GenomeNet

Database: PDB
Entry: 4KM5
LinkDB: 4KM5
Original site: 4KM5 
HEADER    TRANSFERASE                             08-MAY-13   4KM5              
TITLE     X-RAY CRYSTAL STRUCTURE OF HUMAN CYCLIC GMP-AMP SYNTHASE (CGAS)       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIC GMP-AMP SYNTHASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 157-522;                                      
COMPND   5 SYNONYM: CGAMP SYNTHASE, CGAS, H-CGAS, MAB-21 DOMAIN-CONTAINING      
COMPND   6 PROTEIN 1;                                                           
COMPND   7 EC: 2.7.7.-;                                                         
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    DNA SENSOR, INNATE IMMUNITY, ZINC FINGER, NUCLEOTIDYL TRANSFERASE,    
KEYWDS   2 DNA, CYTOPLASMIC, TRANSFERASE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.J.KRANZUSCH,A.S.Y.LEE,J.M.BERGER,J.A.DOUDNA                         
REVDAT   3   15-NOV-17 4KM5    1       REMARK                                   
REVDAT   2   12-JUN-13 4KM5    1       JRNL                                     
REVDAT   1   29-MAY-13 4KM5    0                                                
JRNL        AUTH   P.J.KRANZUSCH,A.S.LEE,J.M.BERGER,J.A.DOUDNA                  
JRNL        TITL   STRUCTURE OF HUMAN CGAS REVEALS A CONSERVED FAMILY OF        
JRNL        TITL 2 SECOND-MESSENGER ENZYMES IN INNATE IMMUNITY.                 
JRNL        REF    CELL REP                      V.   3  1362 2013              
JRNL        REFN                   ESSN 2211-1247                               
JRNL        PMID   23707061                                                     
JRNL        DOI    10.1016/J.CELREP.2013.05.008                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.45                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 15977                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.225                           
REMARK   3   R VALUE            (WORKING SET) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 800                             
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 47.4534 -  4.5390    1.00     2687   142  0.2021 0.1923        
REMARK   3     2  4.5390 -  3.6031    1.00     2541   133  0.2056 0.2211        
REMARK   3     3  3.6031 -  3.1478    1.00     2528   133  0.2497 0.3124        
REMARK   3     4  3.1478 -  2.8600    1.00     2492   133  0.2677 0.2926        
REMARK   3     5  2.8600 -  2.6551    1.00     2490   131  0.2883 0.3363        
REMARK   3     6  2.6551 -  2.4985    0.98     2439   128  0.3253 0.3693        
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)     : 0.400            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.400           
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      :  0.003           3040                                  
REMARK   3   ANGLE     :  0.661           4077                                  
REMARK   3   CHIRALITY :  0.054            439                                  
REMARK   3   PLANARITY :  0.003            519                                  
REMARK   3   DIHEDRAL  : 14.726           1177                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 161 THROUGH 199 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -10.8523  56.2856  17.4548              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5346 T22:   0.6569                                     
REMARK   3      T33:   0.9384 T12:  -0.0561                                     
REMARK   3      T13:  -0.0861 T23:   0.0799                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2623 L22:   1.8599                                     
REMARK   3      L33:   9.3960 L12:  -0.2691                                     
REMARK   3      L13:   0.8708 L23:   0.0508                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0604 S12:  -0.2343 S13:  -0.1566                       
REMARK   3      S21:  -0.4194 S22:   0.3030 S23:   0.6584                       
REMARK   3      S31:   0.0857 S32:  -1.2834 S33:  -0.3456                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 200 THROUGH 272 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   8.0406  59.6839  32.1330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6091 T22:   0.6083                                     
REMARK   3      T33:   0.6068 T12:   0.0541                                     
REMARK   3      T13:  -0.1433 T23:  -0.0035                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5100 L22:   3.1542                                     
REMARK   3      L33:   5.5269 L12:  -0.7198                                     
REMARK   3      L13:  -2.4856 L23:  -1.0968                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1384 S12:  -0.5547 S13:   0.0517                       
REMARK   3      S21:   0.2780 S22:   0.0623 S23:  -0.1616                       
REMARK   3      S31:   0.0075 S32:   0.5805 S33:  -0.0794                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 273 THROUGH 405 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   3.5028  60.3288  23.1502              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5246 T22:   0.5121                                     
REMARK   3      T33:   0.5567 T12:   0.0275                                     
REMARK   3      T13:  -0.0671 T23:  -0.0558                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9792 L22:   3.7407                                     
REMARK   3      L33:   4.0392 L12:  -0.1714                                     
REMARK   3      L13:  -0.3922 L23:  -1.5544                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0056 S12:  -0.3721 S13:  -0.1406                       
REMARK   3      S21:   0.0801 S22:   0.1629 S23:   0.0720                       
REMARK   3      S31:   0.4072 S32:   0.1245 S33:  -0.1735                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 406 THROUGH 522 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   7.9336  55.6369   3.5916              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8038 T22:   0.4135                                     
REMARK   3      T33:   0.4758 T12:   0.0485                                     
REMARK   3      T13:  -0.1317 T23:  -0.0322                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8814 L22:   3.7105                                     
REMARK   3      L33:   3.5283 L12:  -0.2803                                     
REMARK   3      L13:   0.2908 L23:   0.9257                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4278 S12:   0.4038 S13:  -0.3033                       
REMARK   3      S21:  -0.7793 S22:  -0.2090 S23:   0.0104                       
REMARK   3      S31:   0.9015 S32:   0.1756 S33:  -0.2031                       
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 4KM5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000079511.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-MAR-13; 03-FEB-13               
REMARK 200  TEMPERATURE           (KELVIN) : 77; 291                            
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : SSRL; ALS                          
REMARK 200  BEAMLINE                       : BL12-2; 8.3.1                      
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.28180; 0.97920                   
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL; CCD                         
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M; ADSC QUANTUM       
REMARK 200                                   315R                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16035                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.499                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.445                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
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) : 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; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.044M POTASSIUM CHLORIDE, 0.01M         
REMARK 280  MAGNESIUM CHLORIDE, 0.025M TRIS PH 7.0, 0.015M TRIS PH 9.0, 6.9%    
REMARK 280  PEG 6000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K, PH 7.8   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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       23.22700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       81.35000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.22700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       81.35000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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 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 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   154                                                      
REMARK 465     GLY A   155                                                      
REMARK 465     SER A   156                                                      
REMARK 465     ASP A   157                                                      
REMARK 465     ALA A   158                                                      
REMARK 465     ALA A   159                                                      
REMARK 465     PRO A   160                                                      
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   NZ   LYS A   439     O    HOH A   713              2.02            
REMARK 500   O    HOH A   712     O    HOH A   719              2.09            
REMARK 500   O    SER A   328     O    HOH A   733              2.12            
REMARK 500   OD2  ASP A   200     O    HOH A   708              2.14            
REMARK 500   O    LYS A   299     O    HOH A   734              2.14            
REMARK 500   O    HOH A   711     O    HOH A   725              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    ASN A 210     -153.14   -125.59                                   
REMARK 500    ARG A 246       -8.12     67.80                                   
REMARK 500    ARG A 255      -24.26     67.53                                   
REMARK 500    ASN A 256       75.54     51.81                                   
REMARK 500    LYS A 315      -37.43   -139.22                                   
REMARK 500    SER A 345      155.30     70.42                                   
REMARK 500    GLU A 372      -12.65     73.39                                   
REMARK 500    PHE A 516       71.35     53.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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  4KM5 A  157   522  UNP    Q8N884   CGAS_HUMAN     157    522             
SEQADV 4KM5 SER A  154  UNP  Q8N884              EXPRESSION TAG                 
SEQADV 4KM5 GLY A  155  UNP  Q8N884              EXPRESSION TAG                 
SEQADV 4KM5 SER A  156  UNP  Q8N884              EXPRESSION TAG                 
SEQRES   1 A  369  SER GLY SER ASP ALA ALA PRO GLY ALA SER LYS LEU ARG          
SEQRES   2 A  369  ALA VAL LEU GLU LYS LEU LYS LEU SER ARG ASP ASP ILE          
SEQRES   3 A  369  SER THR ALA ALA GLY MET VAL LYS GLY VAL VAL ASP HIS          
SEQRES   4 A  369  LEU LEU LEU ARG LEU LYS CYS ASP SER ALA PHE ARG GLY          
SEQRES   5 A  369  VAL GLY LEU LEU ASN THR GLY SER TYR TYR GLU HIS VAL          
SEQRES   6 A  369  LYS ILE SER ALA PRO ASN GLU PHE ASP VAL MET PHE LYS          
SEQRES   7 A  369  LEU GLU VAL PRO ARG ILE GLN LEU GLU GLU TYR SER ASN          
SEQRES   8 A  369  THR ARG ALA TYR TYR PHE VAL LYS PHE LYS ARG ASN PRO          
SEQRES   9 A  369  LYS GLU ASN PRO LEU SER GLN PHE LEU GLU GLY GLU ILE          
SEQRES  10 A  369  LEU SER ALA SER LYS MET LEU SER LYS PHE ARG LYS ILE          
SEQRES  11 A  369  ILE LYS GLU GLU ILE ASN ASP ILE LYS ASP THR ASP VAL          
SEQRES  12 A  369  ILE MET LYS ARG LYS ARG GLY GLY SER PRO ALA VAL THR          
SEQRES  13 A  369  LEU LEU ILE SER GLU LYS ILE SER VAL ASP ILE THR LEU          
SEQRES  14 A  369  ALA LEU GLU SER LYS SER SER TRP PRO ALA SER THR GLN          
SEQRES  15 A  369  GLU GLY LEU ARG ILE GLN ASN TRP LEU SER ALA LYS VAL          
SEQRES  16 A  369  ARG LYS GLN LEU ARG LEU LYS PRO PHE TYR LEU VAL PRO          
SEQRES  17 A  369  LYS HIS ALA LYS GLU GLY ASN GLY PHE GLN GLU GLU THR          
SEQRES  18 A  369  TRP ARG LEU SER PHE SER HIS ILE GLU LYS GLU ILE LEU          
SEQRES  19 A  369  ASN ASN HIS GLY LYS SER LYS THR CYS CYS GLU ASN LYS          
SEQRES  20 A  369  GLU GLU LYS CYS CYS ARG LYS ASP CYS LEU LYS LEU MET          
SEQRES  21 A  369  LYS TYR LEU LEU GLU GLN LEU LYS GLU ARG PHE LYS ASP          
SEQRES  22 A  369  LYS LYS HIS LEU ASP LYS PHE SER SER TYR HIS VAL LYS          
SEQRES  23 A  369  THR ALA PHE PHE HIS VAL CYS THR GLN ASN PRO GLN ASP          
SEQRES  24 A  369  SER GLN TRP ASP ARG LYS ASP LEU GLY LEU CYS PHE ASP          
SEQRES  25 A  369  ASN CYS VAL THR TYR PHE LEU GLN CYS LEU ARG THR GLU          
SEQRES  26 A  369  LYS LEU GLU ASN TYR PHE ILE PRO GLU PHE ASN LEU PHE          
SEQRES  27 A  369  SER SER ASN LEU ILE ASP LYS ARG SER LYS GLU PHE LEU          
SEQRES  28 A  369  THR LYS GLN ILE GLU TYR GLU ARG ASN ASN GLU PHE PRO          
SEQRES  29 A  369  VAL PHE ASP GLU PHE                                          
HET     ZN  A 601       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  HOH   *36(H2 O)                                                     
HELIX    1   1 ALA A  162  ARG A  176  1                                  15    
HELIX    2   2 ASP A  177  CYS A  199  1                                  23    
HELIX    3   3 ASN A  260  PHE A  265  5                                   6    
HELIX    4   4 SER A  272  ASP A  290  1                                  19    
HELIX    5   5 LYS A  301  SER A  305  5                                   5    
HELIX    6   6 ALA A  332  GLN A  335  5                                   4    
HELIX    7   7 GLN A  341  LEU A  344  1                                   4    
HELIX    8   8 ALA A  346  LEU A  354  1                                   9    
HELIX    9   9 SER A  380  ASN A  389  1                                  10    
HELIX   10  10 CYS A  405  PHE A  424  1                                  20    
HELIX   11  11 SER A  434  GLN A  448  1                                  15    
HELIX   12  12 ASP A  452  TRP A  455  5                                   4    
HELIX   13  13 LEU A  460  THR A  477  1                                  18    
HELIX   14  14 ASP A  497  ASN A  514  1                                  18    
SHEET    1   A 7 VAL A 206  LEU A 208  0                                        
SHEET    2   A 7 GLU A 225  GLU A 233 -1  O  LYS A 231   N  GLY A 207           
SHEET    3   A 7 ILE A 316  SER A 326  1  O  THR A 321   N  PHE A 230           
SHEET    4   A 7 PHE A 357  PRO A 361 -1  O  LEU A 359   N  LEU A 324           
SHEET    5   A 7 TRP A 375  SER A 378 -1  O  ARG A 376   N  VAL A 360           
SHEET    6   A 7 TYR A 248  PHE A 253 -1  N  TYR A 249   O  TRP A 375           
SHEET    7   A 7 ILE A 237  GLU A 241 -1  N  GLN A 238   O  LYS A 252           
SHEET    1   B 5 VAL A 206  LEU A 208  0                                        
SHEET    2   B 5 GLU A 225  GLU A 233 -1  O  LYS A 231   N  GLY A 207           
SHEET    3   B 5 ILE A 316  SER A 326  1  O  THR A 321   N  PHE A 230           
SHEET    4   B 5 VAL A 308  ILE A 312 -1  N  LEU A 310   O  VAL A 318           
SHEET    5   B 5 VAL A 296  MET A 298 -1  N  ILE A 297   O  LEU A 311           
CISPEP   1 ARG A  300    LYS A  301          0         0.64                     
CISPEP   2 GLU A  366    GLY A  367          0        -4.30                     
CISPEP   3 ASN A  368    GLY A  369          0         7.37                     
CISPEP   4 ASP A  520    GLU A  521          0         4.52                     
SITE     1 AC1  4 HIS A 390  CYS A 396  CYS A 397  CYS A 404                    
CRYST1   46.454  162.700   58.407  90.00  90.00  90.00 P 21 21 2     4          
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      0.021527  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006146  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017121        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system