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Database: PDB
Entry: 6CC2
LinkDB: 6CC2
Original site: 6CC2 
HEADER    CELL CYCLE                              05-FEB-18   6CC2              
TITLE     CRYSTAL STRUCTURE OF CDC45 FROM ENTAMOEBA HISTOLYTICA                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION CONTROL PROTEIN 45 CDC45 PUTATIVE;           
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ENTAMOEBA HISTOLYTICA;                          
SOURCE   3 ORGANISM_TAXID: 5759;                                                
SOURCE   4 GENE: CL6EHI_049900;                                                 
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CELL DIVISION CONTROL PROTEIN, CELL CYCLE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.SHI,F.KURNIAWAN,K.KURAHASHI,A.BIELINSKY,H.AIHARA                    
REVDAT   2   01-JAN-20 6CC2    1       REMARK                                   
REVDAT   1   27-JUN-18 6CC2    0                                                
JRNL        AUTH   F.KURNIAWAN,K.SHI,K.KURAHASHI,A.K.BIELINSKY,H.AIHARA         
JRNL        TITL   CRYSTAL STRUCTURE OFENTAMOEBA HISTOLYTICACDC45 SUGGESTS A    
JRNL        TITL 2 CONFORMATIONAL SWITCH THAT MAY REGULATE DNA REPLICATION.     
JRNL        REF    ISCIENCE                      V.   3   102 2018              
JRNL        REFN                   ESSN 2589-0042                               
JRNL        PMID   29901028                                                     
JRNL        DOI    10.1016/J.ISCI.2018.04.011                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.66 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (DEV_3063: ???)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.66                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.09                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 107361                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.159                           
REMARK   3   R VALUE            (WORKING SET) : 0.157                           
REMARK   3   FREE R VALUE                     : 0.191                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5435                            
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 37.0994 -  5.1536    0.93     3373   157  0.1698 0.2168        
REMARK   3     2  5.1536 -  4.0923    0.94     3361   190  0.1223 0.1415        
REMARK   3     3  4.0923 -  3.5755    0.96     3425   175  0.1258 0.1628        
REMARK   3     4  3.5755 -  3.2488    0.96     3441   179  0.1389 0.1926        
REMARK   3     5  3.2488 -  3.0160    0.97     3461   197  0.1513 0.1796        
REMARK   3     6  3.0160 -  2.8383    0.94     3358   185  0.1522 0.1846        
REMARK   3     7  2.8383 -  2.6962    0.95     3414   203  0.1482 0.1751        
REMARK   3     8  2.6962 -  2.5788    0.96     3465   172  0.1426 0.1789        
REMARK   3     9  2.5788 -  2.4796    0.98     3485   190  0.1463 0.1844        
REMARK   3    10  2.4796 -  2.3940    0.96     3469   178  0.1474 0.2012        
REMARK   3    11  2.3940 -  2.3192    0.97     3469   186  0.1460 0.1851        
REMARK   3    12  2.3192 -  2.2529    0.92     3341   180  0.1518 0.1812        
REMARK   3    13  2.2529 -  2.1936    0.97     3453   188  0.1474 0.1682        
REMARK   3    14  2.1936 -  2.1401    0.95     3390   200  0.1508 0.2022        
REMARK   3    15  2.1401 -  2.0914    0.98     3510   206  0.1621 0.1928        
REMARK   3    16  2.0914 -  2.0469    0.97     3474   166  0.1592 0.1771        
REMARK   3    17  2.0469 -  2.0060    0.93     3349   185  0.1580 0.1766        
REMARK   3    18  2.0060 -  1.9681    0.96     3437   172  0.1656 0.1772        
REMARK   3    19  1.9681 -  1.9330    0.93     3365   167  0.1768 0.2469        
REMARK   3    20  1.9330 -  1.9002    0.90     3246   160  0.2026 0.2229        
REMARK   3    21  1.9002 -  1.8696    0.95     3372   199  0.2165 0.2651        
REMARK   3    22  1.8696 -  1.8408    0.92     3324   178  0.2279 0.2847        
REMARK   3    23  1.8408 -  1.8137    0.94     3387   166  0.2285 0.2249        
REMARK   3    24  1.8137 -  1.7882    0.96     3458   180  0.2301 0.2687        
REMARK   3    25  1.7882 -  1.7640    0.95     3379   180  0.2334 0.2544        
REMARK   3    26  1.7640 -  1.7411    0.94     3441   185  0.2520 0.2393        
REMARK   3    27  1.7411 -  1.7194    0.95     3419   155  0.2592 0.2941        
REMARK   3    28  1.7194 -  1.6986    0.94     3316   180  0.2710 0.2840        
REMARK   3    29  1.6986 -  1.6789    0.92     3312   208  0.2866 0.3196        
REMARK   3    30  1.6789 -  1.6600    0.89     3232   168  0.2975 0.3083        
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)     : 0.180            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.110           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           4220                                  
REMARK   3   ANGLE     :  0.748           5677                                  
REMARK   3   CHIRALITY :  0.051            630                                  
REMARK   3   PLANARITY :  0.006            708                                  
REMARK   3   DIHEDRAL  : 11.793           2510                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 123 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  35.4157 -21.0860 155.5166              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1870 T22:   0.1459                                     
REMARK   3      T33:   0.2625 T12:  -0.0000                                     
REMARK   3      T13:   0.0436 T23:  -0.0124                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8245 L22:   2.4613                                     
REMARK   3      L33:   3.0530 L12:  -0.2252                                     
REMARK   3      L13:  -0.0740 L23:  -0.1956                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0654 S12:  -0.0062 S13:  -0.3641                       
REMARK   3      S21:  -0.0012 S22:  -0.0122 S23:   0.0661                       
REMARK   3      S31:   0.4812 S32:   0.0332 S33:   0.0359                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 124 THROUGH 213 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  41.8727 -10.5609 147.2512              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1101 T22:   0.2101                                     
REMARK   3      T33:   0.1867 T12:  -0.0142                                     
REMARK   3      T13:   0.0416 T23:  -0.0211                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1758 L22:   2.9101                                     
REMARK   3      L33:   3.5846 L12:  -0.0722                                     
REMARK   3      L13:   0.2696 L23:   0.3886                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0260 S12:  -0.0232 S13:  -0.1694                       
REMARK   3      S21:  -0.0636 S22:  -0.0234 S23:  -0.2073                       
REMARK   3      S31:   0.2832 S32:   0.1750 S33:   0.0627                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 214 THROUGH 417 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  32.1610   9.2739 141.4502              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1512 T22:   0.2119                                     
REMARK   3      T33:   0.1210 T12:  -0.0213                                     
REMARK   3      T13:   0.0070 T23:  -0.0158                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8925 L22:   1.6527                                     
REMARK   3      L33:   1.0367 L12:  -0.1557                                     
REMARK   3      L13:  -0.1246 L23:  -0.3769                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0361 S12:   0.1493 S13:   0.0746                       
REMARK   3      S21:  -0.1155 S22:   0.0214 S23:  -0.0335                       
REMARK   3      S31:  -0.1478 S32:  -0.0035 S33:  -0.0614                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 418 THROUGH 542 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  26.3024   7.2188 169.9778              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1483 T22:   0.1492                                     
REMARK   3      T33:   0.1499 T12:   0.0055                                     
REMARK   3      T13:   0.0226 T23:  -0.0154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6019 L22:   2.0911                                     
REMARK   3      L33:   2.3575 L12:   0.3995                                     
REMARK   3      L13:  -0.7723 L23:   0.2053                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0730 S12:  -0.0840 S13:  -0.1946                       
REMARK   3      S21:   0.1881 S22:  -0.0384 S23:   0.1234                       
REMARK   3      S31:   0.0626 S32:  -0.0203 S33:   0.1090                       
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 6CC2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000232521.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUL-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97880                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57872                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.660                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : 0.06800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.90500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: AUTOSOL                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.27                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM THIOCYANATE (PH 6.9),             
REMARK 280  POLYETHYLENEGLYCOL 3,350, VAPOR DIFFUSION, SITTING DROP,            
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       19.56000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       85.80000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.90500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       85.80000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       19.56000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.90500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLN A   131                                                      
REMARK 465     GLN A   132                                                      
REMARK 465     PHE A   133                                                      
REMARK 465     ILE A   134                                                      
REMARK 465     GLU A   135                                                      
REMARK 465     GLN A   136                                                      
REMARK 465     GLU A   137                                                      
REMARK 465     THR A   138                                                      
REMARK 465     GLN A   139                                                      
REMARK 465     LEU A   140                                                      
REMARK 465     GLU A   141                                                      
REMARK 465     LYS A   142                                                      
REMARK 465     SER A   143                                                      
REMARK 465     ASP A   144                                                      
REMARK 465     LEU A   145                                                      
REMARK 465     LEU A   146                                                      
REMARK 465     GLU A   147                                                      
REMARK 465     VAL A   148                                                      
REMARK 465     ASP A   149                                                      
REMARK 465     ASP A   150                                                      
REMARK 465     ASP A   151                                                      
REMARK 465     LEU A   152                                                      
REMARK 465     ILE A   153                                                      
REMARK 465     GLY A   154                                                      
REMARK 465     LEU A   155                                                      
REMARK 465     ASN A   156                                                      
REMARK 465     LYS A   157                                                      
REMARK 465     SER A   158                                                      
REMARK 465     GLN A   159                                                      
REMARK 465     SER A   160                                                      
REMARK 465     PHE A   161                                                      
REMARK 465     ASN A   162                                                      
REMARK 465     ASN A   163                                                      
REMARK 465     CYS A   164                                                      
REMARK 465     GLU A   165                                                      
REMARK 465     TYR A   166                                                      
REMARK 465     ILE A   167                                                      
REMARK 465     ARG A   168                                                      
REMARK 465     LYS A   169                                                      
REMARK 465     MSE A   170                                                      
REMARK 465     ILE A   543                                                      
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   C    LYS A   538     H    CME A   539              1.60            
REMARK 500   OE2  GLU A   476     O    HOH A   701              1.93            
REMARK 500   O    HOH A   865     O    HOH A  1043              1.95            
REMARK 500   O    HOH A   763     O    HOH A  1030              2.01            
REMARK 500   O    HOH A  1043     O    HOH A  1065              2.05            
REMARK 500   O    HOH A   935     O    HOH A  1076              2.06            
REMARK 500   O    HOH A  1016     O    HOH A  1064              2.07            
REMARK 500   NZ   LYS A   320     O    HOH A   702              2.09            
REMARK 500   OD1  ASP A    76     O    HOH A   703              2.09            
REMARK 500   O    HOH A   808     O    HOH A  1077              2.10            
REMARK 500   O2   EDO A   601     O    HOH A   704              2.12            
REMARK 500   O    HOH A  1071     O    HOH A  1075              2.12            
REMARK 500   O    HOH A   977     O    HOH A  1039              2.12            
REMARK 500   O    HOH A   883     O    HOH A   939              2.14            
REMARK 500   O    HOH A  1002     O    HOH A  1093              2.14            
REMARK 500   O    HOH A   976     O    HOH A   994              2.14            
REMARK 500   O    HOH A   976     O    HOH A   990              2.16            
REMARK 500   O    HOH A  1064     O    HOH A  1097              2.16            
REMARK 500   O    HOH A   915     O    HOH A   976              2.17            
REMARK 500   O    HOH A   870     O    HOH A  1043              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  86      -22.29     83.29                                   
REMARK 500    ASP A  97      104.56    -55.05                                   
REMARK 500    SER A 179     -144.75   -112.62                                   
REMARK 500    TRP A 265     -144.29   -143.50                                   
REMARK 500    ASN A 336        1.14    -69.20                                   
REMARK 500    SER A 516     -167.68   -119.00                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1101        DISTANCE =  6.24 ANGSTROMS                       
REMARK 525    HOH A1102        DISTANCE =  6.63 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 614                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 615                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 616                 
DBREF1 6CC2 A    1   543  UNP                  A0A175JFA5_ENTHI                 
DBREF2 6CC2 A     A0A175JFA5                          1         543             
SEQRES   1 A  543  MSE ILE ILE ASN GLY THR SER PHE GLU GLU LEU TYR ASN          
SEQRES   2 A  543  GLY LEU ARG ASN ARG GLY LYS ASP LYS LYS THR ILE GLN          
SEQRES   3 A  543  LEU TYR VAL SER PRO THR VAL ASP ALA ILE VAL CYS TYR          
SEQRES   4 A  543  LYS ILE LEU SER MSE MSE PHE GLU LYS ASP GLY LEU LEU          
SEQRES   5 A  543  HIS SER ALA VAL PRO VAL ASN ASN TYR GLU THR LEU SER          
SEQRES   6 A  543  ARG VAL PHE LYS GLU THR ILE GLY HIS THR ASP VAL HIS          
SEQRES   7 A  543  THR VAL PHE PHE ILE ASP CYS ALA GLY SER ILE ASP VAL          
SEQRES   8 A  543  SER GLU LEU LEU GLY ASP ILE GLU ASN ILE PHE VAL TYR          
SEQRES   9 A  543  ILE ILE ASP SER HIS ARG PRO PHE ASN LYS LEU ASN VAL          
SEQRES  10 A  543  THR ASN THR ASN ILE GLY LEU ILE THR SER ASN GLU TYR          
SEQRES  11 A  543  GLN GLN PHE ILE GLU GLN GLU THR GLN LEU GLU LYS SER          
SEQRES  12 A  543  ASP LEU LEU GLU VAL ASP ASP ASP LEU ILE GLY LEU ASN          
SEQRES  13 A  543  LYS SER GLN SER PHE ASN ASN CYS GLU TYR ILE ARG LYS          
SEQRES  14 A  543  MSE VAL ASP SER ASP GLY GLU PHE TYR SER GLU SER VAL          
SEQRES  15 A  543  GLY ARG VAL ALA LEU ALA ILE ALA LYS LYS LEU ASN LYS          
SEQRES  16 A  543  VAL GLU ASN ASP MSE TYR TRP TYR ALA ALA ILE GLY VAL          
SEQRES  17 A  543  CYS ASP GLN TYR ILE SER LEU LYS ILE ASN ALA LYS THR          
SEQRES  18 A  543  TYR VAL HIS ALA ILE GLN TYR PHE ILE ASP ASN LEU GLN          
SEQRES  19 A  543  LEU GLU THR LEU GLU ILE THR ASP LEU LEU GLN THR VAL          
SEQRES  20 A  543  LYS THR PRO MSE CYS VAL LYS MSE ASP CYS GLN LEU MSE          
SEQRES  21 A  543  LEU LEU ARG HIS TRP THR LEU TYR ASP SER LEU PHE HIS          
SEQRES  22 A  543  THR ARG GLU ILE ALA SER LYS LEU GLY ILE TRP THR SER          
SEQRES  23 A  543  ARG GLY LYS GLU LYS PHE ASP VAL LEU ILE ALA ASP MSE          
SEQRES  24 A  543  GLY ILE PRO LEU SER GLN ALA GLN GLN SER TYR LYS THR          
SEQRES  25 A  543  MSE SER LEU GLU MSE LYS ASN LYS PHE LEU LEU LYS MSE          
SEQRES  26 A  543  GLU GLY TYR SER LYS PHE TYR HIS PHE GLU ASN LEU PHE          
SEQRES  27 A  543  LEU PRO SER PHE PHE LYS LYS PHE GLY MSE ASP TYR SER          
SEQRES  28 A  543  ILE SER ALA PHE ASP ALA ALA HIS ALA ILE GLY SER ILE          
SEQRES  29 A  543  ILE THR ASN ASP GLU PRO ASP GLN ASN TRP GLN GLN GLN          
SEQRES  30 A  543  PHE TRP GLU GLY PHE LYS LEU LEU SER SER THR THR ALA          
SEQRES  31 A  543  GLU PRO TYR ASP PHE GLY PHE ALA LYS CYS ILE GLU SER          
SEQRES  32 A  543  ASN LYS ASN LEU VAL GLU THR GLY ILE ILE LEU LEU LEU          
SEQRES  33 A  543  SER GLY SER CYS PHE ASN GLU ALA ASN LYS TYR ARG PHE          
SEQRES  34 A  543  CYS SER VAL SER ASP GLU LEU LEU SER ILE ARG PHE LYS          
SEQRES  35 A  543  THR PRO TYR LYS ALA LEU GLN LEU ALA GLN PHE LEU ALA          
SEQRES  36 A  543  GLU ALA SER SER ARG ARG TYR LYS LYS TRP LEU PRO PHE          
SEQRES  37 A  543  ILE LEU ALA VAL LEU ASP ALA GLU LYS LYS THR PHE VAL          
SEQRES  38 A  543  ILE VAL GLY TYR SER SER PRO ILE SER VAL LYS THR LEU          
SEQRES  39 A  543  ASN TYR PHE GLY ALA LYS PHE THR GLN THR ALA GLN ASN          
SEQRES  40 A  543  MSE LYS ILE SER ILE LEU GLN LYS SER PHE ASP SER PHE          
SEQRES  41 A  543  VAL THR GLU ILE HIS ARG GLU ASN LEU VAL LYS TYR LYS          
SEQRES  42 A  543  LYS ALA LEU HIS LYS CME PHE THR SER ILE                      
MODRES 6CC2 MSE A    1  MET  MODIFIED RESIDUE                                   
MODRES 6CC2 MSE A   44  MET  MODIFIED RESIDUE                                   
MODRES 6CC2 MSE A   45  MET  MODIFIED RESIDUE                                   
MODRES 6CC2 MSE A  200  MET  MODIFIED RESIDUE                                   
MODRES 6CC2 MSE A  251  MET  MODIFIED RESIDUE                                   
MODRES 6CC2 MSE A  255  MET  MODIFIED RESIDUE                                   
MODRES 6CC2 MSE A  260  MET  MODIFIED RESIDUE                                   
MODRES 6CC2 MSE A  299  MET  MODIFIED RESIDUE                                   
MODRES 6CC2 MSE A  313  MET  MODIFIED RESIDUE                                   
MODRES 6CC2 MSE A  317  MET  MODIFIED RESIDUE                                   
MODRES 6CC2 MSE A  325  MET  MODIFIED RESIDUE                                   
MODRES 6CC2 MSE A  348  MET  MODIFIED RESIDUE                                   
MODRES 6CC2 MSE A  508  MET  MODIFIED RESIDUE                                   
MODRES 6CC2 CME A  539  CYS  MODIFIED RESIDUE                                   
HET    MSE  A   1       9                                                       
HET    MSE  A  44      10                                                       
HET    MSE  A  45      10                                                       
HET    MSE  A 200      17                                                       
HET    MSE  A 251      17                                                       
HET    MSE  A 255      17                                                       
HET    MSE  A 260      17                                                       
HET    MSE  A 299      17                                                       
HET    MSE  A 313      17                                                       
HET    MSE  A 317      17                                                       
HET    MSE  A 325      10                                                       
HET    MSE  A 348      17                                                       
HET    MSE  A 508      17                                                       
HET    CME  A 539      19                                                       
HET    EDO  A 601      10                                                       
HET    EDO  A 602      10                                                       
HET    EDO  A 603      10                                                       
HET    EDO  A 604      10                                                       
HET    EDO  A 605      10                                                       
HET    EDO  A 606      10                                                       
HET    EDO  A 607      10                                                       
HET    EDO  A 608      10                                                       
HET    EDO  A 609      10                                                       
HET    EDO  A 610      10                                                       
HET    EDO  A 611      10                                                       
HET    EDO  A 612      10                                                       
HET     CL  A 613       1                                                       
HET     CL  A 614       1                                                       
HET     CL  A 615       1                                                       
HET    PEG  A 616      17                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE                                 
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM      CL CHLORIDE ION                                                     
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  MSE    13(C5 H11 N O2 SE)                                           
FORMUL   1  CME    C5 H11 N O3 S2                                               
FORMUL   2  EDO    12(C2 H6 O2)                                                 
FORMUL  14   CL    3(CL 1-)                                                     
FORMUL  17  PEG    C4 H10 O3                                                    
FORMUL  18  HOH   *402(H2 O)                                                    
HELIX    1 AA1 ASN A    4  THR A    6  5                                   3    
HELIX    2 AA2 SER A    7  ASP A   21  1                                  15    
HELIX    3 AA3 THR A   32  ASP A   49  1                                  18    
HELIX    4 AA4 ASN A   60  ILE A   72  1                                  13    
HELIX    5 AA5 ASP A   90  GLY A   96  1                                   7    
HELIX    6 AA6 ASN A  113  ASN A  119  1                                   7    
HELIX    7 AA7 SER A  181  LEU A  193  1                                  13    
HELIX    8 AA8 ASN A  198  SER A  214  1                                  17    
HELIX    9 AA9 ASN A  218  GLN A  234  1                                  17    
HELIX   10 AB1 LEU A  261  TRP A  265  5                                   5    
HELIX   11 AB2 THR A  266  THR A  274  1                                   9    
HELIX   12 AB3 THR A  274  GLY A  282  1                                   9    
HELIX   13 AB4 ARG A  287  MSE A  299  1                                  13    
HELIX   14 AB5 PRO A  302  GLN A  307  1                                   6    
HELIX   15 AB6 SER A  314  TYR A  332  1                                  19    
HELIX   16 AB7 PHE A  334  ASN A  336  5                                   3    
HELIX   17 AB8 SER A  353  ILE A  365  1                                  13    
HELIX   18 AB9 ASN A  373  SER A  386  1                                  14    
HELIX   19 AC1 PRO A  392  GLY A  418  1                                  27    
HELIX   20 AC2 ASP A  434  LYS A  442  1                                   9    
HELIX   21 AC3 THR A  443  LYS A  463  1                                  21    
HELIX   22 AC4 SER A  487  LYS A  492  5                                   6    
HELIX   23 AC5 THR A  493  LYS A  509  1                                  17    
HELIX   24 AC6 ASN A  528  PHE A  540  1                                  13    
SHEET    1 AA1 6 ILE A   2  ILE A   3  0                                        
SHEET    2 AA1 6 ILE A 122  ILE A 125  1  O  LEU A 124   N  ILE A   3           
SHEET    3 AA1 6 PHE A 102  ILE A 106  1  N  ILE A 105   O  GLY A 123           
SHEET    4 AA1 6 VAL A  77  ILE A  83  1  N  VAL A  80   O  PHE A 102           
SHEET    5 AA1 6 THR A  24  VAL A  29  1  N  TYR A  28   O  PHE A  81           
SHEET    6 AA1 6 HIS A  53  PRO A  57  1  O  VAL A  56   N  LEU A  27           
SHEET    1 AA2 2 HIS A 109  ARG A 110  0                                        
SHEET    2 AA2 2 PHE A 177  TYR A 178 -1  O  PHE A 177   N  ARG A 110           
SHEET    1 AA3 3 THR A 237  LEU A 238  0                                        
SHEET    2 AA3 3 MSE A 251  CYS A 257  1  O  VAL A 253   N  LEU A 238           
SHEET    3 AA3 3 PHE A 338  LYS A 344 -1  O  PHE A 343   N  CYS A 252           
SHEET    1 AA4 6 SER A 419  GLU A 423  0                                        
SHEET    2 AA4 6 TYR A 427  VAL A 432 -1  O  PHE A 429   N  PHE A 421           
SHEET    3 AA4 6 PHE A 468  ASP A 474  1  O  ILE A 469   N  ARG A 428           
SHEET    4 AA4 6 THR A 479  TYR A 485 -1  O  THR A 479   N  ASP A 474           
SHEET    5 AA4 6 SER A 519  HIS A 525 -1  O  THR A 522   N  ILE A 482           
SHEET    6 AA4 6 GLN A 514  LYS A 515 -1  N  GLN A 514   O  VAL A 521           
SSBOND   1 CYS A  420    CYS A  430                          1555   1555  2.59  
LINK         C   MSE A   1                 N   ILE A   2     1555   1555  1.32  
LINK         C   SER A  43                 N   MSE A  44     1555   1555  1.32  
LINK         C   MSE A  44                 N   MSE A  45     1555   1555  1.33  
LINK         C   MSE A  45                 N   PHE A  46     1555   1555  1.34  
LINK         C   ASP A 199                 N   MSE A 200     1555   1555  1.33  
LINK         C   MSE A 200                 N   TYR A 201     1555   1555  1.33  
LINK         C   PRO A 250                 N   MSE A 251     1555   1555  1.33  
LINK         C   MSE A 251                 N   CYS A 252     1555   1555  1.33  
LINK         C   LYS A 254                 N   MSE A 255     1555   1555  1.33  
LINK         C   MSE A 255                 N   ASP A 256     1555   1555  1.33  
LINK         C   LEU A 259                 N   MSE A 260     1555   1555  1.32  
LINK         C   MSE A 260                 N   LEU A 261     1555   1555  1.34  
LINK         C   ASP A 298                 N   MSE A 299     1555   1555  1.33  
LINK         C   MSE A 299                 N   GLY A 300     1555   1555  1.33  
LINK         C   THR A 312                 N   MSE A 313     1555   1555  1.33  
LINK         C   MSE A 313                 N   SER A 314     1555   1555  1.33  
LINK         C   GLU A 316                 N   MSE A 317     1555   1555  1.33  
LINK         C   MSE A 317                 N   LYS A 318     1555   1555  1.34  
LINK         C   LYS A 324                 N   MSE A 325     1555   1555  1.34  
LINK         C   MSE A 325                 N   GLU A 326     1555   1555  1.33  
LINK         C   GLY A 347                 N   MSE A 348     1555   1555  1.33  
LINK         C   MSE A 348                 N   ASP A 349     1555   1555  1.32  
LINK         C   ASN A 507                 N   MSE A 508     1555   1555  1.33  
LINK         C   MSE A 508                 N   LYS A 509     1555   1555  1.33  
LINK         C   LYS A 538                 N   CME A 539     1555   1555  1.32  
LINK         C   CME A 539                 N   PHE A 540     1555   1555  1.31  
CISPEP   1 ARG A  110    PRO A  111          0        -6.43                     
SITE     1 AC1  5 ASN A 198  PRO A 250  MSE A 251  LYS A 320                    
SITE     2 AC1  5 HOH A 704                                                     
SITE     1 AC2  7 CYS A 420  PHE A 421  ASN A 422  ARG A 428                    
SITE     2 AC2  7 TYR A 462  ARG A 526  HOH A 912                               
SITE     1 AC3  4 MSE A 508  ILE A 524  HIS A 525  ASN A 528                    
SITE     1 AC4  8 TYR A 178  ILE A 217  THR A 221  GLU A 369                    
SITE     2 AC4  8 PRO A 370  ASP A 371  HOH A 923  HOH A 925                    
SITE     1 AC5  4 GLN A 375  EDO A 608  HOH A 706  HOH A 968                    
SITE     1 AC6  4 THR A 479  GLU A 523  HIS A 525  HOH A 890                    
SITE     1 AC7  3 LEU A 243  ARG A 263  TYR A 310                               
SITE     1 AC8  4 TYR A 130  GLN A 375  EDO A 605  HOH A 714                    
SITE     1 AC9  4 TYR A  39  GLU A  47  HIS A  53  PHE A 382                    
SITE     1 AD1  2 ASP A 256  ARG A 263                                          
SITE     1 AD2  3 LYS A 311  MSE A 313  LYS A 318                               
SITE     1 AD3  3 ARG A 460  LYS A 463  TRP A 465                               
SITE     1 AD4  1 ASN A 406                                                     
SITE     1 AD5  2 ASN A 336  HOH A 993                                          
SITE     1 AD6  8 ILE A 413  SER A 417  GLY A 418  ASN A 422                    
SITE     2 AD6  8 ALA A 424  ASN A 425  SER A 433  ASP A 434                    
CRYST1   39.120   73.810  171.600  90.00  90.00  90.00 P 21 21 21    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      0.025562  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013548  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005828        0.00000                         
HETATM    1  N   MSE A   1      46.825 -21.985 161.080  1.00 26.57           N  
ANISOU    1  N   MSE A   1     2715   3476   3904   1095     59    474       N  
HETATM    2  CA  MSE A   1      48.019 -21.962 160.236  1.00 35.85           C  
ANISOU    2  CA  MSE A   1     3707   4766   5148   1190     78    454       C  
HETATM    3  C   MSE A   1      47.820 -21.044 159.040  1.00 29.24           C  
ANISOU    3  C   MSE A   1     2800   3975   4333   1051    150    355       C  
HETATM    4  O   MSE A   1      46.689 -20.734 158.671  1.00 28.97           O  
ANISOU    4  O   MSE A   1     2884   3847   4276    922    196    297       O  
HETATM    5  CB  MSE A   1      48.368 -23.369 159.756  1.00 59.93           C  
ANISOU    5  CB  MSE A   1     6817   7697   8256   1397    158    474       C  
HETATM    6  CG  MSE A   1      47.291 -24.042 158.930  1.00 84.27           C  
ANISOU    6  CG  MSE A   1    10093  10570  11356   1358    277    403       C  
HETATM    7 SE   MSE A   1      47.852 -25.808 158.309  1.00110.51          SE  
ANISOU    7 SE   MSE A   1    13523  13716  14751   1631    377    409      SE  
HETATM    8  CE  MSE A   1      46.181 -26.372 157.472  1.00120.37           C  
ANISOU    8  CE  MSE A   1    15037  14700  15998   1474    482    300       C  
HETATM    9  HA  MSE A   1      48.766 -21.638 160.764  1.00 43.02           H  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system