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Database: PDB
Entry: 4LEV
LinkDB: 4LEV
Original site: 4LEV 
HEADER    TRANSFERASE                             26-JUN-13   4LEV              
TITLE     STRUCTURE OF HUMAN CGAS                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIC GMP-AMP SYNTHASE;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: HUMAN CGAS CATALYTIC DOMAIN, 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    NTASE, DNA SENSOR, TRANSFERASE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.LI                                                                  
REVDAT   2   08-JAN-14 4LEV    1       JRNL                                     
REVDAT   1   25-DEC-13 4LEV    0                                                
JRNL        AUTH   X.LI,C.SHU,G.YI,C.T.CHATON,C.L.SHELTON,J.DIAO,X.ZUO,C.C.KAO, 
JRNL        AUTH 2 A.B.HERR,P.LI                                                
JRNL        TITL   CYCLIC GMP-AMP SYNTHASE IS ACTIVATED BY DOUBLE-STRANDED      
JRNL        TITL 2 DNA-INDUCED OLIGOMERIZATION.                                 
JRNL        REF    IMMUNITY                      V.  39  1019 2013              
JRNL        REFN                   ISSN 1074-7613                               
JRNL        PMID   24332030                                                     
JRNL        DOI    10.1016/J.IMMUNI.2013.10.019                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 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) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.45                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 111235                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.168                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.202                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.480                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3876                            
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 38.4555 -  5.9192    0.98     3829   148  0.1719 0.2042        
REMARK   3     2  5.9192 -  4.7009    0.99     3864   139  0.1589 0.1693        
REMARK   3     3  4.7009 -  4.1075    1.00     3956   142  0.1423 0.1644        
REMARK   3     4  4.1075 -  3.7323    1.00     3899   145  0.1473 0.1702        
REMARK   3     5  3.7323 -  3.4649    1.00     3914   136  0.1526 0.2100        
REMARK   3     6  3.4649 -  3.2608    1.00     3989   144  0.1696 0.2359        
REMARK   3     7  3.2608 -  3.0975    1.00     3835   136  0.1812 0.2060        
REMARK   3     8  3.0975 -  2.9628    1.00     3899   144  0.1701 0.2188        
REMARK   3     9  2.9628 -  2.8487    1.00     3947   135  0.1709 0.1978        
REMARK   3    10  2.8487 -  2.7505    1.00     3887   141  0.1708 0.2130        
REMARK   3    11  2.7505 -  2.6645    1.00     3891   144  0.1687 0.1946        
REMARK   3    12  2.6645 -  2.5883    1.00     3995   144  0.1598 0.1875        
REMARK   3    13  2.5883 -  2.5202    1.00     3879   138  0.1577 0.2059        
REMARK   3    14  2.5202 -  2.4587    1.00     3936   145  0.1608 0.2035        
REMARK   3    15  2.4587 -  2.4029    1.00     3910   135  0.1631 0.1942        
REMARK   3    16  2.4029 -  2.3517    1.00     3888   134  0.1660 0.2143        
REMARK   3    17  2.3517 -  2.3047    0.99     3872   139  0.1694 0.2416        
REMARK   3    18  2.3047 -  2.2612    0.99     3909   151  0.1741 0.1794        
REMARK   3    19  2.2612 -  2.2208    0.99     3886   135  0.1659 0.2043        
REMARK   3    20  2.2208 -  2.1832    1.00     3896   137  0.1688 0.2423        
REMARK   3    21  2.1832 -  2.1480    1.00     3922   146  0.1780 0.2402        
REMARK   3    22  2.1480 -  2.1149    0.99     3893   146  0.1925 0.2428        
REMARK   3    23  2.1149 -  2.0838    0.99     3848   138  0.1909 0.2237        
REMARK   3    24  2.0838 -  2.0545    0.99     3898   145  0.1985 0.2104        
REMARK   3    25  2.0545 -  2.0267    0.97     3742   137  0.2105 0.2154        
REMARK   3    26  2.0267 -  2.0004    0.92     3631   127  0.2377 0.2446        
REMARK   3    27  2.0004 -  1.9754    0.86     3343   118  0.2448 0.2739        
REMARK   3    28  1.9754 -  1.9516    0.75     3001   107  0.2695 0.2896        
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)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.640           
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      :  0.010           6244                                  
REMARK   3   ANGLE     :  1.338           8385                                  
REMARK   3   CHIRALITY :  0.091            901                                  
REMARK   3   PLANARITY :  0.007           1072                                  
REMARK   3   DIHEDRAL  : 15.027           2419                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resid 154 through 179 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 155.4847  24.7763  19.1948              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5521 T22:   0.2625                                     
REMARK   3      T33:   0.5268 T12:   0.0052                                     
REMARK   3      T13:   0.0372 T23:  -0.0722                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2527 L22:   4.6119                                     
REMARK   3      L33:   6.2951 L12:   0.0758                                     
REMARK   3      L13:   0.6179 L23:   0.1918                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3060 S12:  -0.4836 S13:   0.8585                       
REMARK   3      S21:   0.7952 S22:  -0.0708 S23:  -0.3785                       
REMARK   3      S31:  -1.2722 S32:  -0.2766 S33:   0.3254                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resid 180 through 253 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 130.4688  11.6515   1.6862              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3125 T22:   0.4266                                     
REMARK   3      T33:   0.3472 T12:  -0.0008                                     
REMARK   3      T13:  -0.0852 T23:  -0.0237                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0437 L22:   1.6918                                     
REMARK   3      L33:   2.0300 L12:  -0.3037                                     
REMARK   3      L13:  -0.4556 L23:  -1.0711                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1161 S12:   0.2630 S13:   0.3220                       
REMARK   3      S21:   0.0759 S22:   0.0677 S23:   0.3038                       
REMARK   3      S31:  -0.0280 S32:  -0.2399 S33:  -0.1942                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resid 254 through 326 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 130.0162  10.9077  -7.7415              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4570 T22:   0.5666                                     
REMARK   3      T33:   0.3424 T12:  -0.0755                                     
REMARK   3      T13:  -0.1037 T23:   0.0166                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8611 L22:   3.7171                                     
REMARK   3      L33:   2.4039 L12:   0.5688                                     
REMARK   3      L13:   0.7006 L23:  -0.4163                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2367 S12:   0.6864 S13:   0.1733                       
REMARK   3      S21:  -0.8572 S22:   0.3016 S23:   0.2688                       
REMARK   3      S31:   0.2268 S32:  -0.2594 S33:  -0.0034                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resid 327 through 405 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 135.0257   5.7939  16.3370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1616 T22:   0.1895                                     
REMARK   3      T33:   0.1460 T12:  -0.0156                                     
REMARK   3      T13:   0.0164 T23:  -0.0182                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7447 L22:   1.5632                                     
REMARK   3      L33:   1.6127 L12:   0.2924                                     
REMARK   3      L13:   0.5989 L23:   0.5042                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0260 S12:   0.2173 S13:  -0.1377                       
REMARK   3      S21:  -0.1502 S22:   0.0858 S23:   0.0267                       
REMARK   3      S31:   0.0752 S32:   0.0288 S33:  -0.0461                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'A' and (resid 406 through 522 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 153.4694   6.2320  13.5650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2366 T22:   0.1940                                     
REMARK   3      T33:   0.1678 T12:  -0.0156                                     
REMARK   3      T13:   0.0160 T23:  -0.0076                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6829 L22:   1.2133                                     
REMARK   3      L33:   1.5416 L12:  -0.3034                                     
REMARK   3      L13:  -0.4979 L23:  -0.0288                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0161 S12:   0.2882 S13:   0.0299                       
REMARK   3      S21:  -0.2012 S22:  -0.0049 S23:  -0.0471                       
REMARK   3      S31:  -0.0502 S32:   0.0563 S33:   0.0265                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'B' and (resid 154 through 178 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 122.0146   2.8651  53.2775              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5156 T22:   0.2370                                     
REMARK   3      T33:   0.4798 T12:   0.0296                                     
REMARK   3      T13:  -0.0007 T23:   0.0441                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.6724 L22:   3.9039                                     
REMARK   3      L33:   4.1537 L12:   0.0624                                     
REMARK   3      L13:   1.3926 L23:   0.5656                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4317 S12:   0.5141 S13:  -1.0507                       
REMARK   3      S21:   0.4529 S22:  -0.2358 S23:  -0.5624                       
REMARK   3      S31:   0.6455 S32:   0.6825 S33:  -0.0860                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'B' and (resid 179 through 248 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 104.7868  13.2326  27.9242              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4952 T22:   0.5870                                     
REMARK   3      T33:   0.4626 T12:   0.0546                                     
REMARK   3      T13:  -0.1709 T23:  -0.0804                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0942 L22:   1.4987                                     
REMARK   3      L33:   1.3430 L12:   0.5162                                     
REMARK   3      L13:   0.1483 L23:   1.1865                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1180 S12:   0.2485 S13:  -0.1181                       
REMARK   3      S21:  -0.1622 S22:  -0.0894 S23:   0.3522                       
REMARK   3      S31:   0.2280 S32:  -0.2043 S33:   0.0219                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'B' and (resid 249 through 272 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  98.9981  29.1348  16.0314              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8200 T22:   0.8806                                     
REMARK   3      T33:   0.6017 T12:   0.2060                                     
REMARK   3      T13:  -0.2898 T23:  -0.0143                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9457 L22:   0.3290                                     
REMARK   3      L33:   0.6825 L12:   0.4615                                     
REMARK   3      L13:   0.2755 L23:  -0.0994                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3368 S12:   0.7430 S13:   0.1728                       
REMARK   3      S21:  -1.0464 S22:  -0.0888 S23:   0.7385                       
REMARK   3      S31:   0.0091 S32:  -0.0757 S33:   0.0132                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain 'B' and (resid 273 through 326 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  94.5277  11.2075  30.3593              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4118 T22:   0.8008                                     
REMARK   3      T33:   0.7332 T12:  -0.0695                                     
REMARK   3      T13:  -0.1383 T23:  -0.1369                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5050 L22:   1.9492                                     
REMARK   3      L33:   2.1804 L12:   0.1231                                     
REMARK   3      L13:  -0.5648 L23:  -0.8901                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3688 S12:   0.1476 S13:  -0.2769                       
REMARK   3      S21:   0.0376 S22:  -0.3527 S23:   0.8690                       
REMARK   3      S31:   0.2722 S32:  -0.7511 S33:  -0.0031                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: chain 'B' and (resid 327 through 405 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 118.8332  21.3682  31.9198              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1846 T22:   0.2925                                     
REMARK   3      T33:   0.2583 T12:   0.0476                                     
REMARK   3      T13:   0.0047 T23:   0.0062                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2746 L22:   1.6265                                     
REMARK   3      L33:   2.0039 L12:  -0.8433                                     
REMARK   3      L13:   0.1186 L23:   0.1596                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0602 S12:   0.1180 S13:  -0.0210                       
REMARK   3      S21:  -0.0233 S22:  -0.0934 S23:   0.2658                       
REMARK   3      S31:  -0.1858 S32:  -0.3604 S33:   0.0555                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: chain 'B' and (resid 406 through 456 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 115.7828  18.0724  48.0940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1685 T22:   0.1700                                     
REMARK   3      T33:   0.1903 T12:   0.0052                                     
REMARK   3      T13:   0.0063 T23:   0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0064 L22:   1.4895                                     
REMARK   3      L33:   1.8524 L12:  -0.4722                                     
REMARK   3      L13:  -0.7277 L23:   0.5212                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0427 S12:   0.0070 S13:  -0.2256                       
REMARK   3      S21:   0.0049 S22:  -0.0628 S23:   0.1817                       
REMARK   3      S31:   0.0955 S32:  -0.2035 S33:   0.0860                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: chain 'B' and (resid 457 through 522 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 115.9591  23.4218  52.3811              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1530 T22:   0.1675                                     
REMARK   3      T33:   0.1955 T12:   0.0040                                     
REMARK   3      T13:   0.0216 T23:  -0.0163                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8055 L22:   1.3473                                     
REMARK   3      L33:   3.0423 L12:  -0.1265                                     
REMARK   3      L13:  -0.5842 L23:   0.4378                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0716 S12:   0.0335 S13:   0.0055                       
REMARK   3      S21:   0.0714 S22:  -0.0751 S23:   0.1139                       
REMARK   3      S31:  -0.0847 S32:  -0.3312 S33:  -0.0111                       
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 4LEV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB080541.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-FEB-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 153                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : SI                                 
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   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
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) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.98                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.4                               
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: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-30% JEFFAMINE M-600, PH 6.0, VAPOR    
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      106.49050            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.85750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      106.49050            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.85750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 36190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 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 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      284.29112            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       23.85750            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       79.42647            
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   OE2  GLU B   418     O    HOH B   811              2.03            
REMARK 500   NZ   LYS B   164     O    HOH B   836              2.08            
REMARK 500   O    HOH A   768     O    HOH A   891              2.08            
REMARK 500   OE1  GLU A   286     O    HOH A   869              2.12            
REMARK 500   OD2  ASP A   157     O    HOH A   837              2.13            
REMARK 500   OD1  ASP B   191     OH   TYR B   214              2.14            
REMARK 500   NZ   LYS A   458     O    HOH A   875              2.16            
REMARK 500   OG   SER B   305     O    PRO B   361              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    GLU A   314     NZ   LYS A   506     4655     2.16            
REMARK 500   OD2  ASP A   456     NZ   LYS B   400     4656     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 306   C   -  N   -  CA  ANGL. DEV. = -20.3 DEGREES          
REMARK 500    PRO B 257   C   -  N   -  CA  ANGL. DEV. =   9.7 DEGREES          
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 180      -39.64    -26.07                                   
REMARK 500    LEU A 209      -78.92    -72.70                                   
REMARK 500    ASN A 210       85.91    -55.92                                   
REMARK 500    TYR A 214       58.35    -97.17                                   
REMARK 500    TYR A 215      154.74    173.44                                   
REMARK 500    GLU A 216       93.14    176.77                                   
REMARK 500    ARG A 236       89.44   -152.80                                   
REMARK 500    SER A 243       47.25     35.79                                   
REMARK 500    ARG A 246      -30.23     67.20                                   
REMARK 500    PRO A 261       22.20    -67.65                                   
REMARK 500    THR A 294      116.86   -160.04                                   
REMARK 500    SER A 313     -135.80     53.65                                   
REMARK 500    TRP A 343      -68.18   -107.80                                   
REMARK 500    SER A 345      153.46    106.33                                   
REMARK 500    LYS A 362      111.49   -167.75                                   
REMARK 500    GLU A 366     -160.24   -101.94                                   
REMARK 500    LYS A 428        2.48     43.33                                   
REMARK 500    ARG B 176       60.75   -112.98                                   
REMARK 500    LEU B 209      -75.70    -71.11                                   
REMARK 500    ASN B 210       94.98    -67.83                                   
REMARK 500    ARG B 236       70.91     35.84                                   
REMARK 500    ARG B 246      -31.37     73.37                                   
REMARK 500    LYS B 254      -74.10    -58.12                                   
REMARK 500    PRO B 257     -129.73    -11.75                                   
REMARK 500    LYS B 258      -76.32     41.68                                   
REMARK 500    PRO B 261        9.94    -60.94                                   
REMARK 500    GLN B 264       -7.65    -59.44                                   
REMARK 500    ASN B 289        0.59    -64.12                                   
REMARK 500    THR B 294     -161.44   -117.76                                   
REMARK 500    ARG B 302       -3.00   -158.29                                   
REMARK 500    PRO B 306       40.98   -102.84                                   
REMARK 500    ALA B 307      -61.89     -9.23                                   
REMARK 500    SER B 313     -121.60     47.47                                   
REMARK 500    GLU B 314       26.67   -143.23                                   
REMARK 500    TRP B 343      -66.20   -107.90                                   
REMARK 500    SER B 345      155.21    103.85                                   
REMARK 500    GLU B 366     -122.99    -75.03                                   
REMARK 500    GLU B 373       40.78   -102.18                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 SER A  305     PRO A  306                  143.85                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    SER A 305        24.9      L          L   OUTSIDE RANGE           
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 B 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 390   NE2                                                    
REMARK 620 2 CYS B 397   SG  108.2                                              
REMARK 620 3 CYS B 396   SG  111.3 129.4                                        
REMARK 620 4 CYS B 404   SG   98.1 104.1 100.3                                  
REMARK 620 N                    1     2     3                                   
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  112.3                                              
REMARK 620 3 CYS A 397   SG  106.2 130.7                                        
REMARK 620 4 CYS A 404   SG   95.4 100.1 105.8                                  
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 ZN B 601                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4LEW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4LEY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4LEZ   RELATED DB: PDB                                   
DBREF  4LEV A  157   522  UNP    Q8N884   CGAS_HUMAN     157    522             
DBREF  4LEV B  157   522  UNP    Q8N884   CGAS_HUMAN     157    522             
SEQADV 4LEV PHE A  154  UNP  Q8N884              EXPRESSION TAG                 
SEQADV 4LEV GLU A  155  UNP  Q8N884              EXPRESSION TAG                 
SEQADV 4LEV LEU A  156  UNP  Q8N884              EXPRESSION TAG                 
SEQADV 4LEV PHE B  154  UNP  Q8N884              EXPRESSION TAG                 
SEQADV 4LEV GLU B  155  UNP  Q8N884              EXPRESSION TAG                 
SEQADV 4LEV LEU B  156  UNP  Q8N884              EXPRESSION TAG                 
SEQRES   1 A  369  PHE GLU LEU 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE          
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                                          
SEQRES   1 B  369  PHE GLU LEU ASP ALA ALA PRO GLY ALA SER LYS LEU ARG          
SEQRES   2 B  369  ALA VAL LEU GLU LYS LEU LYS LEU SER ARG ASP ASP ILE          
SEQRES   3 B  369  SER THR ALA ALA GLY MSE VAL LYS GLY VAL VAL ASP HIS          
SEQRES   4 B  369  LEU LEU LEU ARG LEU LYS CYS ASP SER ALA PHE ARG GLY          
SEQRES   5 B  369  VAL GLY LEU LEU ASN THR GLY SER TYR TYR GLU HIS VAL          
SEQRES   6 B  369  LYS ILE SER ALA PRO ASN GLU PHE ASP VAL MSE PHE LYS          
SEQRES   7 B  369  LEU GLU VAL PRO ARG ILE GLN LEU GLU GLU TYR SER ASN          
SEQRES   8 B  369  THR ARG ALA TYR TYR PHE VAL LYS PHE LYS ARG ASN PRO          
SEQRES   9 B  369  LYS GLU ASN PRO LEU SER GLN PHE LEU GLU GLY GLU ILE          
SEQRES  10 B  369  LEU SER ALA SER LYS MSE LEU SER LYS PHE ARG LYS ILE          
SEQRES  11 B  369  ILE LYS GLU GLU ILE ASN ASP ILE LYS ASP THR ASP VAL          
SEQRES  12 B  369  ILE MSE LYS ARG LYS ARG GLY GLY SER PRO ALA VAL THR          
SEQRES  13 B  369  LEU LEU ILE SER GLU LYS ILE SER VAL ASP ILE THR LEU          
SEQRES  14 B  369  ALA LEU GLU SER LYS SER SER TRP PRO ALA SER THR GLN          
SEQRES  15 B  369  GLU GLY LEU ARG ILE GLN ASN TRP LEU SER ALA LYS VAL          
SEQRES  16 B  369  ARG LYS GLN LEU ARG LEU LYS PRO PHE TYR LEU VAL PRO          
SEQRES  17 B  369  LYS HIS ALA LYS GLU GLY ASN GLY PHE GLN GLU GLU THR          
SEQRES  18 B  369  TRP ARG LEU SER PHE SER HIS ILE GLU LYS GLU ILE LEU          
SEQRES  19 B  369  ASN ASN HIS GLY LYS SER LYS THR CYS CYS GLU ASN LYS          
SEQRES  20 B  369  GLU GLU LYS CYS CYS ARG LYS ASP CYS LEU LYS LEU MSE          
SEQRES  21 B  369  LYS TYR LEU LEU GLU GLN LEU LYS GLU ARG PHE LYS ASP          
SEQRES  22 B  369  LYS LYS HIS LEU ASP LYS PHE SER SER TYR HIS VAL LYS          
SEQRES  23 B  369  THR ALA PHE PHE HIS VAL CYS THR GLN ASN PRO GLN ASP          
SEQRES  24 B  369  SER GLN TRP ASP ARG LYS ASP LEU GLY LEU CYS PHE ASP          
SEQRES  25 B  369  ASN CYS VAL THR TYR PHE LEU GLN CYS LEU ARG THR GLU          
SEQRES  26 B  369  LYS LEU GLU ASN TYR PHE ILE PRO GLU PHE ASN LEU PHE          
SEQRES  27 B  369  SER SER ASN LEU ILE ASP LYS ARG SER LYS GLU PHE LEU          
SEQRES  28 B  369  THR LYS GLN ILE GLU TYR GLU ARG ASN ASN GLU PHE PRO          
SEQRES  29 B  369  VAL PHE ASP GLU PHE                                          
MODRES 4LEV MSE A  185  MET  SELENOMETHIONINE                                   
MODRES 4LEV MSE A  229  MET  SELENOMETHIONINE                                   
MODRES 4LEV MSE A  276  MET  SELENOMETHIONINE                                   
MODRES 4LEV MSE A  298  MET  SELENOMETHIONINE                                   
MODRES 4LEV MSE A  413  MET  SELENOMETHIONINE                                   
MODRES 4LEV MSE B  185  MET  SELENOMETHIONINE                                   
MODRES 4LEV MSE B  229  MET  SELENOMETHIONINE                                   
MODRES 4LEV MSE B  276  MET  SELENOMETHIONINE                                   
MODRES 4LEV MSE B  298  MET  SELENOMETHIONINE                                   
MODRES 4LEV MSE B  413  MET  SELENOMETHIONINE                                   
HET    MSE  A 185       8                                                       
HET    MSE  A 229       8                                                       
HET    MSE  A 276       8                                                       
HET    MSE  A 298       8                                                       
HET    MSE  A 413      16                                                       
HET    MSE  B 185      16                                                       
HET    MSE  B 229       8                                                       
HET    MSE  B 276       8                                                       
HET    MSE  B 298       8                                                       
HET    MSE  B 413      16                                                       
HET     ZN  A 601       1                                                       
HET     ZN  B 601       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      ZN ZINC ION                                                         
FORMUL   1  MSE    10(C5 H11 N O2 SE)                                           
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   5  HOH   *451(H2 O)                                                    
HELIX    1   1 GLY A  161  SER A  175  1                                  15    
HELIX    2   2 ILE A  179  LYS A  198  1                                  20    
HELIX    3   3 CYS A  199  ARG A  204  5                                   6    
HELIX    4   4 LEU A  262  GLN A  264  5                                   3    
HELIX    5   5 SER A  272  ASN A  289  1                                  18    
HELIX    6   6 PRO A  331  GLN A  335  5                                   5    
HELIX    7   7 SER A  345  LEU A  354  1                                  10    
HELIX    8   8 PHE A  379  ASN A  389  1                                  11    
HELIX    9   9 CYS A  405  PHE A  424  1                                  20    
HELIX   10  10 LYS A  425  LYS A  428  5                                   4    
HELIX   11  11 SER A  434  ASN A  449  1                                  16    
HELIX   12  12 GLN A  451  LYS A  458  5                                   8    
HELIX   13  13 ASP A  459  GLU A  478  1                                  20    
HELIX   14  14 ASP A  497  ASN A  514  1                                  18    
HELIX   15  15 PRO A  517  PHE A  522  1                                   6    
HELIX   16  16 ALA B  162  SER B  175  1                                  14    
HELIX   17  17 ASP B  178  CYS B  199  1                                  22    
HELIX   18  18 ASP B  200  ARG B  204  5                                   5    
HELIX   19  19 LEU B  262  GLN B  264  5                                   3    
HELIX   20  20 SER B  272  ASN B  289  1                                  18    
HELIX   21  21 PRO B  331  GLN B  335  5                                   5    
HELIX   22  22 SER B  345  LEU B  354  1                                  10    
HELIX   23  23 PHE B  379  ASN B  389  1                                  11    
HELIX   24  24 ASN B  399  LYS B  403  5                                   5    
HELIX   25  25 CYS B  405  PHE B  424  1                                  20    
HELIX   26  26 SER B  434  ASN B  449  1                                  16    
HELIX   27  27 GLN B  451  LYS B  458  5                                   8    
HELIX   28  28 ASP B  459  GLU B  478  1                                  20    
HELIX   29  29 ASP B  497  ASN B  514  1                                  18    
HELIX   30  30 GLU B  515  ASP B  520  5                                   6    
SHEET    1   A 7 GLY A 207  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  SER A 317   N  PHE A 226           
SHEET    4   A 7 PHE A 357  PRO A 361 -1  O  PHE A 357   N  SER A 326           
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 GLY A 207  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  SER A 317   N  PHE A 226           
SHEET    4   B 5 VAL A 308  ILE A 312 -1  N  VAL A 308   O  ILE A 320           
SHEET    5   B 5 VAL A 296  MSE 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           
SHEET    1   D 2 ALA A 364  LYS A 365  0                                        
SHEET    2   D 2 PHE A 370  GLN A 371 -1  O  GLN A 371   N  ALA A 364           
SHEET    1   E 7 VAL B 206  LEU B 208  0                                        
SHEET    2   E 7 GLU B 225  GLU B 233 -1  O  LYS B 231   N  GLY B 207           
SHEET    3   E 7 ILE B 316  SER B 326  1  O  THR B 321   N  PHE B 230           
SHEET    4   E 7 PHE B 357  PRO B 361 -1  O  LEU B 359   N  LEU B 324           
SHEET    5   E 7 TRP B 375  SER B 378 -1  O  ARG B 376   N  VAL B 360           
SHEET    6   E 7 TYR B 248  PHE B 253 -1  N  TYR B 249   O  TRP B 375           
SHEET    7   E 7 ILE B 237  GLU B 241 -1  N  GLN B 238   O  LYS B 252           
SHEET    1   F 5 VAL B 206  LEU B 208  0                                        
SHEET    2   F 5 GLU B 225  GLU B 233 -1  O  LYS B 231   N  GLY B 207           
SHEET    3   F 5 ILE B 316  SER B 326  1  O  THR B 321   N  PHE B 230           
SHEET    4   F 5 VAL B 308  ILE B 312 -1  N  VAL B 308   O  ILE B 320           
SHEET    5   F 5 VAL B 296  MSE B 298 -1  N  ILE B 297   O  LEU B 311           
SHEET    1   G 2 LEU B 266  GLU B 267  0                                        
SHEET    2   G 2 ILE B 270  LEU B 271 -1  O  ILE B 270   N  GLU B 267           
SHEET    1   H 2 ALA B 364  LYS B 365  0                                        
SHEET    2   H 2 PHE B 370  GLN B 371 -1  O  GLN B 371   N  ALA B 364           
LINK         C   GLY A 184                 N   MSE A 185     1555   1555  1.33  
LINK         C   MSE A 185                 N   VAL A 186     1555   1555  1.34  
LINK         C   VAL A 228                 N   MSE A 229     1555   1555  1.33  
LINK         C   MSE A 229                 N   PHE A 230     1555   1555  1.33  
LINK         C   LYS A 275                 N   MSE A 276     1555   1555  1.33  
LINK         C   MSE A 276                 N   LEU A 277     1555   1555  1.33  
LINK         C   ILE A 297                 N   MSE A 298     1555   1555  1.33  
LINK         C   MSE A 298                 N   LYS A 299     1555   1555  1.33  
LINK         C   LEU A 412                 N  AMSE A 413     1555   1555  1.34  
LINK         C   LEU A 412                 N  BMSE A 413     1555   1555  1.33  
LINK         C  AMSE A 413                 N   LYS A 414     1555   1555  1.33  
LINK         C  BMSE A 413                 N   LYS A 414     1555   1555  1.33  
LINK         C   GLY B 184                 N  AMSE B 185     1555   1555  1.33  
LINK         C   GLY B 184                 N  BMSE B 185     1555   1555  1.33  
LINK         C  AMSE B 185                 N   VAL B 186     1555   1555  1.33  
LINK         C  BMSE B 185                 N   VAL B 186     1555   1555  1.33  
LINK         C   VAL B 228                 N   MSE B 229     1555   1555  1.33  
LINK         C   MSE B 229                 N   PHE B 230     1555   1555  1.33  
LINK         C   LYS B 275                 N   MSE B 276     1555   1555  1.32  
LINK         C   MSE B 276                 N   LEU B 277     1555   1555  1.33  
LINK         C   ILE B 297                 N   MSE B 298     1555   1555  1.33  
LINK         C   MSE B 298                 N   LYS B 299     1555   1555  1.33  
LINK         C   LEU B 412                 N  AMSE B 413     1555   1555  1.34  
LINK         C   LEU B 412                 N  BMSE B 413     1555   1555  1.33  
LINK         C  AMSE B 413                 N   LYS B 414     1555   1555  1.33  
LINK         C  BMSE B 413                 N   LYS B 414     1555   1555  1.33  
LINK         NE2 HIS B 390                ZN    ZN B 601     1555   1555  2.07  
LINK         NE2 HIS A 390                ZN    ZN A 601     1555   1555  2.14  
LINK         SG  CYS B 397                ZN    ZN B 601     1555   1555  2.25  
LINK         SG  CYS B 396                ZN    ZN B 601     1555   1555  2.28  
LINK         SG  CYS A 396                ZN    ZN A 601     1555   1555  2.29  
LINK         SG  CYS A 397                ZN    ZN A 601     1555   1555  2.34  
LINK         SG  CYS B 404                ZN    ZN B 601     1555   1555  2.35  
LINK         SG  CYS A 404                ZN    ZN A 601     1555   1555  2.36  
SITE     1 AC1  4 HIS A 390  CYS A 396  CYS A 397  CYS A 404                    
SITE     1 AC2  4 HIS B 390  CYS B 396  CYS B 397  CYS B 404                    
CRYST1  212.981   47.715   86.869  90.00 113.89  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.004695  0.000000  0.002080        0.00000                         
SCALE2      0.000000  0.020958  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012590        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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