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Database: PDB
Entry: 5VDR
LinkDB: 5VDR
Original site: 5VDR 
HEADER    TRANSFERASE                             03-APR-17   5VDR              
TITLE     HUMAN CYCLIC GMP-AMP SYNTHASE (CGAS) IN COMPLEX WITH 3',3'-CDIMP      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIC GMP-AMP SYNTHASE;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 161-521;                                      
COMPND   5 SYNONYM: H-CGAS,2'3'-CGAMP SYNTHASE,MAB-21 DOMAIN-CONTAINING PROTEIN 
COMPND   6 1;                                                                   
COMPND   7 EC: 2.7.7.86;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MB21D1, C6ORF150;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSFERASE, STING, CGAMP                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.J.BYRNES,J.D.HALL                                                   
REVDAT   3   06-DEC-17 5VDR    1       JRNL                                     
REVDAT   2   04-OCT-17 5VDR    1       JRNL                                     
REVDAT   1   27-SEP-17 5VDR    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.    3.04 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) : 3.04                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 55.90                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 16454                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 757                             
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 55.9102 -  5.2009    0.98     3297   161  0.1901 0.2140        
REMARK   3     2  5.2009 -  4.1285    1.00     3260   151  0.1800 0.2284        
REMARK   3     3  4.1285 -  3.6067    0.90     2879   137  0.2144 0.3062        
REMARK   3     4  3.6067 -  3.2770    0.96     3060   155  0.2490 0.2915        
REMARK   3     5  3.2770 -  3.0421    1.00     3201   153  0.2840 0.3219        
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)     : 0.370            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.910           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 65.99                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 84.04                          
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           5953                                  
REMARK   3   ANGLE     :  0.604           8053                                  
REMARK   3   CHIRALITY :  0.030            891                                  
REMARK   3   PLANARITY :  0.003            989                                  
REMARK   3   DIHEDRAL  : 13.544           2157                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 11                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 160 THROUGH 197 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -30.7802  19.3202  24.4666              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5179 T22:   0.9562                                     
REMARK   3      T33:   1.4132 T12:  -0.0814                                     
REMARK   3      T13:   0.0545 T23:  -0.0219                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7977 L22:   0.2064                                     
REMARK   3      L33:   0.3344 L12:  -0.3507                                     
REMARK   3      L13:   0.5859 L23:  -0.2600                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6999 S12:   0.1215 S13:   1.1627                       
REMARK   3      S21:   0.4110 S22:  -0.8419 S23:  -0.9112                       
REMARK   3      S31:  -0.3382 S32:   0.7427 S33:   0.1137                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 198 THROUGH 224 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -20.0986  11.6402  20.9340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7603 T22:   1.2341                                     
REMARK   3      T33:   1.4318 T12:   0.0717                                     
REMARK   3      T13:  -0.0013 T23:   0.2293                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1029 L22:   0.3087                                     
REMARK   3      L33:   2.4525 L12:  -0.1157                                     
REMARK   3      L13:  -0.3700 L23:   0.8545                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0683 S12:  -0.1353 S13:   0.2808                       
REMARK   3      S21:   0.0052 S22:  -0.3235 S23:  -0.8828                       
REMARK   3      S31:  -0.3456 S32:   0.3309 S33:   0.2870                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 225 THROUGH 272 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.4148  -6.1115  16.9858              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6161 T22:   1.1620                                     
REMARK   3      T33:   1.0490 T12:   0.2293                                     
REMARK   3      T13:   0.0330 T23:   0.1718                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5636 L22:   3.6457                                     
REMARK   3      L33:   1.2932 L12:   0.7101                                     
REMARK   3      L13:   0.1277 L23:  -0.5305                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0012 S12:   0.0074 S13:   0.1702                       
REMARK   3      S21:  -0.0613 S22:  -0.0276 S23:  -1.1614                       
REMARK   3      S31:   0.4248 S32:   0.9302 S33:   0.0661                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 273 THROUGH 306 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -11.9313   8.2523  31.5028              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7817 T22:   1.1360                                     
REMARK   3      T33:   1.1041 T12:  -0.0612                                     
REMARK   3      T13:  -0.1996 T23:   0.2541                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2198 L22:   2.1660                                     
REMARK   3      L33:   6.9817 L12:  -0.5303                                     
REMARK   3      L13:  -1.1264 L23:   3.7549                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0889 S12:  -0.3905 S13:   0.6160                       
REMARK   3      S21:   1.1829 S22:  -0.7004 S23:  -1.0810                       
REMARK   3      S31:   0.1658 S32:   0.5876 S33:   0.4904                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 307 THROUGH 476 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -35.6389   2.6066  18.4647              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4169 T22:   0.3596                                     
REMARK   3      T33:   0.2441 T12:  -0.0064                                     
REMARK   3      T13:   0.0024 T23:   0.0095                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4556 L22:   2.1550                                     
REMARK   3      L33:   3.4915 L12:  -0.1607                                     
REMARK   3      L13:  -0.5253 L23:  -0.6966                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1282 S12:  -0.0323 S13:  -0.0013                       
REMARK   3      S21:  -0.0994 S22:  -0.1113 S23:  -0.2114                       
REMARK   3      S31:  -0.1384 S32:   0.4454 S33:   0.0168                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 477 THROUGH 521 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -42.5085  -3.9211  29.6600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4507 T22:   0.3491                                     
REMARK   3      T33:   0.3061 T12:   0.0737                                     
REMARK   3      T13:  -0.0262 T23:  -0.0120                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6278 L22:   1.6832                                     
REMARK   3      L33:   4.6539 L12:   0.1284                                     
REMARK   3      L13:  -0.8568 L23:  -0.0618                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0282 S12:  -0.4340 S13:  -0.0633                       
REMARK   3      S21:   0.1556 S22:   0.1370 S23:   0.3075                       
REMARK   3      S31:  -0.0532 S32:   0.1717 S33:  -0.0814                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 160 THROUGH 197 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -31.3252  -3.4442 -24.0044              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6308 T22:   0.6009                                     
REMARK   3      T33:   0.5536 T12:   0.0162                                     
REMARK   3      T13:  -0.1323 T23:   0.0711                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1675 L22:   2.0155                                     
REMARK   3      L33:   0.9319 L12:  -0.0310                                     
REMARK   3      L13:   1.3527 L23:   0.4232                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5233 S12:   0.6176 S13:  -1.0680                       
REMARK   3      S21:  -0.0689 S22:  -0.3472 S23:  -0.2244                       
REMARK   3      S31:   0.4728 S32:   0.4065 S33:  -0.0918                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 198 THROUGH 272 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.4695  17.7358 -17.5733              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6648 T22:   1.0480                                     
REMARK   3      T33:   0.9821 T12:  -0.1715                                     
REMARK   3      T13:  -0.1784 T23:  -0.0402                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0617 L22:   4.6880                                     
REMARK   3      L33:   1.6218 L12:  -1.1009                                     
REMARK   3      L13:  -0.8189 L23:  -0.3041                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1308 S12:  -0.3162 S13:  -0.2415                       
REMARK   3      S21:   0.3350 S22:   0.3230 S23:  -1.2467                       
REMARK   3      S31:  -0.0784 S32:   0.7778 S33:  -0.2510                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 273 THROUGH 326 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -14.8274   6.6062 -29.6531              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5830 T22:   0.6872                                     
REMARK   3      T33:   0.9802 T12:   0.0753                                     
REMARK   3      T13:   0.1696 T23:   0.0058                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8773 L22:   4.3101                                     
REMARK   3      L33:   5.0844 L12:   2.2263                                     
REMARK   3      L13:   1.3400 L23:   2.4979                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2981 S12:   0.3186 S13:  -0.8576                       
REMARK   3      S21:  -0.8941 S22:   0.0111 S23:  -1.6493                       
REMARK   3      S31:  -0.3248 S32:   0.3463 S33:  -0.1674                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 327 THROUGH 405 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -30.5706  16.3033 -11.7801              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3717 T22:   0.3106                                     
REMARK   3      T33:   0.2552 T12:  -0.0282                                     
REMARK   3      T13:  -0.0755 T23:   0.0122                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9623 L22:   2.9069                                     
REMARK   3      L33:   3.6520 L12:  -0.3026                                     
REMARK   3      L13:  -1.4835 L23:  -0.4718                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0148 S12:  -0.0682 S13:  -0.0156                       
REMARK   3      S21:   0.0617 S22:   0.0123 S23:  -0.2504                       
REMARK   3      S31:  -0.0612 S32:   0.3068 S33:  -0.1004                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 406 THROUGH 521 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -43.0094  15.5296 -25.9832              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3693 T22:   0.2692                                     
REMARK   3      T33:   0.2385 T12:  -0.0195                                     
REMARK   3      T13:   0.0075 T23:   0.0096                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1843 L22:   3.4523                                     
REMARK   3      L33:   4.1496 L12:  -0.0323                                     
REMARK   3      L13:   1.0951 L23:  -0.7440                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1050 S12:   0.3611 S13:   0.1357                       
REMARK   3      S21:  -0.2696 S22:   0.0783 S23:   0.2583                       
REMARK   3      S31:  -0.1103 S32:   0.1411 S33:  -0.1647                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND SEGID                           
REMARK   3     SELECTION          : CHAIN B AND SEGID                           
REMARK   3     ATOM PAIRS NUMBER  : 3252                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5VDR 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_1000227269.                                   
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   : 16476                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.040                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 55.901                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.10100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.04                     
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) : 0.49100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: 4O67                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18-20% PEG 3350, 0.2 M AMMONIUM          
REMARK 280  CITRATE PH 7, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      107.76400            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.19750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      107.76400            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.19750            
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     GLU A   366                                                      
REMARK 465     GLY A   367                                                      
REMARK 465     ASN A   368                                                      
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     LYS A 219    CG   CD   CE   NZ                                   
REMARK 470     LYS A 254    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    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 365    CG   CD   CE   NZ                                   
REMARK 470     LYS A 384    CG   CD   CE   NZ                                   
REMARK 470     LYS A 400    CG   CD   CE   NZ                                   
REMARK 470     GLU A 401    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 418    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     ARG B 176    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B 210    CG   OD1  ND2                                       
REMARK 470     THR B 211    OG1  CG2                                            
REMARK 470     GLU B 240    CG   CD   OE1  OE2                                  
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     GLU B 287    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 292    CG   CD   CE   NZ                                   
REMARK 470     ASP B 293    CG   OD1  OD2                                       
REMARK 470     ASP B 295    CG   OD1  OD2                                       
REMARK 470     ARG B 302    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 339    NE   CZ   NH1  NH2                                  
REMARK 470     GLN B 351    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 365    CG   CD   CE   NZ                                   
REMARK 470     LYS B 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: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NZ   LYS B   315     O17  9B7 B   602     4444     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    CYS A 199       34.14    -83.22                                   
REMARK 500    PHE A 203       36.19    -84.81                                   
REMARK 500    THR A 211       33.04    -97.47                                   
REMARK 500    TYR A 214     -159.65   -125.28                                   
REMARK 500    GLU A 267       46.03    -92.13                                   
REMARK 500    GLU A 314       19.71     59.17                                   
REMARK 500    LYS A 315      -31.94   -141.06                                   
REMARK 500    TRP A 343      -64.54    -96.74                                   
REMARK 500    SER A 345      148.76     77.79                                   
REMARK 500    PHE A 424       42.26   -109.39                                   
REMARK 500    PHE A 516       72.87     39.95                                   
REMARK 500    CYS B 199       33.93    -82.86                                   
REMARK 500    PHE B 203       36.26    -85.06                                   
REMARK 500    THR B 211       33.63    -97.91                                   
REMARK 500    GLU B 267       46.19    -92.34                                   
REMARK 500    ASP B 293      -26.37     70.96                                   
REMARK 500    LYS B 315      -31.19   -142.54                                   
REMARK 500    TRP B 343      -65.02    -97.02                                   
REMARK 500    SER B 345      148.68     78.23                                   
REMARK 500    PHE B 424       42.12   -109.43                                   
REMARK 500    PHE B 516       72.23     40.35                                   
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  114.0                                              
REMARK 620 3 CYS A 397   SG   98.6 121.5                                        
REMARK 620 4 CYS A 404   SG   96.1 116.4 106.1                                  
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  125.5                                              
REMARK 620 3 CYS B 397   SG   99.7 120.9                                        
REMARK 620 4 CYS B 404   SG  102.2 107.2  96.2                                  
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 9B7 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 9B7 B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9B7 B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9B7 B 604                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5VDO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VDP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VDQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 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  5VDR A  161   522  UNP    Q8N884   CGAS_HUMAN     161    522             
DBREF  5VDR B  161   522  UNP    Q8N884   CGAS_HUMAN     161    522             
SEQADV 5VDR MET A  160  UNP  Q8N884              EXPRESSION TAG                 
SEQADV 5VDR 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    9B7  A 602      44                                                       
HET     ZN  B 601       1                                                       
HET    9B7  B 602      44                                                       
HET    9B7  B 603      44                                                       
HET    9B7  B 604      44                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     9B7 3',3'-CDIMP                                                      
HETSYN     9B7 (2R,3R,3AS,5R,7AR,9R,10R,10AS,12R,14AR)-3,5,10,12-               
HETSYN   2 9B7  TETRAHYDROXY-2,9-BIS(6-OXO-3,6-DIHYDRO-9H-PURIN-9-YL)           
HETSYN   3 9B7  OCTAHYDRO-2H,5H,7H,12H-5LAMBDA~5~,12LAMBDA~5~-                  
HETSYN   4 9B7  DIFURO[3,2-D:3',2'-J][1,3,7,9,2,                                
HETSYN   5 9B7  8]TETRAOXADIPHOSPHACYCLODODECINE-5,12-DIONE                     
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  9B7    4(C20 H22 N8 O14 P2)                                         
FORMUL   9  HOH   *32(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 SER A  201  ARG A  204  5                                   4    
HELIX    4 AA4 LEU A  262  LEU A  266  5                                   5    
HELIX    5 AA5 SER A  272  ILE A  291  1                                  20    
HELIX    6 AA6 PRO A  331  GLN A  335  5                                   5    
HELIX    7 AA7 ILE A  340  SER A  345  1                                   6    
HELIX    8 AA8 SER A  345  LEU A  354  1                                  10    
HELIX    9 AA9 PHE A  379  ASN A  389  1                                  11    
HELIX   10 AB1 ASN A  399  LYS A  403  5                                   5    
HELIX   11 AB2 CYS A  405  PHE A  424  1                                  20    
HELIX   12 AB3 SER A  434  ASN A  449  1                                  16    
HELIX   13 AB4 GLN A  451  LYS A  458  5                                   8    
HELIX   14 AB5 ASP A  459  THR A  477  1                                  19    
HELIX   15 AB6 ASP A  497  ASN A  514  1                                  18    
HELIX   16 AB7 GLY B  161  LEU B  172  1                                  12    
HELIX   17 AB8 SER B  175  LYS B  198  1                                  24    
HELIX   18 AB9 SER B  201  ARG B  204  5                                   4    
HELIX   19 AC1 ASN B  260  LEU B  266  5                                   7    
HELIX   20 AC2 SER B  272  ILE B  288  1                                  17    
HELIX   21 AC3 PRO B  331  GLN B  335  5                                   5    
HELIX   22 AC4 ILE B  340  LEU B  354  1                                  15    
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    
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 7 VAL B 206  LEU B 209  0                                        
SHEET    2 AA3 7 GLU B 225  GLU B 233 -1  O  MET B 229   N  LEU B 209           
SHEET    3 AA3 7 ILE B 316  SER B 326  1  O  SER B 317   N  PHE B 226           
SHEET    4 AA3 7 PHE B 357  VAL B 360 -1  O  PHE B 357   N  SER B 326           
SHEET    5 AA3 7 TRP B 375  SER B 378 -1  O  ARG B 376   N  VAL B 360           
SHEET    6 AA3 7 TYR B 248  PHE B 253 -1  N  TYR B 249   O  TRP B 375           
SHEET    7 AA3 7 ILE B 237  GLU B 241 -1  N  GLN B 238   O  LYS B 252           
SHEET    1 AA4 5 VAL B 206  LEU B 209  0                                        
SHEET    2 AA4 5 GLU B 225  GLU B 233 -1  O  MET B 229   N  LEU B 209           
SHEET    3 AA4 5 ILE B 316  SER B 326  1  O  SER B 317   N  PHE B 226           
SHEET    4 AA4 5 ALA B 307  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 2 ALA B 364  GLU B 366  0                                        
SHEET    2 AA5 2 GLY B 369  GLN B 371 -1  O  GLN B 371   N  ALA B 364           
LINK         NE2 HIS A 390                ZN    ZN A 601     1555   1555  2.22  
LINK         SG  CYS A 396                ZN    ZN A 601     1555   1555  2.38  
LINK         SG  CYS A 397                ZN    ZN A 601     1555   1555  2.37  
LINK         SG  CYS A 404                ZN    ZN A 601     1555   1555  2.36  
LINK         NE2 HIS B 390                ZN    ZN B 601     1555   1555  2.17  
LINK         SG  CYS B 396                ZN    ZN B 601     1555   1555  2.40  
LINK         SG  CYS B 397                ZN    ZN B 601     1555   1555  2.35  
LINK         SG  CYS B 404                ZN    ZN B 601     1555   1555  2.35  
SITE     1 AC1  4 HIS A 390  CYS A 396  CYS A 397  CYS A 404                    
SITE     1 AC2 12 ASP A 227  MET A 229  PRO A 306  THR A 321                    
SITE     2 AC2 12 LYS A 362  ARG A 376  SER A 378  SER A 380                    
SITE     3 AC2 12 SER A 434  TYR A 436  HOH A 708  HOH A 716                    
SITE     1 AC3  4 HIS B 390  CYS B 396  CYS B 397  CYS B 404                    
SITE     1 AC4 10 ASP B 177  ASP B 178  THR B 181  ALA B 182                    
SITE     2 AC4 10 ASN B 224  SER B 313  LYS B 315  ILE B 316                    
SITE     3 AC4 10 ASN B 494  9B7 B 603                                          
SITE     1 AC5  8 LYS B 315  GLY B 367  ASN B 368  ARG B 423                    
SITE     2 AC5  8 PHE B 424  GLN B 507  TYR B 510  9B7 B 602                    
SITE     1 AC6 16 ASP B 227  MET B 229  GLY B 304  SER B 305                    
SITE     2 AC6 16 PRO B 306  THR B 321  LYS B 362  ARG B 376                    
SITE     3 AC6 16 SER B 378  SER B 380  SER B 434  TYR B 436                    
SITE     4 AC6 16 HOH B 703  HOH B 704  HOH B 713  HOH B 716                    
CRYST1  215.528   48.395   89.099  90.00 109.89  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      0.004640  0.000000  0.001679        0.00000                         
SCALE2      0.000000  0.020663  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011936        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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