GenomeNet

Database: PDB
Entry: 6EDC
LinkDB: 6EDC
Original site: 6EDC 
HEADER    TRANSFERASE/DNA                         09-AUG-18   6EDC              
TITLE     HCGAS-16BP DSDNA COMPLEX                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIC GMP-AMP SYNTHASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: H-CGAS,2'3'-CGAMP SYNTHASE,MAB-21 DOMAIN-CONTAINING PROTEIN 
COMPND   5 1;                                                                   
COMPND   6 EC: 2.7.7.86;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: DNA (5'-                                                   
COMPND  11 D(*AP*AP*AP*TP*TP*GP*CP*CP*GP*AP*AP*GP*AP*CP*GP*AP*A)-3');           
COMPND  12 CHAIN: B;                                                            
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: DNA (5'-D(*TP*TP*CP*GP*TP*CP*TP*TP*CP*GP*GP*CP*AP*AP*T)-   
COMPND  16 3');                                                                 
COMPND  17 CHAIN: C;                                                            
COMPND  18 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: CGAS, C6ORF150, MB21D1;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 MOL_ID: 3;                                                           
SOURCE  13 SYNTHETIC: YES;                                                      
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_TAXID: 9606                                                 
KEYWDS    HUMAN CGAS DNA COMPLEX, TRANSFERASE-DNA COMPLEX                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.XIE,L.LAMA,C.ADURA,J.F.GLICKMAN,T.TUSCHL,D.J.PATEL                  
REVDAT   3   26-JUN-19 6EDC    1       JRNL                                     
REVDAT   2   12-JUN-19 6EDC    1       JRNL                                     
REVDAT   1   29-MAY-19 6EDC    0                                                
JRNL        AUTH   W.XIE,L.LAMA,C.ADURA,D.TOMITA,J.F.GLICKMAN,T.TUSCHL,         
JRNL        AUTH 2 D.J.PATEL                                                    
JRNL        TITL   HUMAN CGAS CATALYTIC DOMAIN HAS AN ADDITIONAL DNA-BINDING    
JRNL        TITL 2 INTERFACE THAT ENHANCES ENZYMATIC ACTIVITY AND LIQUID-PHASE  
JRNL        TITL 3 CONDENSATION.                                                
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 116 11946 2019              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   31142647                                                     
JRNL        DOI    10.1073/PNAS.1905013116                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.71 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.71                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 86.44                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 19571                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.241                           
REMARK   3   R VALUE            (WORKING SET) : 0.239                           
REMARK   3   FREE R VALUE                     : 0.278                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.930                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 964                             
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 86.4845 -  5.1880    0.98     2869   143  0.2184 0.2547        
REMARK   3     2  5.1880 -  4.1179    0.99     2707   138  0.2011 0.2373        
REMARK   3     3  4.1179 -  3.5974    0.99     2664   131  0.2333 0.2641        
REMARK   3     4  3.5974 -  3.2684    0.99     2631   160  0.2629 0.3203        
REMARK   3     5  3.2684 -  3.0342    1.00     2641   123  0.2903 0.2901        
REMARK   3     6  3.0342 -  2.8553    1.00     2625   143  0.3191 0.3951        
REMARK   3     7  2.8553 -  2.7123    0.94     2470   126  0.3295 0.3685        
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) : 28.560           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.004           3635                                  
REMARK   3   ANGLE     :  0.509           5014                                  
REMARK   3   CHIRALITY :  0.035            551                                  
REMARK   3   PLANARITY :  0.003            524                                  
REMARK   3   DIHEDRAL  : 19.800           2094                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6EDC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-AUG-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000236116.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-JUL-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19571                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.710                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 86.441                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 12.00                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.71                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: PHASER                                                
REMARK 200 STARTING MODEL: 4K96                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NACL, 0.1 M HEPES, PH 7.5, AND     
REMARK 280  28% PEG400 (V/V), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       79.54800            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      159.09600            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      119.32200            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      198.87000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       39.77400            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       79.54800            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      159.09600            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      198.87000            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      119.32200            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       39.77400            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3230 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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     ASP A   157                                                      
REMARK 465     ALA A   158                                                      
REMARK 465     ALA A   159                                                      
REMARK 465     PRO A   160                                                      
REMARK 465     ARG A   255                                                      
REMARK 465     ASN A   256                                                      
REMARK 465     PRO A   257                                                      
REMARK 465     LYS A   258                                                      
REMARK 465     GLU A   259                                                      
REMARK 465     LYS A   292                                                      
REMARK 465     ASP A   293                                                      
REMARK 465     THR A   294                                                      
REMARK 465     LYS A   365                                                      
REMARK 465     GLU A   366                                                      
REMARK 465     GLY A   367                                                      
REMARK 465     ASN A   368                                                      
REMARK 465     GLY A   369                                                      
REMARK 465     PHE A   370                                                      
REMARK 465     PHE A   522                                                      
REMARK 465      DT C     1                                                      
REMARK 465      DT C    17                                                      
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      DA B   1    O5'                                                 
REMARK 470      DT C   2    P    OP1  OP2  O5'                                  
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   NH2  ARG A   476     OE2  GLU A   509              2.16            
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       55.33   -108.61                                   
REMARK 500    VAL A 218       15.55   -140.78                                   
REMARK 500    SER A 221      -23.45   -150.96                                   
REMARK 500    SER A 243     -133.70     52.87                                   
REMARK 500    ARG A 246      -20.94     67.25                                   
REMARK 500    GLU A 299     -176.69   -179.60                                   
REMARK 500    PRO A 306       93.79    -63.88                                   
REMARK 500    GLU A 314       53.55     33.02                                   
REMARK 500    LYS A 315      -42.38   -148.22                                   
REMARK 500    TRP A 343      -77.34    -96.71                                   
REMARK 500    ASN A 389       55.46   -147.91                                   
REMARK 500    ASP A 459       38.12    -97.47                                   
REMARK 500    PHE A 516       78.03     55.69                                   
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  102.1                                              
REMARK 620 3 CYS A 397   SG   86.3 134.0                                        
REMARK 620 4 CYS A 404   SG   80.9 122.0 103.9                                  
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                  
DBREF  6EDC A  157   522  UNP    Q8N884   CGAS_HUMAN     157    522             
DBREF  6EDC B    1    17  PDB    6EDC     6EDC             1     17             
DBREF  6EDC C    1    17  PDB    6EDC     6EDC             1     17             
SEQADV 6EDC GLU A  299  UNP  Q8N884    LYS   299 ENGINEERED MUTATION            
SEQADV 6EDC ALA A  300  UNP  Q8N884    ARG   300 ENGINEERED MUTATION            
SEQADV 6EDC GLU A  301  UNP  Q8N884    LYS   301 ENGINEERED MUTATION            
SEQRES   1 A  366  ASP ALA ALA PRO GLY ALA SER LYS LEU ARG ALA VAL LEU          
SEQRES   2 A  366  GLU LYS LEU LYS LEU SER ARG ASP ASP ILE SER THR ALA          
SEQRES   3 A  366  ALA GLY MET VAL LYS GLY VAL VAL ASP HIS LEU LEU LEU          
SEQRES   4 A  366  ARG LEU LYS CYS ASP SER ALA PHE ARG GLY VAL GLY LEU          
SEQRES   5 A  366  LEU ASN THR GLY SER TYR TYR GLU HIS VAL LYS ILE SER          
SEQRES   6 A  366  ALA PRO ASN GLU PHE ASP VAL MET PHE LYS LEU GLU VAL          
SEQRES   7 A  366  PRO ARG ILE GLN LEU GLU GLU TYR SER ASN THR ARG ALA          
SEQRES   8 A  366  TYR TYR PHE VAL LYS PHE LYS ARG ASN PRO LYS GLU ASN          
SEQRES   9 A  366  PRO LEU SER GLN PHE LEU GLU GLY GLU ILE LEU SER ALA          
SEQRES  10 A  366  SER LYS MET LEU SER LYS PHE ARG LYS ILE ILE LYS GLU          
SEQRES  11 A  366  GLU ILE ASN ASP ILE LYS ASP THR ASP VAL ILE MET GLU          
SEQRES  12 A  366  ALA GLU ARG GLY GLY SER PRO ALA VAL THR LEU LEU ILE          
SEQRES  13 A  366  SER GLU LYS ILE SER VAL ASP ILE THR LEU ALA LEU GLU          
SEQRES  14 A  366  SER LYS SER SER TRP PRO ALA SER THR GLN GLU GLY LEU          
SEQRES  15 A  366  ARG ILE GLN ASN TRP LEU SER ALA LYS VAL ARG LYS GLN          
SEQRES  16 A  366  LEU ARG LEU LYS PRO PHE TYR LEU VAL PRO LYS HIS ALA          
SEQRES  17 A  366  LYS GLU GLY ASN GLY PHE GLN GLU GLU THR TRP ARG LEU          
SEQRES  18 A  366  SER PHE SER HIS ILE GLU LYS GLU ILE LEU ASN ASN HIS          
SEQRES  19 A  366  GLY LYS SER LYS THR CYS CYS GLU ASN LYS GLU GLU LYS          
SEQRES  20 A  366  CYS CYS ARG LYS ASP CYS LEU LYS LEU MET LYS TYR LEU          
SEQRES  21 A  366  LEU GLU GLN LEU LYS GLU ARG PHE LYS ASP LYS LYS HIS          
SEQRES  22 A  366  LEU ASP LYS PHE SER SER TYR HIS VAL LYS THR ALA PHE          
SEQRES  23 A  366  PHE HIS VAL CYS THR GLN ASN PRO GLN ASP SER GLN TRP          
SEQRES  24 A  366  ASP ARG LYS ASP LEU GLY LEU CYS PHE ASP ASN CYS VAL          
SEQRES  25 A  366  THR TYR PHE LEU GLN CYS LEU ARG THR GLU LYS LEU GLU          
SEQRES  26 A  366  ASN TYR PHE ILE PRO GLU PHE ASN LEU PHE SER SER ASN          
SEQRES  27 A  366  LEU ILE ASP LYS ARG SER LYS GLU PHE LEU THR LYS GLN          
SEQRES  28 A  366  ILE GLU TYR GLU ARG ASN ASN GLU PHE PRO VAL PHE ASP          
SEQRES  29 A  366  GLU PHE                                                      
SEQRES   1 B   17   DA  DA  DA  DT  DT  DG  DC  DC  DG  DA  DA  DG  DA          
SEQRES   2 B   17   DC  DG  DA  DA                                              
SEQRES   1 C   17   DT  DT  DT  DC  DG  DT  DC  DT  DT  DC  DG  DG  DC          
SEQRES   2 C   17   DA  DA  DT  DT                                              
HET     ZN  A 601       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   4   ZN    ZN 2+                                                        
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 GLY A  212  GLU A  216  1                                   5    
HELIX    4 AA4 LEU A  262  GLN A  264  5                                   3    
HELIX    5 AA5 SER A  272  ASP A  290  1                                  19    
HELIX    6 AA6 PRO A  331  GLN A  335  5                                   5    
HELIX    7 AA7 SER A  345  LYS A  355  1                                  11    
HELIX    8 AA8 PHE A  379  ASN A  388  1                                  10    
HELIX    9 AA9 ASN A  399  LYS A  403  5                                   5    
HELIX   10 AB1 CYS A  405  PHE A  424  1                                  20    
HELIX   11 AB2 SER A  434  ASN A  449  1                                  16    
HELIX   12 AB3 GLN A  451  LYS A  458  5                                   8    
HELIX   13 AB4 ASP A  459  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    
SHEET    1 AA1 7 VAL A 206  THR A 211  0                                        
SHEET    2 AA1 7 GLU A 225  GLU A 233 -1  O  LYS A 231   N  GLY A 207           
SHEET    3 AA1 7 ILE A 316  SER A 326  1  O  GLU A 325   N  LEU A 232           
SHEET    4 AA1 7 PHE A 357  PRO A 361 -1  O  LEU A 359   N  LEU A 324           
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  GLU A 240   O  PHE A 250           
SHEET    1 AA2 5 VAL A 206  THR A 211  0                                        
SHEET    2 AA2 5 GLU A 225  GLU A 233 -1  O  LYS A 231   N  GLY A 207           
SHEET    3 AA2 5 ILE A 316  SER A 326  1  O  GLU A 325   N  LEU A 232           
SHEET    4 AA2 5 VAL A 308  ILE A 312 -1  N  LEU A 310   O  VAL A 318           
SHEET    5 AA2 5 VAL A 296  GLU A 299 -1  N  GLU A 299   O  THR A 309           
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           
LINK         NE2 HIS A 390                ZN    ZN A 601     1555   1555  2.02  
LINK         SG  CYS A 396                ZN    ZN A 601     1555   1555  2.29  
LINK         SG  CYS A 397                ZN    ZN A 601     1555   1555  2.27  
LINK         SG  CYS A 404                ZN    ZN A 601     1555   1555  2.25  
SITE     1 AC1  4 HIS A 390  CYS A 396  CYS A 397  CYS A 404                    
CRYST1   99.813   99.813  238.644  90.00  90.00 120.00 P 61 2 2     12          
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      0.010019  0.005784  0.000000        0.00000                         
SCALE2      0.000000  0.011569  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004190        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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