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Database: PDB
Entry: 4O69
LinkDB: 4O69
Original site: 4O69 
HEADER    TRANSFERASE                             20-DEC-13   4O69              
TITLE     HUMAN CYCLIC GMP-AMP SYNTHASE (CGAS) IN COMPLEX WITH SULFATE ION      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIC GMP-AMP SYNTHASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CGAMP SYNTHASE, CGAS, H-CGAS, MAB-21 DOMAIN-CONTAINING      
COMPND   5 PROTEIN 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: MB21D1, C6ORF150;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    IMMUNE RESPONSE, TRANSFERASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.ZHANG,Z.CHEN,X.W.ZHANG,Z.J.CHEN                                     
REVDAT   2   05-MAR-14 4O69    1       JRNL                                     
REVDAT   1   05-FEB-14 4O69    0                                                
JRNL        AUTH   X.ZHANG,J.WU,F.DU,H.XU,L.SUN,Z.CHEN,C.A.BRAUTIGAM,X.ZHANG,   
JRNL        AUTH 2 Z.J.CHEN                                                     
JRNL        TITL   THE CYTOSOLIC DNA SENSOR CGAS FORMS AN OLIGOMERIC COMPLEX    
JRNL        TITL 2 WITH DNA AND UNDERGOES SWITCH-LIKE CONFORMATIONAL CHANGES IN 
JRNL        TITL 3 THE ACTIVATION LOOP.                                         
JRNL        REF    CELL REP                      V.   6   421 2014              
JRNL        REFN                   ESSN 2211-1247                               
JRNL        PMID   24462292                                                     
JRNL        DOI    10.1016/J.CELREP.2014.01.003                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.07                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 35012                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.224                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1755                            
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 33.0724 -  5.2890    0.98     2785   146  0.2063 0.2514        
REMARK   3     2  5.2890 -  4.2008    1.00     2648   140  0.1569 0.1806        
REMARK   3     3  4.2008 -  3.6706    1.00     2614   137  0.1609 0.1534        
REMARK   3     4  3.6706 -  3.3353    1.00     2585   136  0.1816 0.2245        
REMARK   3     5  3.3353 -  3.0964    0.99     2574   135  0.1969 0.2630        
REMARK   3     6  3.0964 -  2.9140    0.99     2530   133  0.1998 0.2493        
REMARK   3     7  2.9140 -  2.7681    0.99     2539   135  0.2032 0.2380        
REMARK   3     8  2.7681 -  2.6477    0.99     2506   132  0.2066 0.2701        
REMARK   3     9  2.6477 -  2.5458    0.99     2515   133  0.2045 0.2369        
REMARK   3    10  2.5458 -  2.4580    0.99     2506   133  0.2144 0.2584        
REMARK   3    11  2.4580 -  2.3811    0.99     2506   132  0.2299 0.2818        
REMARK   3    12  2.3811 -  2.3131    0.99     2488   133  0.2346 0.2578        
REMARK   3    13  2.3131 -  2.2522    0.99     2461   130  0.2756 0.3206        
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)     : 0.270            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.420           
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      :  0.008           2984                                  
REMARK   3   ANGLE     :  1.064           3999                                  
REMARK   3   CHIRALITY :  0.070            433                                  
REMARK   3   PLANARITY :  0.004            500                                  
REMARK   3   DIHEDRAL  : 15.878           1151                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resid 160 through 248 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  22.0199 -38.7649  -0.9455              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3830 T22:   0.6707                                     
REMARK   3      T33:   0.5173 T12:   0.0266                                     
REMARK   3      T13:   0.0171 T23:   0.0553                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2444 L22:   1.4814                                     
REMARK   3      L33:   1.4982 L12:   2.4980                                     
REMARK   3      L13:   0.0593 L23:   0.2351                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0319 S12:   0.1745 S13:   0.3054                       
REMARK   3      S21:  -0.0249 S22:  -0.0097 S23:   0.2402                       
REMARK   3      S31:  -0.1451 S32:  -0.1629 S33:   0.0399                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resid 249 through 405 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  22.7866 -47.6538   0.6274              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2527 T22:   0.5094                                     
REMARK   3      T33:   0.3519 T12:   0.0118                                     
REMARK   3      T13:   0.0110 T23:  -0.0123                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5451 L22:   1.2084                                     
REMARK   3      L33:   3.7015 L12:   0.5248                                     
REMARK   3      L13:   1.2880 L23:   0.5643                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0557 S12:   0.5932 S13:  -0.3248                       
REMARK   3      S21:  -0.0409 S22:   0.0255 S23:   0.2648                       
REMARK   3      S31:   0.1169 S32:  -0.3162 S33:  -0.1173                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resid 406 through 521 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  42.0283 -36.6730  -7.0699              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2570 T22:   0.5637                                     
REMARK   3      T33:   0.3166 T12:   0.0066                                     
REMARK   3      T13:   0.0164 T23:  -0.0442                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1885 L22:   4.3496                                     
REMARK   3      L33:   5.8721 L12:   0.8504                                     
REMARK   3      L13:  -0.6232 L23:  -1.1108                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0723 S12:   0.5021 S13:  -0.0397                       
REMARK   3      S21:  -0.6858 S22:   0.1834 S23:  -0.0543                       
REMARK   3      S31:  -0.1419 S32:   0.0868 S33:  -0.1001                       
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 4O69 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB084094.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97921                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35060                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
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) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.29                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
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: PHASES                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.57                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M (NH4)2SO4, 0.1 M BIS-TRIS, PH 5.5,   
REMARK 280  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       80.44367            
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      160.88733            
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      120.66550            
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      201.10917            
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       40.22183            
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       80.44367            
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      160.88733            
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      201.10917            
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      120.66550            
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       40.22183            
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 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     LYS A   292                                                      
REMARK 465     ASP A   293                                                      
REMARK 465     GLY A   304                                                      
REMARK 465     SER A   305                                                      
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 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   OD1  ASN A   210     O    HOH A   805              2.08            
REMARK 500   O    HOH A   840     O    HOH A   843              2.12            
REMARK 500   O    HOH A   794     O    HOH A   797              2.15            
REMARK 500   O    HOH A   819     O    HOH A   863              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 243     -132.97     57.33                                   
REMARK 500    ASN A 256       72.82   -117.75                                   
REMARK 500    GLU A 314       16.82     58.49                                   
REMARK 500    LYS A 315      -47.96   -137.07                                   
REMARK 500    TRP A 343      -77.03   -111.22                                   
REMARK 500    LYS A 362      118.77   -161.78                                   
REMARK 500    ALA A 364     -165.36   -117.62                                   
REMARK 500    ASN A 389       72.78   -152.26                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 390   NE2                                                    
REMARK 620 2 CYS A 396   SG  114.8                                              
REMARK 620 3 CYS A 397   SG  107.4 130.6                                        
REMARK 620 4 CYS A 404   SG   95.8  96.5 103.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 604                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4O67   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4O68   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4O6A   RELATED DB: PDB                                   
DBREF  4O69 A  161   522  UNP    Q8N884   CGAS_HUMAN     161    522             
SEQADV 4O69 MET A  160  UNP  Q8N884              EXPRESSION TAG                 
SEQRES   1 A  363  MET GLY ALA SER LYS LEU ARG ALA VAL LEU GLU LYS LEU          
SEQRES   2 A  363  LYS LEU SER ARG ASP ASP ILE SER THR ALA ALA GLY MET          
SEQRES   3 A  363  VAL LYS GLY VAL VAL ASP HIS LEU LEU LEU ARG LEU LYS          
SEQRES   4 A  363  CYS ASP SER ALA PHE ARG GLY VAL GLY LEU LEU ASN THR          
SEQRES   5 A  363  GLY SER TYR TYR GLU HIS VAL LYS ILE SER ALA PRO ASN          
SEQRES   6 A  363  GLU PHE ASP VAL MET PHE LYS LEU GLU VAL PRO ARG ILE          
SEQRES   7 A  363  GLN LEU GLU GLU TYR SER ASN THR ARG ALA TYR TYR PHE          
SEQRES   8 A  363  VAL LYS PHE LYS ARG ASN PRO LYS GLU ASN PRO LEU SER          
SEQRES   9 A  363  GLN PHE LEU GLU GLY GLU ILE LEU SER ALA SER LYS MET          
SEQRES  10 A  363  LEU SER LYS PHE ARG LYS ILE ILE LYS GLU GLU ILE ASN          
SEQRES  11 A  363  ASP ILE LYS ASP THR ASP VAL ILE MET LYS ARG LYS ARG          
SEQRES  12 A  363  GLY GLY SER PRO ALA VAL THR LEU LEU ILE SER GLU LYS          
SEQRES  13 A  363  ILE SER VAL ASP ILE THR LEU ALA LEU GLU SER LYS SER          
SEQRES  14 A  363  SER TRP PRO ALA SER THR GLN GLU GLY LEU ARG ILE GLN          
SEQRES  15 A  363  ASN TRP LEU SER ALA LYS VAL ARG LYS GLN LEU ARG LEU          
SEQRES  16 A  363  LYS PRO PHE TYR LEU VAL PRO LYS HIS ALA LYS GLU GLY          
SEQRES  17 A  363  ASN GLY PHE GLN GLU GLU THR TRP ARG LEU SER PHE SER          
SEQRES  18 A  363  HIS ILE GLU LYS GLU ILE LEU ASN ASN HIS GLY LYS SER          
SEQRES  19 A  363  LYS THR CYS CYS GLU ASN LYS GLU GLU LYS CYS CYS ARG          
SEQRES  20 A  363  LYS ASP CYS LEU LYS LEU MET LYS TYR LEU LEU GLU GLN          
SEQRES  21 A  363  LEU LYS GLU ARG PHE LYS ASP LYS LYS HIS LEU ASP LYS          
SEQRES  22 A  363  PHE SER SER TYR HIS VAL LYS THR ALA PHE PHE HIS VAL          
SEQRES  23 A  363  CYS THR GLN ASN PRO GLN ASP SER GLN TRP ASP ARG LYS          
SEQRES  24 A  363  ASP LEU GLY LEU CYS PHE ASP ASN CYS VAL THR TYR PHE          
SEQRES  25 A  363  LEU GLN CYS LEU ARG THR GLU LYS LEU GLU ASN TYR PHE          
SEQRES  26 A  363  ILE PRO GLU PHE ASN LEU PHE SER SER ASN LEU ILE ASP          
SEQRES  27 A  363  LYS ARG SER LYS GLU PHE LEU THR LYS GLN ILE GLU TYR          
SEQRES  28 A  363  GLU ARG ASN ASN GLU PHE PRO VAL PHE ASP GLU PHE              
HET     ZN  A 601       1                                                       
HET    SO4  A 602       5                                                       
HET    SO4  A 603       5                                                       
HET    SO4  A 604       5                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  SO4    3(O4 S 2-)                                                   
FORMUL   6  HOH   *169(H2 O)                                                    
HELIX    1   1 GLY A  161  LEU A  174  1                                  14    
HELIX    2   2 SER A  175  CYS A  199  1                                  25    
HELIX    3   3 ASN A  260  GLN A  264  5                                   5    
HELIX    4   4 SER A  272  ILE A  291  1                                  20    
HELIX    5   5 PRO A  331  GLN A  335  5                                   5    
HELIX    6   6 SER A  345  LEU A  354  1                                  10    
HELIX    7   7 PHE A  379  ASN A  388  1                                  10    
HELIX    8   8 ASN A  399  LYS A  403  5                                   5    
HELIX    9   9 CYS A  405  PHE A  424  1                                  20    
HELIX   10  10 SER A  434  ASN A  449  1                                  16    
HELIX   11  11 GLN A  451  LYS A  458  5                                   8    
HELIX   12  12 ASP A  459  GLU A  478  1                                  20    
HELIX   13  13 ASP A  497  ASN A  514  1                                  18    
HELIX   14  14 GLU A  515  ASP A  520  5                                   6    
SHEET    1   A 7 VAL A 206  LEU A 209  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  GLU A 240   O  PHE A 250           
SHEET    1   B 5 VAL A 206  LEU A 209  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  ILE A 312   O  ILE A 316           
SHEET    5   B 5 VAL A 296  MET A 298 -1  N  ILE A 297   O  LEU A 311           
SHEET    1   C 2 LEU A 266  GLU A 267  0                                        
SHEET    2   C 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  2.07  
LINK         SG  CYS A 396                ZN    ZN A 601     1555   1555  2.28  
LINK         SG  CYS A 397                ZN    ZN A 601     1555   1555  2.34  
LINK         SG  CYS A 404                ZN    ZN A 601     1555   1555  2.45  
SITE     1 AC1  4 HIS A 390  CYS A 396  CYS A 397  CYS A 404                    
SITE     1 AC2  5 SER A 213  LYS A 414  SER A 435  HOH A 813                    
SITE     2 AC2  5 HOH A 842                                                     
SITE     1 AC3  7 LEU A 387  ASN A 388  HIS A 390  LYS A 407                    
SITE     2 AC3  7 HOH A 723  HOH A 755  HOH A 776                               
SITE     1 AC4  2 LYS A 362  ARG A 376                                          
CRYST1  101.027  101.027  241.331  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      0.009898  0.005715  0.000000        0.00000                         
SCALE2      0.000000  0.011430  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004144        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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