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Database: PDB
Entry: 4LEW
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Original site: 4LEW 
HEADER    TRANSFERASE                             26-JUN-13   4LEW              
TITLE     STRUCTURE OF HUMAN CGAS                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIC GMP-AMP SYNTHASE;                                   
COMPND   3 CHAIN: B, A;                                                         
COMPND   4 FRAGMENT: 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 4LEW    1       JRNL                                     
REVDAT   1   25-DEC-13 4LEW    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.    2.04 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) : 2.04                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.75                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 97840                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3973                            
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 40.7552 -  6.1870    0.98     3303   141  0.1794 0.2309        
REMARK   3     2  6.1870 -  4.9135    0.99     3345   145  0.1737 0.1900        
REMARK   3     3  4.9135 -  4.2932    1.00     3322   151  0.1494 0.1750        
REMARK   3     4  4.2932 -  3.9010    0.99     3364   138  0.1506 0.1944        
REMARK   3     5  3.9010 -  3.6216    1.00     3346   144  0.1621 0.2033        
REMARK   3     6  3.6216 -  3.4082    1.00     3402   132  0.1655 0.2096        
REMARK   3     7  3.4082 -  3.2375    1.00     3377   151  0.1746 0.2110        
REMARK   3     8  3.2375 -  3.0967    1.00     3316   143  0.1874 0.2551        
REMARK   3     9  3.0967 -  2.9775    1.00     3437   135  0.1963 0.2423        
REMARK   3    10  2.9775 -  2.8748    1.00     3329   142  0.1930 0.3111        
REMARK   3    11  2.8748 -  2.7849    1.00     3358   152  0.1987 0.2840        
REMARK   3    12  2.7849 -  2.7053    1.00     3394   119  0.1818 0.2266        
REMARK   3    13  2.7053 -  2.6341    1.00     3328   150  0.1759 0.2130        
REMARK   3    14  2.6341 -  2.5699    1.00     3366   143  0.1843 0.2529        
REMARK   3    15  2.5699 -  2.5114    1.00     3396   147  0.1674 0.1774        
REMARK   3    16  2.5114 -  2.4580    1.00     3312   126  0.1738 0.2363        
REMARK   3    17  2.4580 -  2.4088    1.00     3413   154  0.1834 0.2236        
REMARK   3    18  2.4088 -  2.3634    1.00     3325   126  0.1905 0.2634        
REMARK   3    19  2.3634 -  2.3212    1.00     3342   159  0.1825 0.2492        
REMARK   3    20  2.3212 -  2.2818    1.00     3417   126  0.1890 0.2172        
REMARK   3    21  2.2818 -  2.2450    1.00     3332   148  0.1976 0.2518        
REMARK   3    22  2.2450 -  2.2105    1.00     3371   143  0.1971 0.2062        
REMARK   3    23  2.2105 -  2.1780    1.00     3384   135  0.2080 0.2709        
REMARK   3    24  2.1780 -  2.1473    1.00     3358   160  0.2136 0.2429        
REMARK   3    25  2.1473 -  2.1183    1.00     3297   140  0.2245 0.2347        
REMARK   3    26  2.1183 -  2.0908    1.00     3428   125  0.2287 0.2995        
REMARK   3    27  2.0908 -  2.0647    1.00     3346   158  0.2425 0.2879        
REMARK   3    28  2.0647 -  2.0398    0.95     3159   140  0.2607 0.2874        
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)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.470           
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      :  0.009           6030                                  
REMARK   3   ANGLE     :  1.122           8089                                  
REMARK   3   CHIRALITY :  0.078            876                                  
REMARK   3   PLANARITY :  0.006           1029                                  
REMARK   3   DIHEDRAL  : 14.809           2331                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'B' and (resid 162 through 224 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -22.1683  78.2677  62.0440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5272 T22:   0.6244                                     
REMARK   3      T33:   0.8515 T12:  -0.0946                                     
REMARK   3      T13:   0.0095 T23:   0.1615                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.3349 L22:   4.2775                                     
REMARK   3      L33:   0.2725 L12:   1.6196                                     
REMARK   3      L13:  -0.6800 L23:  -1.3391                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0515 S12:   0.3679 S13:   0.3033                       
REMARK   3      S21:  -0.1688 S22:   0.2001 S23:   1.0987                       
REMARK   3      S31:   0.0079 S32:  -0.5895 S33:  -0.1327                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'B' and (resid 225 through 286 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.8414  95.0963  69.8216              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8000 T22:   0.4165                                     
REMARK   3      T33:   0.4472 T12:  -0.1643                                     
REMARK   3      T13:   0.1179 T23:  -0.0910                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2824 L22:   3.0337                                     
REMARK   3      L33:   3.0973 L12:  -1.7173                                     
REMARK   3      L13:   0.9717 L23:  -1.1199                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0076 S12:  -0.2467 S13:   0.4986                       
REMARK   3      S21:   0.6538 S22:   0.2304 S23:  -0.4263                       
REMARK   3      S31:  -1.0320 S32:   0.3256 S33:  -0.2624                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'B' and (resid 287 through 405 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -10.0750  80.0853  66.8447              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2411 T22:   0.3303                                     
REMARK   3      T33:   0.2583 T12:  -0.0494                                     
REMARK   3      T13:   0.0697 T23:  -0.0190                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6426 L22:   2.4084                                     
REMARK   3      L33:   2.8371 L12:  -0.1797                                     
REMARK   3      L13:  -0.4982 L23:   0.5771                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0709 S12:  -0.2901 S13:   0.3471                       
REMARK   3      S21:   0.2432 S22:   0.1090 S23:   0.2722                       
REMARK   3      S31:  -0.4152 S32:  -0.0432 S33:  -0.1338                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'B' and (resid 406 through 520 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -12.9288  64.7875  77.9333              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3381 T22:   0.3418                                     
REMARK   3      T33:   0.1940 T12:  -0.0383                                     
REMARK   3      T13:   0.0290 T23:   0.0623                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2869 L22:   1.7500                                     
REMARK   3      L33:   4.0756 L12:  -0.2065                                     
REMARK   3      L13:  -1.2268 L23:   0.8357                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1723 S12:  -0.1474 S13:  -0.0721                       
REMARK   3      S21:   0.4677 S22:   0.0087 S23:   0.1904                       
REMARK   3      S31:   0.5935 S32:  -0.1709 S33:   0.1003                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'A' and (resid 157 through 180 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  22.6698  56.2283  41.2551              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2513 T22:   0.2498                                     
REMARK   3      T33:   0.4041 T12:   0.0109                                     
REMARK   3      T13:  -0.0306 T23:   0.0772                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5566 L22:   8.1525                                     
REMARK   3      L33:   2.9931 L12:   1.2226                                     
REMARK   3      L13:   0.0565 L23:   1.2297                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3084 S12:  -0.1272 S13:  -0.3783                       
REMARK   3      S21:   0.3818 S22:  -0.0344 S23:  -0.6256                       
REMARK   3      S31:   0.0235 S32:   0.3017 S33:  -0.1587                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'A' and (resid 181 through 272 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   7.7733  86.1727  33.5728              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1919 T22:   0.1761                                     
REMARK   3      T33:   0.3822 T12:   0.0044                                     
REMARK   3      T13:   0.0098 T23:  -0.0215                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9399 L22:   3.0203                                     
REMARK   3      L33:   1.6007 L12:   1.7902                                     
REMARK   3      L13:   0.8479 L23:   1.0233                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0692 S12:  -0.0472 S13:   0.0178                       
REMARK   3      S21:  -0.1543 S22:   0.0027 S23:  -0.4532                       
REMARK   3      S31:  -0.1820 S32:   0.0090 S33:   0.0005                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'A' and (resid 273 through 405 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   8.5367  77.2835  35.0272              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1523 T22:   0.1901                                     
REMARK   3      T33:   0.2517 T12:  -0.0108                                     
REMARK   3      T13:   0.0363 T23:  -0.0553                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3081 L22:   3.1624                                     
REMARK   3      L33:   0.9591 L12:   0.3895                                     
REMARK   3      L13:  -0.4564 L23:  -0.1925                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0935 S12:  -0.0117 S13:   0.1758                       
REMARK   3      S21:  -0.3181 S22:   0.1880 S23:  -0.5100                       
REMARK   3      S31:  -0.0922 S32:   0.0606 S33:  -0.1030                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'A' and (resid 406 through 520 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  10.0282  57.4911  29.2675              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2387 T22:   0.0986                                     
REMARK   3      T33:   0.1735 T12:   0.0383                                     
REMARK   3      T13:   0.0212 T23:  -0.0035                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1401 L22:   1.7068                                     
REMARK   3      L33:   3.0036 L12:  -0.4061                                     
REMARK   3      L13:  -0.3579 L23:   0.2789                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0389 S12:   0.1727 S13:  -0.1970                       
REMARK   3      S21:  -0.4038 S22:  -0.1146 S23:  -0.1080                       
REMARK   3      S31:   0.1856 S32:   0.1477 S33:   0.0355                       
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 4LEW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-AUG-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB080542.                                      
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                             : 7.0                                
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) : 2.040                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.08300                            
REMARK 200  R SYM                      (I) : 0.08300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 31.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
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   (%): 46.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-20% PEG 3350, 0.2 M A.S., PH 7.0,     
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       55.74000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP B   157                                                      
REMARK 465     ALA B   158                                                      
REMARK 465     ALA B   159                                                      
REMARK 465     PRO B   160                                                      
REMARK 465     GLY B   161                                                      
REMARK 465     GLU B   521                                                      
REMARK 465     PHE B   522                                                      
REMARK 465     SER A   213                                                      
REMARK 465     TYR A   214                                                      
REMARK 465     GLU A   521                                                      
REMARK 465     PHE A   522                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS B 427    CG   CD   CE   NZ                                   
REMARK 470     LYS A 427    CG   CD   CE   NZ                                   
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   O    LEU B   209     O    HOH B   756              2.17            
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    ALA B 222       72.34     56.68                                   
REMARK 500    ARG B 236       96.29     30.60                                   
REMARK 500    SER B 243     -134.45     55.15                                   
REMARK 500    ARG B 246      -24.76     63.80                                   
REMARK 500    ARG B 255      165.93     60.78                                   
REMARK 500    ASN B 256       46.28   -172.71                                   
REMARK 500    PRO B 257       36.40     10.62                                   
REMARK 500    ASP B 293     -106.65     59.22                                   
REMARK 500    THR B 294     -107.22   -120.06                                   
REMARK 500    LYS B 301     -153.85    -89.14                                   
REMARK 500    ARG B 302     -122.49   -128.02                                   
REMARK 500    SER B 313      101.49    -54.25                                   
REMARK 500    GLU B 314       12.79    161.12                                   
REMARK 500    TRP B 343      -67.77   -105.70                                   
REMARK 500    SER B 345      152.90    106.69                                   
REMARK 500    ASN B 368      -19.88     66.26                                   
REMARK 500    GLU B 372      151.83     95.55                                   
REMARK 500    PHE B 516       70.21     52.74                                   
REMARK 500    ARG A 176       24.32    -74.17                                   
REMARK 500    GLU A 216      111.63   -172.23                                   
REMARK 500    ARG A 246      -27.71     71.30                                   
REMARK 500    ARG A 302     -119.77   -115.60                                   
REMARK 500    SER A 313     -109.37     53.11                                   
REMARK 500    TRP A 343      -68.15   -107.03                                   
REMARK 500    SER A 345      156.37    104.89                                   
REMARK 500    LYS A 362      151.44    176.68                                   
REMARK 500    LYS A 365       32.33    -74.85                                   
REMARK 500    ASN A 368       24.62   -163.12                                   
REMARK 500    GLN A 371       41.41     36.25                                   
REMARK 500    PHE A 516       60.81     38.10                                   
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 ILE B  291     LYS B  292                  148.54                    
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  110.9                                              
REMARK 620 3 CYS A 397   SG  110.1 129.3                                        
REMARK 620 4 CYS A 404   SG   93.1  99.8 106.5                                  
REMARK 620 N                    1     2     3                                   
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 396   SG  113.8                                              
REMARK 620 3 CYS B 397   SG  106.8 129.3                                        
REMARK 620 4 CYS B 404   SG   95.8  98.7 106.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 601                  
DBREF  4LEW B  157   522  UNP    Q8N884   CGAS_HUMAN     157    522             
DBREF  4LEW A  157   522  UNP    Q8N884   CGAS_HUMAN     157    522             
SEQRES   1 B  366  ASP ALA ALA PRO GLY ALA SER LYS LEU ARG ALA VAL LEU          
SEQRES   2 B  366  GLU LYS LEU LYS LEU SER ARG ASP ASP ILE SER THR ALA          
SEQRES   3 B  366  ALA GLY MSE VAL LYS GLY VAL VAL ASP HIS LEU LEU LEU          
SEQRES   4 B  366  ARG LEU LYS CYS ASP SER ALA PHE ARG GLY VAL GLY LEU          
SEQRES   5 B  366  LEU ASN THR GLY SER TYR TYR GLU HIS VAL LYS ILE SER          
SEQRES   6 B  366  ALA PRO ASN GLU PHE ASP VAL MSE PHE LYS LEU GLU VAL          
SEQRES   7 B  366  PRO ARG ILE GLN LEU GLU GLU TYR SER ASN THR ARG ALA          
SEQRES   8 B  366  TYR TYR PHE VAL LYS PHE LYS ARG ASN PRO LYS GLU ASN          
SEQRES   9 B  366  PRO LEU SER GLN PHE LEU GLU GLY GLU ILE LEU SER ALA          
SEQRES  10 B  366  SER LYS MSE LEU SER LYS PHE ARG LYS ILE ILE LYS GLU          
SEQRES  11 B  366  GLU ILE ASN ASP ILE LYS ASP THR ASP VAL ILE MSE LYS          
SEQRES  12 B  366  ARG LYS ARG GLY GLY SER PRO ALA VAL THR LEU LEU ILE          
SEQRES  13 B  366  SER GLU LYS ILE SER VAL ASP ILE THR LEU ALA LEU GLU          
SEQRES  14 B  366  SER LYS SER SER TRP PRO ALA SER THR GLN GLU GLY LEU          
SEQRES  15 B  366  ARG ILE GLN ASN TRP LEU SER ALA LYS VAL ARG LYS GLN          
SEQRES  16 B  366  LEU ARG LEU LYS PRO PHE TYR LEU VAL PRO LYS HIS ALA          
SEQRES  17 B  366  LYS GLU GLY ASN GLY PHE GLN GLU GLU THR TRP ARG LEU          
SEQRES  18 B  366  SER PHE SER HIS ILE GLU LYS GLU ILE LEU ASN ASN HIS          
SEQRES  19 B  366  GLY LYS SER LYS THR CYS CYS GLU ASN LYS GLU GLU LYS          
SEQRES  20 B  366  CYS CYS ARG LYS ASP CYS LEU LYS LEU MSE LYS TYR LEU          
SEQRES  21 B  366  LEU GLU GLN LEU LYS GLU ARG PHE LYS ASP LYS LYS HIS          
SEQRES  22 B  366  LEU ASP LYS PHE SER SER TYR HIS VAL LYS THR ALA PHE          
SEQRES  23 B  366  PHE HIS VAL CYS THR GLN ASN PRO GLN ASP SER GLN TRP          
SEQRES  24 B  366  ASP ARG LYS ASP LEU GLY LEU CYS PHE ASP ASN CYS VAL          
SEQRES  25 B  366  THR TYR PHE LEU GLN CYS LEU ARG THR GLU LYS LEU GLU          
SEQRES  26 B  366  ASN TYR PHE ILE PRO GLU PHE ASN LEU PHE SER SER ASN          
SEQRES  27 B  366  LEU ILE ASP LYS ARG SER LYS GLU PHE LEU THR LYS GLN          
SEQRES  28 B  366  ILE GLU TYR GLU ARG ASN ASN GLU PHE PRO VAL PHE ASP          
SEQRES  29 B  366  GLU PHE                                                      
SEQRES   1 A  366  ASP ALA ALA PRO GLY ALA SER LYS LEU ARG ALA VAL LEU          
SEQRES   2 A  366  GLU LYS LEU LYS LEU SER ARG ASP ASP ILE SER THR ALA          
SEQRES   3 A  366  ALA GLY MSE VAL LYS GLY VAL VAL ASP HIS LEU LEU LEU          
SEQRES   4 A  366  ARG LEU LYS CYS ASP SER ALA PHE ARG GLY VAL GLY LEU          
SEQRES   5 A  366  LEU ASN THR GLY SER TYR TYR GLU HIS VAL LYS ILE SER          
SEQRES   6 A  366  ALA PRO ASN GLU PHE ASP VAL MSE PHE LYS LEU GLU VAL          
SEQRES   7 A  366  PRO ARG ILE GLN LEU GLU GLU TYR SER ASN THR ARG ALA          
SEQRES   8 A  366  TYR TYR PHE VAL LYS PHE LYS ARG ASN PRO LYS GLU ASN          
SEQRES   9 A  366  PRO LEU SER GLN PHE LEU GLU GLY GLU ILE LEU SER ALA          
SEQRES  10 A  366  SER LYS MSE LEU SER LYS PHE ARG LYS ILE ILE LYS GLU          
SEQRES  11 A  366  GLU ILE ASN ASP ILE LYS ASP THR ASP VAL ILE MSE LYS          
SEQRES  12 A  366  ARG LYS ARG GLY GLY SER PRO ALA VAL THR LEU LEU ILE          
SEQRES  13 A  366  SER GLU LYS ILE SER VAL ASP ILE THR LEU ALA LEU GLU          
SEQRES  14 A  366  SER LYS SER SER TRP PRO ALA SER THR GLN GLU GLY LEU          
SEQRES  15 A  366  ARG ILE GLN ASN TRP LEU SER ALA LYS VAL ARG LYS GLN          
SEQRES  16 A  366  LEU ARG LEU LYS PRO PHE TYR LEU VAL PRO LYS HIS ALA          
SEQRES  17 A  366  LYS GLU GLY ASN GLY PHE GLN GLU GLU THR TRP ARG LEU          
SEQRES  18 A  366  SER PHE SER HIS ILE GLU LYS GLU ILE LEU ASN ASN HIS          
SEQRES  19 A  366  GLY LYS SER LYS THR CYS CYS GLU ASN LYS GLU GLU LYS          
SEQRES  20 A  366  CYS CYS ARG LYS ASP CYS LEU LYS LEU MSE LYS TYR LEU          
SEQRES  21 A  366  LEU GLU GLN LEU LYS GLU ARG PHE LYS ASP LYS LYS HIS          
SEQRES  22 A  366  LEU ASP LYS PHE SER SER TYR HIS VAL LYS THR ALA PHE          
SEQRES  23 A  366  PHE HIS VAL CYS THR GLN ASN PRO GLN ASP SER GLN TRP          
SEQRES  24 A  366  ASP ARG LYS ASP LEU GLY LEU CYS PHE ASP ASN CYS VAL          
SEQRES  25 A  366  THR TYR PHE LEU GLN CYS LEU ARG THR GLU LYS LEU GLU          
SEQRES  26 A  366  ASN TYR PHE ILE PRO GLU PHE ASN LEU PHE SER SER ASN          
SEQRES  27 A  366  LEU ILE ASP LYS ARG SER LYS GLU PHE LEU THR LYS GLN          
SEQRES  28 A  366  ILE GLU TYR GLU ARG ASN ASN GLU PHE PRO VAL PHE ASP          
SEQRES  29 A  366  GLU PHE                                                      
MODRES 4LEW MSE B  185  MET  SELENOMETHIONINE                                   
MODRES 4LEW MSE B  229  MET  SELENOMETHIONINE                                   
MODRES 4LEW MSE B  276  MET  SELENOMETHIONINE                                   
MODRES 4LEW MSE B  298  MET  SELENOMETHIONINE                                   
MODRES 4LEW MSE B  413  MET  SELENOMETHIONINE                                   
MODRES 4LEW MSE A  185  MET  SELENOMETHIONINE                                   
MODRES 4LEW MSE A  229  MET  SELENOMETHIONINE                                   
MODRES 4LEW MSE A  276  MET  SELENOMETHIONINE                                   
MODRES 4LEW MSE A  298  MET  SELENOMETHIONINE                                   
MODRES 4LEW MSE A  413  MET  SELENOMETHIONINE                                   
HET    MSE  B 185       8                                                       
HET    MSE  B 229       8                                                       
HET    MSE  B 276       8                                                       
HET    MSE  B 298       8                                                       
HET    MSE  B 413       8                                                       
HET    MSE  A 185       8                                                       
HET    MSE  A 229       8                                                       
HET    MSE  A 276       8                                                       
HET    MSE  A 298       8                                                       
HET    MSE  A 413       8                                                       
HET     ZN  B 601       1                                                       
HET     ZN  A 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   *363(H2 O)                                                    
HELIX    1   1 ALA B  162  LEU B  174  1                                  13    
HELIX    2   2 SER B  175  LYS B  198  1                                  24    
HELIX    3   3 LEU B  262  GLN B  264  5                                   3    
HELIX    4   4 SER B  272  GLU B  287  1                                  16    
HELIX    5   5 PRO B  331  GLN B  335  5                                   5    
HELIX    6   6 SER B  345  LEU B  354  1                                  10    
HELIX    7   7 PHE B  379  ASN B  389  1                                  11    
HELIX    8   8 ASN B  399  LYS B  403  5                                   5    
HELIX    9   9 CYS B  405  PHE B  424  1                                  20    
HELIX   10  10 SER B  434  ASN B  449  1                                  16    
HELIX   11  11 GLN B  451  TRP B  455  5                                   5    
HELIX   12  12 ASP B  456  LYS B  458  5                                   3    
HELIX   13  13 ASP B  459  GLU B  478  1                                  20    
HELIX   14  14 ASP B  497  ASN B  514  1                                  18    
HELIX   15  15 GLU B  515  ASP B  520  5                                   6    
HELIX   16  16 GLY A  161  ARG A  176  1                                  16    
HELIX   17  17 SER A  180  CYS A  199  1                                  20    
HELIX   18  18 LEU A  262  GLN A  264  5                                   3    
HELIX   19  19 SER A  272  ASN A  289  1                                  18    
HELIX   20  20 PRO A  331  GLN A  335  5                                   5    
HELIX   21  21 SER A  345  LEU A  354  1                                  10    
HELIX   22  22 PHE A  379  ASN A  389  1                                  11    
HELIX   23  23 CYS A  405  PHE A  424  1                                  20    
HELIX   24  24 SER A  434  ASN A  449  1                                  16    
HELIX   25  25 GLN A  451  TRP A  455  5                                   5    
HELIX   26  26 ASP A  456  LYS A  458  5                                   3    
HELIX   27  27 ASP A  459  GLU A  478  1                                  20    
HELIX   28  28 ASP A  497  ASN A  514  1                                  18    
HELIX   29  29 PHE A  516  ASP A  520  5                                   5    
SHEET    1   A 7 VAL B 206  LEU B 209  0                                        
SHEET    2   A 7 GLU B 225  GLU B 233 -1  O  MSE B 229   N  LEU B 209           
SHEET    3   A 7 ILE B 316  SER B 326  1  O  ALA B 323   N  PHE B 230           
SHEET    4   A 7 PHE B 357  PRO B 361 -1  O  PHE B 357   N  SER B 326           
SHEET    5   A 7 TRP B 375  SER B 378 -1  O  ARG B 376   N  VAL B 360           
SHEET    6   A 7 TYR B 248  PHE B 253 -1  N  TYR B 249   O  TRP B 375           
SHEET    7   A 7 ILE B 237  GLU B 241 -1  N  GLU B 240   O  PHE B 250           
SHEET    1   B 5 VAL B 206  LEU B 209  0                                        
SHEET    2   B 5 GLU B 225  GLU B 233 -1  O  MSE B 229   N  LEU B 209           
SHEET    3   B 5 ILE B 316  SER B 326  1  O  ALA B 323   N  PHE B 230           
SHEET    4   B 5 VAL B 308  ILE B 312 -1  N  LEU B 310   O  VAL B 318           
SHEET    5   B 5 VAL B 296  LYS B 299 -1  N  ILE B 297   O  LEU B 311           
SHEET    1   C 2 LEU B 266  GLU B 267  0                                        
SHEET    2   C 2 ILE B 270  LEU B 271 -1  O  ILE B 270   N  GLU B 267           
SHEET    1   D 7 VAL A 206  LEU A 209  0                                        
SHEET    2   D 7 GLU A 225  GLU A 233 -1  O  LYS A 231   N  GLY A 207           
SHEET    3   D 7 ILE A 316  SER A 326  1  O  ASP A 319   N  VAL A 228           
SHEET    4   D 7 PHE A 357  PRO A 361 -1  O  PHE A 357   N  SER A 326           
SHEET    5   D 7 TRP A 375  SER A 378 -1  O  ARG A 376   N  VAL A 360           
SHEET    6   D 7 TYR A 248  PHE A 253 -1  N  TYR A 249   O  TRP A 375           
SHEET    7   D 7 ILE A 237  GLU A 241 -1  N  GLU A 240   O  PHE A 250           
SHEET    1   E 5 VAL A 206  LEU A 209  0                                        
SHEET    2   E 5 GLU A 225  GLU A 233 -1  O  LYS A 231   N  GLY A 207           
SHEET    3   E 5 ILE A 316  SER A 326  1  O  ASP A 319   N  VAL A 228           
SHEET    4   E 5 VAL A 308  ILE A 312 -1  N  VAL A 308   O  ILE A 320           
SHEET    5   E 5 VAL A 296  LYS A 299 -1  N  ILE A 297   O  LEU A 311           
SHEET    1   F 2 LEU A 266  GLU A 267  0                                        
SHEET    2   F 2 ILE A 270  LEU A 271 -1  O  ILE A 270   N  GLU A 267           
LINK         C   GLY B 184                 N   MSE B 185     1555   1555  1.33  
LINK         C   MSE 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  1.33  
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   MSE B 413     1555   1555  1.33  
LINK         C   MSE B 413                 N   LYS B 414     1555   1555  1.33  
LINK         C   GLY A 184                 N   MSE A 185     1555   1555  1.33  
LINK         C   MSE A 185                 N   VAL A 186     1555   1555  1.33  
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   MSE A 413     1555   1555  1.33  
LINK         C   MSE A 413                 N   LYS A 414     1555   1555  1.33  
LINK         NE2 HIS A 390                ZN    ZN A 601     1555   1555  2.09  
LINK         NE2 HIS B 390                ZN    ZN B 601     1555   1555  2.11  
LINK         SG  CYS B 396                ZN    ZN B 601     1555   1555  2.30  
LINK         SG  CYS A 396                ZN    ZN A 601     1555   1555  2.33  
LINK         SG  CYS B 397                ZN    ZN B 601     1555   1555  2.33  
LINK         SG  CYS A 397                ZN    ZN A 601     1555   1555  2.33  
LINK         SG  CYS A 404                ZN    ZN A 601     1555   1555  2.34  
LINK         SG  CYS B 404                ZN    ZN B 601     1555   1555  2.39  
CISPEP   1 THR A  211    GLY A  212          0        -2.09                     
SITE     1 AC1  4 HIS B 390  CYS B 396  CYS B 397  CYS B 404                    
SITE     1 AC2  4 HIS A 390  CYS A 396  CYS A 397  CYS A 404                    
CRYST1   46.815  111.480   76.414  90.00  92.73  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.021361  0.000000  0.001018        0.00000                         
SCALE2      0.000000  0.008970  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013101        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system