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Database: PDB
Entry: 5VDQ
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HEADER    TRANSFERASE                             03-APR-17   5VDQ              
TITLE     HUMAN CYCLIC GMP-AMP SYNTHASE (CGAS) IN COMPLEX WITH 2',5'-GPAP       
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 5VDQ    1       JRNL                                     
REVDAT   2   04-OCT-17 5VDQ    1       JRNL                                     
REVDAT   1   27-SEP-17 5VDQ    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.    3.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX DEV_1999                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 55.49                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 13599                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.265                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.790                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 652                             
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 55.5002 -  5.5484    0.98     2654   138  0.1893 0.2355        
REMARK   3     2  5.5484 -  4.4045    0.99     2596   122  0.1810 0.2431        
REMARK   3     3  4.4045 -  3.8479    0.99     2589   121  0.1974 0.2527        
REMARK   3     4  3.8479 -  3.4962    1.00     2565   129  0.2417 0.2915        
REMARK   3     5  3.4962 -  3.2456    1.00     2543   142  0.3042 0.3869        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.580            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.520           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 75.12                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 90.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           5894                                  
REMARK   3   ANGLE     :  0.677           7949                                  
REMARK   3   CHIRALITY :  0.033            876                                  
REMARK   3   PLANARITY :  0.003            994                                  
REMARK   3   DIHEDRAL  : 13.258           2177                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 160 THROUGH 199 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -29.1993 -26.5321 -23.6340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8220 T22:   0.5612                                     
REMARK   3      T33:   0.6432 T12:   0.0778                                     
REMARK   3      T13:  -0.0225 T23:   0.1695                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3685 L22:   3.5844                                     
REMARK   3      L33:   1.5699 L12:   1.6184                                     
REMARK   3      L13:   1.8457 L23:   1.8097                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6823 S12:   0.4823 S13:  -1.5625                       
REMARK   3      S21:   0.2403 S22:  -0.3505 S23:  -0.5091                       
REMARK   3      S31:   0.5326 S32:   0.4250 S33:  -0.2611                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 200 THROUGH 272 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -15.7941  -7.2803 -17.4509              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5291 T22:   0.8081                                     
REMARK   3      T33:   0.7759 T12:  -0.1284                                     
REMARK   3      T13:  -0.1310 T23:   0.1034                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8265 L22:   5.7952                                     
REMARK   3      L33:   3.3647 L12:  -2.8579                                     
REMARK   3      L13:  -0.7314 L23:   0.4670                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0788 S12:  -0.1025 S13:   0.2974                       
REMARK   3      S21:  -0.0809 S22:  -0.0307 S23:  -1.2465                       
REMARK   3      S31:  -0.3928 S32:   0.8259 S33:   0.0892                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 273 THROUGH 388 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -21.6438  -9.7256 -20.0164              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5888 T22:   0.5068                                     
REMARK   3      T33:   0.5456 T12:  -0.0644                                     
REMARK   3      T13:  -0.0336 T23:   0.0433                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3782 L22:   2.5298                                     
REMARK   3      L33:   6.2968 L12:  -1.8948                                     
REMARK   3      L13:  -2.0570 L23:   1.2407                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1179 S12:  -0.3271 S13:  -0.0141                       
REMARK   3      S21:  -0.2179 S22:  -0.2482 S23:  -0.3708                       
REMARK   3      S31:  -0.3992 S32:   0.7617 S33:   0.0974                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 389 THROUGH 521 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -43.1431  -9.7867 -23.8925              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5095 T22:   0.2967                                     
REMARK   3      T33:   0.3141 T12:  -0.0200                                     
REMARK   3      T13:   0.0433 T23:  -0.0408                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7124 L22:   3.4875                                     
REMARK   3      L33:   5.8719 L12:   0.6926                                     
REMARK   3      L13:   0.9958 L23:  -1.0826                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0146 S12:   0.1829 S13:  -0.0410                       
REMARK   3      S21:  -0.1264 S22:   0.1204 S23:   0.2216                       
REMARK   3      S31:   0.0005 S32:  -0.0723 S33:  -0.1157                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 160 THROUGH 248 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -23.6025 -14.1660  20.7964              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6129 T22:   0.9270                                     
REMARK   3      T33:   1.0472 T12:   0.0303                                     
REMARK   3      T13:   0.1276 T23:   0.1767                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5193 L22:   1.6649                                     
REMARK   3      L33:   1.0255 L12:  -0.9596                                     
REMARK   3      L13:   0.0487 L23:   0.0792                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1772 S12:   0.6221 S13:   1.1465                       
REMARK   3      S21:  -0.1526 S22:  -0.2162 S23:  -0.7428                       
REMARK   3      S31:  -0.3084 S32:   0.5925 S33:   0.0585                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 249 THROUGH 388 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -19.3571 -23.5188  19.8873              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6521 T22:   0.9531                                     
REMARK   3      T33:   0.6884 T12:   0.0734                                     
REMARK   3      T13:   0.0167 T23:   0.2051                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1327 L22:   4.3929                                     
REMARK   3      L33:   3.6627 L12:   1.1264                                     
REMARK   3      L13:   1.6145 L23:   0.3799                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0219 S12:  -0.1051 S13:   0.0244                       
REMARK   3      S21:   0.4555 S22:  -0.4505 S23:  -1.0609                       
REMARK   3      S31:   0.4288 S32:   1.0002 S33:   0.2927                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 389 THROUGH 521 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -43.4936 -21.9941  23.9181              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4344 T22:   0.4079                                     
REMARK   3      T33:   0.3560 T12:   0.0113                                     
REMARK   3      T13:  -0.0073 T23:   0.0257                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6123 L22:   2.9610                                     
REMARK   3      L33:   7.5360 L12:  -0.7148                                     
REMARK   3      L13:  -0.7862 L23:  -1.0992                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0496 S12:  -0.0386 S13:  -0.0807                       
REMARK   3      S21:   0.0764 S22:   0.1774 S23:   0.2279                       
REMARK   3      S31:  -0.0431 S32:   0.1060 S33:  -0.2196                       
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  : 3338                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5VDQ 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_1000227268.                                   
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   : 13619                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.246                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 55.492                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.08800                            
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) : 3.24                     
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) : 0.50200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: 4O67                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18-20% PEG 3350, 0.2 M AMMONIUM          
REMARK 280  CITRATE PH 7, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      107.60550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.81600            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      107.60550            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.81600            
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     LYS A   219                                                      
REMARK 465     ILE A   220                                                      
REMARK 465     SER A   221                                                      
REMARK 465     PHE A   522                                                      
REMARK 465     SER B   213                                                      
REMARK 465     TYR B   214                                                      
REMARK 465     TYR B   215                                                      
REMARK 465     GLU B   216                                                      
REMARK 465     HIS B   217                                                      
REMARK 465     VAL B   218                                                      
REMARK 465     LYS B   219                                                      
REMARK 465     ILE B   220                                                      
REMARK 465     SER B   221                                                      
REMARK 465     PHE B   522                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 173    CG   CD   CE   NZ                                   
REMARK 470     LEU A 174    CG   CD1  CD2                                       
REMARK 470     ARG A 176    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 177    CG   OD1  OD2                                       
REMARK 470     ASP A 178    CG   OD1  OD2                                       
REMARK 470     ARG A 204    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 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    CD   NE   CZ   NH1  NH2                             
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     ASN B 210    CG   OD1  ND2                                       
REMARK 470     THR B 211    OG1  CG2                                            
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     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 IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER A   435     O28  9BG A   602              2.15            
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    PHE A 203       31.74    -99.69                                   
REMARK 500    PRO A 223        2.49    -44.31                                   
REMARK 500    ARG A 246      -10.24     67.79                                   
REMARK 500    GLU A 267       66.34   -107.92                                   
REMARK 500    ASN A 289       66.50    -67.55                                   
REMARK 500    TRP A 343      -64.23   -106.45                                   
REMARK 500    SER A 345      152.05     76.82                                   
REMARK 500    PRO A 361       76.72    -67.84                                   
REMARK 500    GLU A 372       14.55     52.39                                   
REMARK 500    PHE A 424       42.55   -103.60                                   
REMARK 500    PHE A 516       73.74     51.70                                   
REMARK 500    PHE B 203       31.18    -99.47                                   
REMARK 500    ARG B 246      -10.61     68.29                                   
REMARK 500    GLU B 267       66.45   -108.00                                   
REMARK 500    ASP B 293       -6.14     63.65                                   
REMARK 500    TRP B 343      -63.31   -106.44                                   
REMARK 500    SER B 345      151.42     76.59                                   
REMARK 500    PRO B 361       77.85    -68.12                                   
REMARK 500    GLU B 372       16.52    -69.28                                   
REMARK 500    PHE B 424       43.06   -103.98                                   
REMARK 500    PHE B 516       73.43     52.05                                   
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  118.5                                              
REMARK 620 3 CYS A 397   SG   87.7 120.5                                        
REMARK 620 4 CYS A 404   SG  106.0 120.6  97.3                                  
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  116.4                                              
REMARK 620 3 CYS B 397   SG   94.2 123.2                                        
REMARK 620 4 CYS B 404   SG   96.1 117.1 104.6                                  
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 9BG 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 9BG B 602                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5VDO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VDP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 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  5VDQ A  161   522  UNP    Q8N884   CGAS_HUMAN     161    522             
DBREF  5VDQ B  161   522  UNP    Q8N884   CGAS_HUMAN     161    522             
SEQADV 5VDQ MET A  160  UNP  Q8N884              EXPRESSION TAG                 
SEQADV 5VDQ 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    9BG  A 602      46                                                       
HET     ZN  B 601       1                                                       
HET    9BG  B 602      46                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     9BG 2',5'-GPAP                                                       
HETSYN     9BG [(2~{R},3~{S},4~{R},5~{R})-5-(6-AMINOPURIN-9-YL)-4-              
HETSYN   2 9BG  OXIDANYL-3-PHOSPHONOOXY-OXOLAN-2-YL]METHYL [(2~{R},             
HETSYN   3 9BG  3~{R},4~{R},5~{R})-2-(2-AZANYL-6-OXIDANYLIDENE-3~{H}-           
HETSYN   4 9BG  PURIN-9-YL)-5-(HYDROXYMETHYL)-4-OXIDANYL-OXOLAN-3-YL]           
HETSYN   5 9BG  HYDROGEN PHOSPHATE                                              
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  9BG    2(C20 H26 N10 O14 P2)                                        
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 ASN A  260  GLN A  264  5                                   5    
HELIX    4 AA4 SER A  272  ILE A  288  1                                  17    
HELIX    5 AA5 PRO A  331  GLN A  335  5                                   5    
HELIX    6 AA6 ILE A  340  SER A  345  1                                   6    
HELIX    7 AA7 SER A  345  LEU A  354  1                                  10    
HELIX    8 AA8 PHE A  379  ASN A  389  1                                  11    
HELIX    9 AA9 ASN A  399  LYS A  403  5                                   5    
HELIX   10 AB1 CYS A  405  PHE A  424  1                                  20    
HELIX   11 AB2 SER A  434  ASN A  449  1                                  16    
HELIX   12 AB3 GLN A  451  LYS A  458  5                                   8    
HELIX   13 AB4 ASP A  459  GLU A  478  1                                  20    
HELIX   14 AB5 ASP A  497  ASN A  514  1                                  18    
HELIX   15 AB6 GLU A  515  ASP A  520  5                                   6    
HELIX   16 AB7 GLY B  161  LYS B  173  1                                  13    
HELIX   17 AB8 SER B  175  LYS B  198  1                                  24    
HELIX   18 AB9 LEU B  262  LEU B  266  5                                   5    
HELIX   19 AC1 SER B  272  ILE B  288  1                                  17    
HELIX   20 AC2 PRO B  331  GLN B  335  5                                   5    
HELIX   21 AC3 ILE B  340  SER B  345  1                                   6    
HELIX   22 AC4 SER B  345  LEU B  354  1                                  10    
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  LEU A 310   O  VAL A 318           
SHEET    5 AA2 5 VAL A 296  MET A 298 -1  N  ILE A 297   O  LEU A 311           
SHEET    1 AA3 2 LEU A 266  GLU A 267  0                                        
SHEET    2 AA3 2 ILE A 270  LEU A 271 -1  O  ILE A 270   N  GLU A 267           
SHEET    1 AA4 2 LYS A 365  GLU A 366  0                                        
SHEET    2 AA4 2 GLY A 369  PHE A 370 -1  O  GLY A 369   N  GLU A 366           
SHEET    1 AA5 7 VAL B 206  LEU B 209  0                                        
SHEET    2 AA5 7 GLU B 225  GLU B 233 -1  O  MET B 229   N  LEU B 209           
SHEET    3 AA5 7 ILE B 316  SER B 326  1  O  SER B 317   N  PHE B 226           
SHEET    4 AA5 7 PHE B 357  VAL B 360 -1  O  PHE B 357   N  SER B 326           
SHEET    5 AA5 7 TRP B 375  SER B 378 -1  O  ARG B 376   N  VAL B 360           
SHEET    6 AA5 7 TYR B 248  PHE B 253 -1  N  TYR B 249   O  TRP B 375           
SHEET    7 AA5 7 ILE B 237  GLU B 241 -1  N  GLN B 238   O  LYS B 252           
SHEET    1 AA6 5 VAL B 206  LEU B 209  0                                        
SHEET    2 AA6 5 GLU B 225  GLU B 233 -1  O  MET B 229   N  LEU B 209           
SHEET    3 AA6 5 ILE B 316  SER B 326  1  O  SER B 317   N  PHE B 226           
SHEET    4 AA6 5 ALA B 307  ILE B 312 -1  N  LEU B 310   O  VAL B 318           
SHEET    5 AA6 5 VAL B 296  MET B 298 -1  N  ILE B 297   O  LEU B 311           
LINK         NE2 HIS A 390                ZN    ZN A 601     1555   1555  2.30  
LINK         SG  CYS A 396                ZN    ZN A 601     1555   1555  2.42  
LINK         SG  CYS A 397                ZN    ZN A 601     1555   1555  2.46  
LINK         SG  CYS A 404                ZN    ZN A 601     1555   1555  2.25  
LINK         NE2 HIS B 390                ZN    ZN B 601     1555   1555  2.26  
LINK         SG  CYS B 396                ZN    ZN B 601     1555   1555  2.46  
LINK         SG  CYS B 397                ZN    ZN B 601     1555   1555  2.30  
LINK         SG  CYS B 404                ZN    ZN B 601     1555   1555  2.34  
SITE     1 AC1  4 HIS A 390  CYS A 396  CYS A 397  CYS A 404                    
SITE     1 AC2  9 GLU A 216  ASP A 227  SER A 305  ALA A 307                    
SITE     2 AC2  9 LYS A 362  ARG A 376  SER A 434  SER A 435                    
SITE     3 AC2  9 TYR A 436                                                     
SITE     1 AC3  4 HIS B 390  CYS B 396  CYS B 397  CYS B 404                    
SITE     1 AC4 10 ASP B 227  SER B 305  ASP B 319  THR B 321                    
SITE     2 AC4 10 LYS B 362  ARG B 376  LYS B 414  SER B 434                    
SITE     3 AC4 10 SER B 435  TYR B 436                                          
CRYST1  215.211   47.632   88.365  90.00 110.05  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      0.004647  0.000000  0.001696        0.00000                         
SCALE2      0.000000  0.020994  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012047        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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