GenomeNet

Database: PDB
Entry: 6MJU
LinkDB: 6MJU
Original site: 6MJU 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       22-SEP-18   6MJU              
TITLE     HUMAN CGAS CATALYTIC DOMAIN BOUND WITH THE INHIBITOR G108             
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                                                      
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 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    HUMAN CGAS, DNA SENSOR, IMMUNE SYSTEM, TRANSFERASE-TRANSFERASE        
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.LAMA,C.ADURA,W.XIE,D.TOMITA,T.KAMEI,V.KURYAVYI,T.GOGAKOS,           
AUTHOR   2 J.I.STEINBERG,M.MILLER,L.RAMOS-ESPIRITU,Y.ASANO,S.HASHIZUME,J.AIDA,  
AUTHOR   3 T.IMAEDA,R.OKAMOTO,A.J.JENNINGS,M.MICHINOM,T.KUROITA,A.STAMFORD,     
AUTHOR   4 P.GAO,P.MEINKE,J.F.GLICKMAN,D.J.PATEL,T.TUSCHL                       
REVDAT   2   05-JUN-19 6MJU    1       JRNL                                     
REVDAT   1   29-MAY-19 6MJU    0                                                
JRNL        AUTH   L.LAMA,C.ADURA,W.XIE,D.TOMITA,T.KAMEI,V.KURYAVYI,T.GOGAKOS,  
JRNL        AUTH 2 J.I.STEINBERG,M.MILLER,L.RAMOS-ESPIRITU,Y.ASANO,S.HASHIZUME, 
JRNL        AUTH 3 J.AIDA,T.IMAEDA,R.OKAMOTO,A.J.JENNINGS,M.MICHINO,T.KUROITA,  
JRNL        AUTH 4 A.STAMFORD,P.GAO,P.MEINKE,J.F.GLICKMAN,D.J.PATEL,T.TUSCHL    
JRNL        TITL   DEVELOPMENT OF HUMAN CGAS-SPECIFIC SMALL-MOLECULE INHIBITORS 
JRNL        TITL 2 FOR REPRESSION OF DSDNA-TRIGGERED INTERFERON EXPRESSION.     
JRNL        REF    NAT COMMUN                    V.  10  2261 2019              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   31113940                                                     
JRNL        DOI    10.1038/S41467-019-08620-4                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.45 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) : 2.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.43                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 17109                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.226                           
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.020                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1714                            
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 29.4271 -  5.5977    0.98     1313   154  0.1983 0.2145        
REMARK   3     2  5.5977 -  4.4480    1.00     1327   136  0.1919 0.2399        
REMARK   3     3  4.4480 -  3.8872    0.98     1281   139  0.1996 0.2298        
REMARK   3     4  3.8872 -  3.5324    1.00     1293   145  0.2194 0.2548        
REMARK   3     5  3.5324 -  3.2796    0.99     1295   145  0.2357 0.2847        
REMARK   3     6  3.2796 -  3.0865    1.00     1296   142  0.2569 0.2797        
REMARK   3     7  3.0865 -  2.9320    1.00     1284   141  0.2715 0.2847        
REMARK   3     8  2.9320 -  2.8045    0.97     1260   142  0.2794 0.3067        
REMARK   3     9  2.8045 -  2.6966    0.99     1283   143  0.2749 0.3132        
REMARK   3    10  2.6966 -  2.6036    1.00     1286   148  0.2922 0.3784        
REMARK   3    11  2.6036 -  2.5223    0.99     1272   146  0.3120 0.3927        
REMARK   3    12  2.5223 -  2.4502    0.92     1205   133  0.3157 0.3589        
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)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.110           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 61.40                          
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      :  0.002           2808                                  
REMARK   3   ANGLE     :  0.519           3764                                  
REMARK   3   CHIRALITY :  0.038            403                                  
REMARK   3   PLANARITY :  0.003            474                                  
REMARK   3   DIHEDRAL  : 16.150           1703                                  
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 6MJU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-SEP-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000236977.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-NOV-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
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-E                            
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 : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17109                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.430                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 9.700                              
REMARK 200  R MERGE                    (I) : 0.06900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.064 M SODIUM CITRATE 7.0, 0.1 M        
REMARK 280  HEPES, PH 7.0, 10% PEG5000MME, VAPOR DIFFUSION, HANGING DROP,       
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64                             
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                                                 
REMARK 290       5555   Y,-X+Y,Z+1/3                                            
REMARK 290       6555   X-Y,X,Z+2/3                                             
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       19.98567            
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       39.97133            
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        0.00000            
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       19.98567            
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       39.97133            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 16920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 726  LIES ON A SPECIAL POSITION.                          
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     SER A   151                                                      
REMARK 465     ILE A   152                                                      
REMARK 465     LEU A   153                                                      
REMARK 465     VAL A   154                                                      
REMARK 465     ARG A   155                                                      
REMARK 465     ARG A   156                                                      
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     ILE A   288                                                      
REMARK 465     ASN A   289                                                      
REMARK 465     ASP A   290                                                      
REMARK 465     ILE A   291                                                      
REMARK 465     LYS A   292                                                      
REMARK 465     ASP A   293                                                      
REMARK 465     THR A   294                                                      
REMARK 465     ASP A   295                                                      
REMARK 465     VAL A   296                                                      
REMARK 465     ILE A   297                                                      
REMARK 465     MET A   298                                                      
REMARK 465     LYS A   299                                                      
REMARK 465     ARG A   300                                                      
REMARK 465     LYS A   301                                                      
REMARK 465     ARG A   302                                                      
REMARK 465     GLY A   303                                                      
REMARK 465     LEU A   311                                                      
REMARK 465     ILE A   312                                                      
REMARK 465     SER A   313                                                      
REMARK 465     GLU A   314                                                      
REMARK 465     LYS A   315                                                      
REMARK 465     LYS A   365                                                      
REMARK 465     GLU A   366                                                      
REMARK 465     GLY A   367                                                      
REMARK 465     ASN A   368                                                      
REMARK 465     PHE A   522                                                      
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       45.04    -88.65                                   
REMARK 500    LYS A 252     -167.69   -124.59                                   
REMARK 500    GLU A 267       77.74   -118.28                                   
REMARK 500    GLU A 286       37.41    -89.41                                   
REMARK 500    SER A 345      145.92     84.29                                   
REMARK 500    PHE A 370       69.15     63.71                                   
REMARK 500    PHE A 424       46.58   -107.27                                   
REMARK 500    ASN A 449       79.53   -116.32                                   
REMARK 500    PHE A 516       76.80     60.24                                   
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 602  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 390   NE2                                                    
REMARK 620 2 CYS A 396   SG  113.6                                              
REMARK 620 3 CYS A 397   SG  103.5 131.0                                        
REMARK 620 4 CYS A 404   SG   93.7 102.2 106.2                                  
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 JUM A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 602                  
DBREF  6MJU A  152   522  UNP    Q8N884   CGAS_HUMAN     152    522             
SEQADV 6MJU SER A  151  UNP  Q8N884              EXPRESSION TAG                 
SEQADV 6MJU GLU A  427  UNP  Q8N884    LYS   427 ENGINEERED MUTATION            
SEQADV 6MJU GLU A  428  UNP  Q8N884    LYS   428 ENGINEERED MUTATION            
SEQRES   1 A  372  SER ILE LEU VAL ARG ARG ASP ALA ALA PRO GLY ALA SER          
SEQRES   2 A  372  LYS LEU ARG ALA VAL LEU GLU LYS LEU LYS LEU SER ARG          
SEQRES   3 A  372  ASP ASP ILE SER THR ALA ALA GLY MET VAL LYS GLY VAL          
SEQRES   4 A  372  VAL ASP HIS LEU LEU LEU ARG LEU LYS CYS ASP SER ALA          
SEQRES   5 A  372  PHE ARG GLY VAL GLY LEU LEU ASN THR GLY SER TYR TYR          
SEQRES   6 A  372  GLU HIS VAL LYS ILE SER ALA PRO ASN GLU PHE ASP VAL          
SEQRES   7 A  372  MET PHE LYS LEU GLU VAL PRO ARG ILE GLN LEU GLU GLU          
SEQRES   8 A  372  TYR SER ASN THR ARG ALA TYR TYR PHE VAL LYS PHE LYS          
SEQRES   9 A  372  ARG ASN PRO LYS GLU ASN PRO LEU SER GLN PHE LEU GLU          
SEQRES  10 A  372  GLY GLU ILE LEU SER ALA SER LYS MET LEU SER LYS PHE          
SEQRES  11 A  372  ARG LYS ILE ILE LYS GLU GLU ILE ASN ASP ILE LYS ASP          
SEQRES  12 A  372  THR ASP VAL ILE MET LYS ARG LYS ARG GLY GLY SER PRO          
SEQRES  13 A  372  ALA VAL THR LEU LEU ILE SER GLU LYS ILE SER VAL ASP          
SEQRES  14 A  372  ILE THR LEU ALA LEU GLU SER LYS SER SER TRP PRO ALA          
SEQRES  15 A  372  SER THR GLN GLU GLY LEU ARG ILE GLN ASN TRP LEU SER          
SEQRES  16 A  372  ALA LYS VAL ARG LYS GLN LEU ARG LEU LYS PRO PHE TYR          
SEQRES  17 A  372  LEU VAL PRO LYS HIS ALA LYS GLU GLY ASN GLY PHE GLN          
SEQRES  18 A  372  GLU GLU THR TRP ARG LEU SER PHE SER HIS ILE GLU LYS          
SEQRES  19 A  372  GLU ILE LEU ASN ASN HIS GLY LYS SER LYS THR CYS CYS          
SEQRES  20 A  372  GLU ASN LYS GLU GLU LYS CYS CYS ARG LYS ASP CYS LEU          
SEQRES  21 A  372  LYS LEU MET LYS TYR LEU LEU GLU GLN LEU LYS GLU ARG          
SEQRES  22 A  372  PHE LYS ASP GLU GLU HIS LEU ASP LYS PHE SER SER TYR          
SEQRES  23 A  372  HIS VAL LYS THR ALA PHE PHE HIS VAL CYS THR GLN ASN          
SEQRES  24 A  372  PRO GLN ASP SER GLN TRP ASP ARG LYS ASP LEU GLY LEU          
SEQRES  25 A  372  CYS PHE ASP ASN CYS VAL THR TYR PHE LEU GLN CYS LEU          
SEQRES  26 A  372  ARG THR GLU LYS LEU GLU ASN TYR PHE ILE PRO GLU PHE          
SEQRES  27 A  372  ASN LEU PHE SER SER ASN LEU ILE ASP LYS ARG SER LYS          
SEQRES  28 A  372  GLU PHE LEU THR LYS GLN ILE GLU TYR GLU ARG ASN ASN          
SEQRES  29 A  372  GLU PHE PRO VAL PHE ASP GLU PHE                              
HET    JUM  A 601      24                                                       
HET     ZN  A 602       1                                                       
HETNAM     JUM 1-[6,7-DICHLORO-9-(1H-PYRAZOL-4-YL)-1,3,4,5-TETRAHYDRO-          
HETNAM   2 JUM  2H-PYRIDO[4,3-B]INDOL-2-YL]-2-HYDROXYETHAN-1-ONE                
HETNAM      ZN ZINC ION                                                         
FORMUL   2  JUM    C16 H14 CL2 N4 O2                                            
FORMUL   3   ZN    ZN 2+                                                        
FORMUL   4  HOH   *26(H2 O)                                                     
HELIX    1 AA1 ALA A  162  LEU A  174  1                                  13    
HELIX    2 AA2 ASP A  178  LYS A  198  1                                  21    
HELIX    3 AA3 ASN A  260  GLN A  264  5                                   5    
HELIX    4 AA4 SER A  272  GLU A  286  1                                  15    
HELIX    5 AA5 PRO A  331  GLN A  335  5                                   5    
HELIX    6 AA6 SER A  345  LYS A  355  1                                  11    
HELIX    7 AA7 PHE A  379  ASN A  389  1                                  11    
HELIX    8 AA8 ASN A  399  LYS A  403  5                                   5    
HELIX    9 AA9 CYS A  405  PHE A  424  1                                  20    
HELIX   10 AB1 GLU A  427  LYS A  432  5                                   6    
HELIX   11 AB2 SER A  434  ASN A  449  1                                  16    
HELIX   12 AB3 GLN A  451  LYS A  458  5                                   8    
HELIX   13 AB4 ASP A  459  GLU A  478  1                                  20    
HELIX   14 AB5 ASP A  497  ASN A  514  1                                  18    
HELIX   15 AB6 PHE A  516  ASP A  520  5                                   5    
SHEET    1 AA1 6 GLU A 225  GLU A 233  0                                        
SHEET    2 AA1 6 SER A 317  SER A 326  1  O  SER A 317   N  PHE A 226           
SHEET    3 AA1 6 PHE A 357  PRO A 361 -1  O  LEU A 359   N  LEU A 324           
SHEET    4 AA1 6 TRP A 375  SER A 378 -1  O  ARG A 376   N  VAL A 360           
SHEET    5 AA1 6 TYR A 248  PHE A 253 -1  N  TYR A 249   O  TRP A 375           
SHEET    6 AA1 6 ILE A 237  GLU A 241 -1  N  GLN A 238   O  LYS A 252           
SHEET    1 AA2 3 GLU A 225  GLU A 233  0                                        
SHEET    2 AA2 3 SER A 317  SER A 326  1  O  SER A 317   N  PHE A 226           
SHEET    3 AA2 3 ALA A 307  LEU A 310 -1  N  VAL A 308   O  ILE A 320           
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 602     1555   1555  2.06  
LINK         SG  CYS A 396                ZN    ZN A 602     1555   1555  2.29  
LINK         SG  CYS A 397                ZN    ZN A 602     1555   1555  2.28  
LINK         SG  CYS A 404                ZN    ZN A 602     1555   1555  2.29  
SITE     1 AC1 10 LYS A 362  ARG A 376  LEU A 377  SER A 434                    
SITE     2 AC1 10 TYR A 436  HIS A 437  ASN A 482  LEU A 490                    
SITE     3 AC1 10 HOH A 703  HOH A 706                                          
SITE     1 AC2  4 HIS A 390  CYS A 396  CYS A 397  CYS A 404                    
CRYST1  116.989  116.989   59.957  90.00  90.00 120.00 P 64          6          
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      0.008548  0.004935  0.000000        0.00000                         
SCALE2      0.000000  0.009870  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016679        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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