S23:  -0.4469                       
REMARK   3      S31:   0.1317 S32:   0.5901 S33:   0.0197                       
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  : 3287                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5VDO 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_1000227162.                                   
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   : 14176                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.218                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 55.718                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : 0.16500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.22                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.39                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: 4O67                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.19                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18-20% PEG 3350, 0.2 M AMMONIUM          
REMARK 280  CITRATE PH 7, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      108.21150            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.83500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      108.21150            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.83500            
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     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     LYS A 254    CG   CD   CE   NZ                                   
REMARK 470     LYS A 258    CG   CD   CE   NZ                                   
REMARK 470     GLU A 259    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 289    CG   OD1  ND2                                       
REMARK 470     ASP A 290    CG   OD1  OD2                                       
REMARK 470     ASP A 293    CG   OD1  OD2                                       
REMARK 470     THR A 294    OG1  CG2                                            
REMARK 470     ASP A 295    CG   OD1  OD2                                       
REMARK 470     ARG A 302    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 314    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 315    CG   CD   CE   NZ                                   
REMARK 470     ARG A 339    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 385    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 400    CG   CD   CE   NZ                                   
REMARK 470     GLU A 401    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 425    CG   CD   CE   NZ                                   
REMARK 470     LYS A 428    CG   CD   CE   NZ                                   
REMARK 470     GLU A 521    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 173    CG   CD   CE   NZ                                   
REMARK 470     ASN B 210    CG   OD1  ND2                                       
REMARK 470     THR B 211    OG1  CG2                                            
REMARK 470     ILE B 220    CG1  CG2  CD1                                       
REMARK 470     SER B 221    OG                                                  
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    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 425    CG   CD   CE   NZ                                   
REMARK 470     ASP B 426    CG   OD1  OD2                                       
REMARK 470     LYS B 428    CG   CD   CE   NZ                                   
REMARK 470     GLU B 521    CG   CD   OE1  OE2                                  
REMARK 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       31.48    -96.62                                   
REMARK 500    ASN A 210       93.61    -65.33                                   
REMARK 500    ARG A 246       -6.16     64.47                                   
REMARK 500    GLU A 267       52.45    -95.09                                   
REMARK 500    ASP A 290       77.03     48.66                                   
REMARK 500    LYS A 315      -36.61   -141.17                                   
REMARK 500    TRP A 343      -70.81    -87.96                                   
REMARK 500    SER A 345      147.70     75.89                                   
REMARK 500    LEU A 354       31.74    -90.41                                   
REMARK 500    PRO A 361       95.40    -67.50                                   
REMARK 500    ASN A 368       40.54    -96.97                                   
REMARK 500    GLU A 372       18.05     55.21                                   
REMARK 500    PHE A 516       71.58     52.01                                   
REMARK 500    PHE B 203       32.30    -95.12                                   
REMARK 500    ASN B 210       92.13    -65.64                                   
REMARK 500    ARG B 246       -6.00     63.81                                   
REMARK 500    GLU B 267       52.53    -95.82                                   
REMARK 500    ASP B 293       -9.56     66.08                                   
REMARK 500    LYS B 315      -37.22   -140.83                                   
REMARK 500    TRP B 343      -71.45    -87.87                                   
REMARK 500    SER B 345      147.30     75.37                                   
REMARK 500    LEU B 354       31.66    -90.69                                   
REMARK 500    PRO B 361       96.72    -67.45                                   
REMARK 500    GLU B 372       21.15    -72.53                                   
REMARK 500    PHE B 516       72.09     52.36                                   
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  126.0                                              
REMARK 620 3 CYS A 397   SG  104.2 120.0                                        
REMARK 620 4 CYS A 404   SG  101.9 103.7  94.7                                  
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  121.3                                              
REMARK 620 3 CYS B 397   SG  107.8 120.8                                        
REMARK 620 4 CYS B 404   SG  101.5 101.1  99.2                                  
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 1YC 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 1YC B 602                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
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: 5VDU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VDV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VDW   RELATED DB: PDB                                   
DBREF  5VDO A  161   522  UNP    Q8N884   CGAS_HUMAN     161    522             
DBREF  5VDO B  161   522  UNP    Q8N884   CGAS_HUMAN     161    522             
SEQADV 5VDO MET A  160  UNP  Q8N884              EXPRESSION TAG                 
SEQADV 5VDO 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    1YC  A 602      45                                                       
HET     ZN  B 601       1                                                       
HET    1YC  B 602      45                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     1YC 2-AMINO-9-[(1R,3R,6R,8R,9R,11S,14R,16R,17R,18R)-16-(6-           
HETNAM   2 1YC  AMINO-9H-PURIN-9-YL)-3,11,17,18-TETRAHYDROXY-3,11-              
HETNAM   3 1YC  DIOXIDO-2,4,7,10,12,15-HEXAOXA-3,11-                            
HETNAM   4 1YC  DIPHOSPHATRICYCLO[12.2.1.1~6,9~]OCTADEC-8-YL]-1,9-              
HETNAM   5 1YC  DIHYDRO-6H-PURIN-6-ONE                                          
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  1YC    2(C20 H24 N10 O13 P2)                                        
FORMUL   7  HOH   *2(H2 O)                                                      
HELIX    1 AA1 GLY A  161  LYS A  173  1                                  13    
HELIX    2 AA2 SER A  175  LYS A  198  1                                  24    
HELIX    3 AA3 CYS A  199  ASP A  200  5                                   2    
HELIX    4 AA4 SER A  201  ARG A  204  5                                   4    
HELIX    5 AA5 ASN A  260  GLN A  264  5                                   5    
HELIX    6 AA6 SER A  272  ILE A  288  1                                  17    
HELIX    7 AA7 PRO A  331  GLN A  335  5                                   5    
HELIX    8 AA8 LEU A  344  LEU A  354  1                                  11    
HELIX    9 AA9 PHE A  379  ASN A  389  1                                  11    
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 PHE A  516  GLU A  521  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 CYS B  199  ASP B  200  5                                   2    
HELIX   19 AC1 SER B  201  ARG B  204  5                                   4    
HELIX   20 AC2 ASN B  260  GLN B  264  5                                   5    
HELIX   21 AC3 SER B  272  ILE B  288  1                                  17    
HELIX   22 AC4 PRO B  331  GLN B  335  5                                   5    
HELIX   23 AC5 LEU B  344  LEU B  354  1                                  11    
HELIX   24 AC6 PHE B  379  ASN B  389  1                                  11    
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    
SHEET    1 AA1 5 VAL A 206  LEU A 208  0                                        
SHEET    2 AA1 5 GLU A 225  GLU A 233 -1  O  LYS A 231   N  GLY A 207           
SHEET    3 AA1 5 ILE A 316  GLU A 325  1  O  THR A 321   N  PHE A 230           
SHEET    4 AA1 5 VAL A 308  ILE A 312 -1  N  ILE A 312   O  ILE A 316           
SHEET    5 AA1 5 VAL A 296  MET A 298 -1  N  ILE A 297   O  LEU A 311           
SHEET    1 AA2 4 ILE A 237  GLU A 241  0                                        
SHEET    2 AA2 4 TYR A 248  PHE A 253 -1  O  LYS A 252   N  GLN A 238           
SHEET    3 AA2 4 TRP A 375  SER A 378 -1  O  TRP A 375   N  TYR A 249           
SHEET    4 AA2 4 TYR A 358  PRO A 361 -1  N  VAL A 360   O  ARG A 376           
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 5 VAL B 206  LEU B 209  0                                        
SHEET    2 AA4 5 GLU B 225  GLU B 233 -1  O  LYS B 231   N  GLY B 207           
SHEET    3 AA4 5 ILE B 316  GLU B 325  1  O  ALA B 323   N  PHE B 230           
SHEET    4 AA4 5 VAL B 308  ILE B 312 -1  N  ILE B 312   O  ILE B 316           
SHEET    5 AA4 5 VAL B 296  MET B 298 -1  N  ILE B 297   O  LEU B 311           
SHEET    1 AA5 4 ILE B 237  GLU B 241  0                                        
SHEET    2 AA5 4 TYR B 248  PHE B 253 -1  O  LYS B 252   N  GLN B 238           
SHEET    3 AA5 4 TRP B 375  SER B 378 -1  O  TRP B 375   N  TYR B 249           
SHEET    4 AA5 4 TYR B 358  PRO B 361 -1  N  VAL B 360   O  ARG B 376           
SHEET    1 AA6 2 LEU B 266  GLU B 267  0                                        
SHEET    2 AA6 2 ILE B 270  LEU B 271 -1  O  ILE B 270   N  GLU B 267           
LINK         NE2 HIS A 390                ZN    ZN A 601     1555   1555  2.08  
LINK         SG  CYS A 396                ZN    ZN A 601     1555   1555  2.45  
LINK         SG  CYS A 397                ZN    ZN A 601     1555   1555  2.40  
LINK         SG  CYS A 404                ZN    ZN A 601     1555   1555  2.34  
LINK         NE2 HIS B 390                ZN    ZN B 601     1555   1555  2.09  
LINK         SG  CYS B 396                ZN    ZN B 601     1555   1555  2.54  
LINK         SG  CYS B 397                ZN    ZN B 601     1555   1555  2.30  
LINK         SG  CYS B 404                ZN    ZN B 601     1555   1555  2.33  
SITE     1 AC1  4 HIS A 390  CYS A 396  CYS A 397  CYS A 404                    
SITE     1 AC2  6 SER A 305  ASP A 319  LYS A 362  ARG A 376                    
SITE     2 AC2  6 SER A 434  TYR A 436                                          
SITE     1 AC3  4 HIS B 390  CYS B 396  CYS B 397  CYS B 404                    
SITE     1 AC4  7 SER B 305  ALA B 307  ASP B 319  LYS B 362                    
SITE     2 AC4  7 ARG B 376  SER B 434  TYR B 436                               
CRYST1  216.423   47.670   88.861  90.00 110.18  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  0.001698        0.00000                         
SCALE2      0.000000  0.020977  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011989        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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