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Database: PDB
Entry: 2XHY
LinkDB: 2XHY
Original site: 2XHY 
HEADER    HYDROLASE                               24-JUN-10   2XHY              
TITLE     CRYSTAL STRUCTURE OF E.COLI BGLA                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 6-PHOSPHO-BETA-GLUCOSIDASE BGLA;                           
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: BGLA;                                                       
COMPND   5 EC: 3.2.1.86                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K-12                                                         
KEYWDS    HYDROLASE, GLYCOSIDASE                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.TOTIR,C.ZUBIETA,N.ECHOLS,A.P.MAY,C.L.GEE,M.NANAO,T.ALBER            
REVDAT   2   28-MAR-12 2XHY    1       AUTHOR JRNL   REMARK VERSN               
REVDAT   1   06-JUL-11 2XHY    0                                                
JRNL        AUTH   M.TOTIR,N.ECHOLS,M.NANAO,C.L.GEE,A.MOSKALEVA,S.GRADIA,       
JRNL        AUTH 2 A.T.IAVARONE,J.M.BERGER,A.P.MAY,C.ZUBIETA,T.ALBER            
JRNL        TITL   MACRO-TO-MICRO STRUCTURAL PROTEOMICS: NATIVE SOURCE          
JRNL        TITL 2 PROTEINS FOR HIGH-THROUGHPUT CRYSTALLIZATION.                
JRNL        REF    PLOS ONE                      V.   7 32498 2012              
JRNL        REFN                   ISSN 1932-6203                               
JRNL        PMID   22393408                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0032498                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6_289)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.94                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.960                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 82815                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.00                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 4153                            
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 22.9412 -  7.0784    0.98     2794   149  0.1549 0.1635        
REMARK   3     2  7.0784 -  5.6459    0.98     2774   146  0.1535 0.2210        
REMARK   3     3  5.6459 -  4.9403    0.98     2767   141  0.1373 0.2102        
REMARK   3     4  4.9403 -  4.4923    0.98     2806   149  0.1170 0.1590        
REMARK   3     5  4.4923 -  4.1724    0.98     2752   140  0.1178 0.1712        
REMARK   3     6  4.1724 -  3.9277    0.98     2810   146  0.1186 0.1793        
REMARK   3     7  3.9277 -  3.7319    0.98     2754   141  0.1262 0.1848        
REMARK   3     8  3.7319 -  3.5700    0.98     2756   170  0.1259 0.1908        
REMARK   3     9  3.5700 -  3.4331    0.98     2763   145  0.1313 0.1996        
REMARK   3    10  3.4331 -  3.3150    0.98     2745   147  0.1568 0.2240        
REMARK   3    11  3.3150 -  3.2116    0.98     2767   148  0.1647 0.2493        
REMARK   3    12  3.2116 -  3.1200    0.98     2791   142  0.1682 0.2297        
REMARK   3    13  3.1200 -  3.0381    0.98     2725   144  0.1703 0.2370        
REMARK   3    14  3.0381 -  2.9641    0.98     2778   137  0.1754 0.2580        
REMARK   3    15  2.9641 -  2.8969    0.97     2758   138  0.1799 0.2656        
REMARK   3    16  2.8969 -  2.8353    0.97     2754   136  0.1891 0.2436        
REMARK   3    17  2.8353 -  2.7787    0.97     2829   127  0.1864 0.2533        
REMARK   3    18  2.7787 -  2.7264    0.97     2664   147  0.1957 0.3134        
REMARK   3    19  2.7264 -  2.6777    0.97     2813   134  0.1961 0.2570        
REMARK   3    20  2.6777 -  2.6324    0.97     2744   135  0.2070 0.2871        
REMARK   3    21  2.6324 -  2.5900    0.97     2761   147  0.1941 0.2773        
REMARK   3    22  2.5900 -  2.5502    0.97     2721   157  0.1956 0.2967        
REMARK   3    23  2.5502 -  2.5128    0.97     2742   156  0.2111 0.2989        
REMARK   3    24  2.5128 -  2.4774    0.97     2732   144  0.2321 0.3657        
REMARK   3    25  2.4774 -  2.4440    0.95     2723   144  0.2305 0.2976        
REMARK   3    26  2.4440 -  2.4123    0.83     2330   121  0.2231 0.3115        
REMARK   3    27  2.4123 -  2.3821    0.74     2070   129  0.2320 0.3293        
REMARK   3    28  2.3821 -  2.3535    0.68     1886   104  0.2303 0.2747        
REMARK   3    29  2.3535 -  2.3261    0.62     1739   100  0.2317 0.3204        
REMARK   3    30  2.3261 -  2.3000    0.57     1614    89  0.2394 0.3222        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3   K_SOL              : 0.35                                          
REMARK   3   B_SOL              : 34.76                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.360            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.280           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.95                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.10950                                             
REMARK   3    B22 (A**2) : 0.52690                                              
REMARK   3    B33 (A**2) : 0.58270                                              
REMARK   3    B12 (A**2) : 0.59920                                              
REMARK   3    B13 (A**2) : -0.67730                                             
REMARK   3    B23 (A**2) : 1.39060                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003          15755                                  
REMARK   3   ANGLE     :  0.704          21324                                  
REMARK   3   CHIRALITY :  0.054           2121                                  
REMARK   3   PLANARITY :  0.002           2763                                  
REMARK   3   DIHEDRAL  : 15.998           5613                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 2XHY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-JUL-10.                  
REMARK 100 THE PDBE ID CODE IS EBI-44306.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JAN-08                          
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               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.92004                            
REMARK 200  MONOCHROMATOR                  : SI                                 
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (QUANTUM 315R)                 
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 83032                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 22.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -10.000                            
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.7                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.14000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 66.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1XK6                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 34300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.5 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 34800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.4 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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     MET A     1                                                      
REMARK 465     ILE A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 465     GLY A   329                                                      
REMARK 465     ASP A   330                                                      
REMARK 465     ALA A   331                                                      
REMARK 465     ILE A   332                                                      
REMARK 465     SER A   333                                                      
REMARK 465     GLY A   334                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ILE B     2                                                      
REMARK 465     VAL B     3                                                      
REMARK 465     THR B   328                                                      
REMARK 465     GLY B   329                                                      
REMARK 465     ASP B   330                                                      
REMARK 465     ALA B   331                                                      
REMARK 465     ILE B   332                                                      
REMARK 465     SER B   333                                                      
REMARK 465     GLY B   334                                                      
REMARK 465     PHE B   335                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ILE C     2                                                      
REMARK 465     VAL C     3                                                      
REMARK 465     LYS C     4                                                      
REMARK 465     THR C   328                                                      
REMARK 465     GLY C   329                                                      
REMARK 465     ASP C   330                                                      
REMARK 465     ALA C   331                                                      
REMARK 465     ILE C   332                                                      
REMARK 465     SER C   333                                                      
REMARK 465     GLY C   334                                                      
REMARK 465     PHE C   335                                                      
REMARK 465     GLU C   336                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ILE D     2                                                      
REMARK 465     VAL D     3                                                      
REMARK 465     LYS D     4                                                      
REMARK 465     GLU D   325                                                      
REMARK 465     GLY D   326                                                      
REMARK 465     GLY D   327                                                      
REMARK 465     THR D   328                                                      
REMARK 465     GLY D   329                                                      
REMARK 465     ASP D   330                                                      
REMARK 465     ALA D   331                                                      
REMARK 465     ILE D   332                                                      
REMARK 465     SER D   333                                                      
REMARK 465     GLY D   334                                                      
REMARK 465     PHE D   335                                                      
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     ASP A 348    OD1  OD2                                            
REMARK 470     ASP B 348    OD1  OD2                                            
REMARK 470     LYS C   5    CG   CD   CE   NZ                                   
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    VAL A  23      -42.58   -130.07                                   
REMARK 500    ALA A  44     -174.26   -171.75                                   
REMARK 500    ALA A  66     -127.36     53.43                                   
REMARK 500    GLU A 136       38.53   -163.74                                   
REMARK 500    SER A 147     -147.82     62.17                                   
REMARK 500    THR A 177      -73.93    -83.62                                   
REMARK 500    GLU A 180       63.09     34.28                                   
REMARK 500    ASN A 233       97.61   -165.22                                   
REMARK 500    TYR A 317      -31.60   -137.03                                   
REMARK 500    GLU A 325     -122.12    -98.86                                   
REMARK 500    ASN A 378      124.99    173.20                                   
REMARK 500    ASP A 394       59.79    -98.20                                   
REMARK 500    VAL B  23      -39.75   -131.86                                   
REMARK 500    ALA B  66     -124.63     50.63                                   
REMARK 500    GLU B 136       43.13   -147.50                                   
REMARK 500    SER B 147     -150.05     67.20                                   
REMARK 500    THR B 177      -75.54    -82.85                                   
REMARK 500    GLU B 180       57.09     31.73                                   
REMARK 500    ASN B 233       98.56   -162.60                                   
REMARK 500    ASP B 354       77.51   -160.43                                   
REMARK 500    PHE B 374      104.58   -162.97                                   
REMARK 500    ASP B 394       66.44   -101.34                                   
REMARK 500    VAL C  23      -39.13   -130.14                                   
REMARK 500    ALA C  66     -129.44     44.12                                   
REMARK 500    ALA C  93      109.88    -55.15                                   
REMARK 500    GLU C 136       40.60   -157.90                                   
REMARK 500    SER C 147     -150.47     64.95                                   
REMARK 500    THR C 177      -79.25    -89.03                                   
REMARK 500    GLU C 180       54.21     32.30                                   
REMARK 500    ASN C 233       96.03   -168.38                                   
REMARK 500    TYR C 317      -33.76   -133.32                                   
REMARK 500    SER C 338     -167.01   -114.13                                   
REMARK 500    ASN C 378      145.04   -172.76                                   
REMARK 500    ASP C 394       60.85   -107.24                                   
REMARK 500    ALA D  66     -129.16     49.58                                   
REMARK 500    GLU D 136       39.91   -154.10                                   
REMARK 500    SER D 147     -151.26     62.79                                   
REMARK 500    THR D 177      -76.15    -76.73                                   
REMARK 500    GLU D 180       54.23     33.45                                   
REMARK 500    ASN D 233       90.67   -171.37                                   
REMARK 500    PRO D 234       -5.34    -58.34                                   
REMARK 500    ASN D 378      127.43   -171.15                                   
REMARK 500    ASP D 394       56.96   -104.08                                   
REMARK 500    TYR D 414      -61.55    -90.31                                   
REMARK 500    TYR D 422      112.78   -160.45                                   
REMARK 500    ASP D 429      133.05    -40.00                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "CA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A1480                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A1482                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A1483                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B1481                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B1482                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B1483                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1484                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1485                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B1486                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B1487                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR C1480                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR C1481                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR D1480                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR D1481                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR C1483                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR D1482                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR D1483                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR D1484                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR D1485                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1486                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR D1487                  
DBREF  2XHY A    1   479  UNP    Q46829   BGLA_ECOLI       1    479             
DBREF  2XHY B    1   479  UNP    Q46829   BGLA_ECOLI       1    479             
DBREF  2XHY C    1   479  UNP    Q46829   BGLA_ECOLI       1    479             
DBREF  2XHY D    1   479  UNP    Q46829   BGLA_ECOLI       1    479             
SEQRES   1 A  479  MET ILE VAL LYS LYS LEU THR LEU PRO LYS ASP PHE LEU          
SEQRES   2 A  479  TRP GLY GLY ALA VAL ALA ALA HIS GLN VAL GLU GLY GLY          
SEQRES   3 A  479  TRP ASN LYS GLY GLY LYS GLY PRO SER ILE CYS ASP VAL          
SEQRES   4 A  479  LEU THR GLY GLY ALA HIS GLY VAL PRO ARG GLU ILE THR          
SEQRES   5 A  479  LYS GLU VAL LEU PRO GLY LYS TYR TYR PRO ASN HIS GLU          
SEQRES   6 A  479  ALA VAL ASP PHE TYR GLY HIS TYR LYS GLU ASP ILE LYS          
SEQRES   7 A  479  LEU PHE ALA GLU MET GLY PHE LYS CYS PHE ARG THR SER          
SEQRES   8 A  479  ILE ALA TRP THR ARG ILE PHE PRO LYS GLY ASP GLU ALA          
SEQRES   9 A  479  GLN PRO ASN GLU GLU GLY LEU LYS PHE TYR ASP ASP MET          
SEQRES  10 A  479  PHE ASP GLU LEU LEU LYS TYR ASN ILE GLU PRO VAL ILE          
SEQRES  11 A  479  THR LEU SER HIS PHE GLU MET PRO LEU HIS LEU VAL GLN          
SEQRES  12 A  479  GLN TYR GLY SER TRP THR ASN ARG LYS VAL VAL ASP PHE          
SEQRES  13 A  479  PHE VAL ARG PHE ALA GLU VAL VAL PHE GLU ARG TYR LYS          
SEQRES  14 A  479  HIS LYS VAL LYS TYR TRP MET THR PHE ASN GLU ILE ASN          
SEQRES  15 A  479  ASN GLN ARG ASN TRP ARG ALA PRO LEU PHE GLY TYR CYS          
SEQRES  16 A  479  CYS SER GLY VAL VAL TYR THR GLU HIS GLU ASN PRO GLU          
SEQRES  17 A  479  GLU THR MET TYR GLN VAL LEU HIS HIS GLN PHE VAL ALA          
SEQRES  18 A  479  SER ALA LEU ALA VAL LYS ALA ALA ARG ARG ILE ASN PRO          
SEQRES  19 A  479  GLU MET LYS VAL GLY CYS MET LEU ALA MET VAL PRO LEU          
SEQRES  20 A  479  TYR PRO TYR SER CYS ASN PRO ASP ASP VAL MET PHE ALA          
SEQRES  21 A  479  GLN GLU SER MET ARG GLU ARG TYR VAL PHE THR ASP VAL          
SEQRES  22 A  479  GLN LEU ARG GLY TYR TYR PRO SER TYR VAL LEU ASN GLU          
SEQRES  23 A  479  TRP GLU ARG ARG GLY PHE ASN ILE LYS MET GLU ASP GLY          
SEQRES  24 A  479  ASP LEU ASP VAL LEU ARG GLU GLY THR CYS ASP TYR LEU          
SEQRES  25 A  479  GLY PHE SER TYR TYR MET THR ASN ALA VAL LYS ALA GLU          
SEQRES  26 A  479  GLY GLY THR GLY ASP ALA ILE SER GLY PHE GLU GLY SER          
SEQRES  27 A  479  VAL PRO ASN PRO TYR VAL LYS ALA SER ASP TRP GLY TRP          
SEQRES  28 A  479  GLN ILE ASP PRO VAL GLY LEU ARG TYR ALA LEU CYS GLU          
SEQRES  29 A  479  LEU TYR GLU ARG TYR GLN ARG PRO LEU PHE ILE VAL GLU          
SEQRES  30 A  479  ASN GLY PHE GLY ALA TYR ASP LYS VAL GLU GLU ASP GLY          
SEQRES  31 A  479  SER ILE ASN ASP ASP TYR ARG ILE ASP TYR LEU ARG ALA          
SEQRES  32 A  479  HIS ILE GLU GLU MET LYS LYS ALA VAL THR TYR ASP GLY          
SEQRES  33 A  479  VAL ASP LEU MET GLY TYR THR PRO TRP GLY CYS ILE ASP          
SEQRES  34 A  479  CYS VAL SER PHE THR THR GLY GLN TYR SER LYS ARG TYR          
SEQRES  35 A  479  GLY PHE ILE TYR VAL ASN LYS HIS ASP ASP GLY THR GLY          
SEQRES  36 A  479  ASP MET SER ARG SER ARG LYS LYS SER PHE ASN TRP TYR          
SEQRES  37 A  479  LYS GLU VAL ILE ALA SER ASN GLY GLU LYS LEU                  
SEQRES   1 B  479  MET ILE VAL LYS LYS LEU THR LEU PRO LYS ASP PHE LEU          
SEQRES   2 B  479  TRP GLY GLY ALA VAL ALA ALA HIS GLN VAL GLU GLY GLY          
SEQRES   3 B  479  TRP ASN LYS GLY GLY LYS GLY PRO SER ILE CYS ASP VAL          
SEQRES   4 B  479  LEU THR GLY GLY ALA HIS GLY VAL PRO ARG GLU ILE THR          
SEQRES   5 B  479  LYS GLU VAL LEU PRO GLY LYS TYR TYR PRO ASN HIS GLU          
SEQRES   6 B  479  ALA VAL ASP PHE TYR GLY HIS TYR LYS GLU ASP ILE LYS          
SEQRES   7 B  479  LEU PHE ALA GLU MET GLY PHE LYS CYS PHE ARG THR SER          
SEQRES   8 B  479  ILE ALA TRP THR ARG ILE PHE PRO LYS GLY ASP GLU ALA          
SEQRES   9 B  479  GLN PRO ASN GLU GLU GLY LEU LYS PHE TYR ASP ASP MET          
SEQRES  10 B  479  PHE ASP GLU LEU LEU LYS TYR ASN ILE GLU PRO VAL ILE          
SEQRES  11 B  479  THR LEU SER HIS PHE GLU MET PRO LEU HIS LEU VAL GLN          
SEQRES  12 B  479  GLN TYR GLY SER TRP THR ASN ARG LYS VAL VAL ASP PHE          
SEQRES  13 B  479  PHE VAL ARG PHE ALA GLU VAL VAL PHE GLU ARG TYR LYS          
SEQRES  14 B  479  HIS LYS VAL LYS TYR TRP MET THR PHE ASN GLU ILE ASN          
SEQRES  15 B  479  ASN GLN ARG ASN TRP ARG ALA PRO LEU PHE GLY TYR CYS          
SEQRES  16 B  479  CYS SER GLY VAL VAL TYR THR GLU HIS GLU ASN PRO GLU          
SEQRES  17 B  479  GLU THR MET TYR GLN VAL LEU HIS HIS GLN PHE VAL ALA          
SEQRES  18 B  479  SER ALA LEU ALA VAL LYS ALA ALA ARG ARG ILE ASN PRO          
SEQRES  19 B  479  GLU MET LYS VAL GLY CYS MET LEU ALA MET VAL PRO LEU          
SEQRES  20 B  479  TYR PRO TYR SER CYS ASN PRO ASP ASP VAL MET PHE ALA          
SEQRES  21 B  479  GLN GLU SER MET ARG GLU ARG TYR VAL PHE THR ASP VAL          
SEQRES  22 B  479  GLN LEU ARG GLY TYR TYR PRO SER TYR VAL LEU ASN GLU          
SEQRES  23 B  479  TRP GLU ARG ARG GLY PHE ASN ILE LYS MET GLU ASP GLY          
SEQRES  24 B  479  ASP LEU ASP VAL LEU ARG GLU GLY THR CYS ASP TYR LEU          
SEQRES  25 B  479  GLY PHE SER TYR TYR MET THR ASN ALA VAL LYS ALA GLU          
SEQRES  26 B  479  GLY GLY THR GLY ASP ALA ILE SER GLY PHE GLU GLY SER          
SEQRES  27 B  479  VAL PRO ASN PRO TYR VAL LYS ALA SER ASP TRP GLY TRP          
SEQRES  28 B  479  GLN ILE ASP PRO VAL GLY LEU ARG TYR ALA LEU CYS GLU          
SEQRES  29 B  479  LEU TYR GLU ARG TYR GLN ARG PRO LEU PHE ILE VAL GLU          
SEQRES  30 B  479  ASN GLY PHE GLY ALA TYR ASP LYS VAL GLU GLU ASP GLY          
SEQRES  31 B  479  SER ILE ASN ASP ASP TYR ARG ILE ASP TYR LEU ARG ALA          
SEQRES  32 B  479  HIS ILE GLU GLU MET LYS LYS ALA VAL THR TYR ASP GLY          
SEQRES  33 B  479  VAL ASP LEU MET GLY TYR THR PRO TRP GLY CYS ILE ASP          
SEQRES  34 B  479  CYS VAL SER PHE THR THR GLY GLN TYR SER LYS ARG TYR          
SEQRES  35 B  479  GLY PHE ILE TYR VAL ASN LYS HIS ASP ASP GLY THR GLY          
SEQRES  36 B  479  ASP MET SER ARG SER ARG LYS LYS SER PHE ASN TRP TYR          
SEQRES  37 B  479  LYS GLU VAL ILE ALA SER ASN GLY GLU LYS LEU                  
SEQRES   1 C  479  MET ILE VAL LYS LYS LEU THR LEU PRO LYS ASP PHE LEU          
SEQRES   2 C  479  TRP GLY GLY ALA VAL ALA ALA HIS GLN VAL GLU GLY GLY          
SEQRES   3 C  479  TRP ASN LYS GLY GLY LYS GLY PRO SER ILE CYS ASP VAL          
SEQRES   4 C  479  LEU THR GLY GLY ALA HIS GLY VAL PRO ARG GLU ILE THR          
SEQRES   5 C  479  LYS GLU VAL LEU PRO GLY LYS TYR TYR PRO ASN HIS GLU          
SEQRES   6 C  479  ALA VAL ASP PHE TYR GLY HIS TYR LYS GLU ASP ILE LYS          
SEQRES   7 C  479  LEU PHE ALA GLU MET GLY PHE LYS CYS PHE ARG THR SER          
SEQRES   8 C  479  ILE ALA TRP THR ARG ILE PHE PRO LYS GLY ASP GLU ALA          
SEQRES   9 C  479  GLN PRO ASN GLU GLU GLY LEU LYS PHE TYR ASP ASP MET          
SEQRES  10 C  479  PHE ASP GLU LEU LEU LYS TYR ASN ILE GLU PRO VAL ILE          
SEQRES  11 C  479  THR LEU SER HIS PHE GLU MET PRO LEU HIS LEU VAL GLN          
SEQRES  12 C  479  GLN TYR GLY SER TRP THR ASN ARG LYS VAL VAL ASP PHE          
SEQRES  13 C  479  PHE VAL ARG PHE ALA GLU VAL VAL PHE GLU ARG TYR LYS          
SEQRES  14 C  479  HIS LYS VAL LYS TYR TRP MET THR PHE ASN GLU ILE ASN          
SEQRES  15 C  479  ASN GLN ARG ASN TRP ARG ALA PRO LEU PHE GLY TYR CYS          
SEQRES  16 C  479  CYS SER GLY VAL VAL TYR THR GLU HIS GLU ASN PRO GLU          
SEQRES  17 C  479  GLU THR MET TYR GLN VAL LEU HIS HIS GLN PHE VAL ALA          
SEQRES  18 C  479  SER ALA LEU ALA VAL LYS ALA ALA ARG ARG ILE ASN PRO          
SEQRES  19 C  479  GLU MET LYS VAL GLY CYS MET LEU ALA MET VAL PRO LEU          
SEQRES  20 C  479  TYR PRO TYR SER CYS ASN PRO ASP ASP VAL MET PHE ALA          
SEQRES  21 C  479  GLN GLU SER MET ARG GLU ARG TYR VAL PHE THR ASP VAL          
SEQRES  22 C  479  GLN LEU ARG GLY TYR TYR PRO SER TYR VAL LEU ASN GLU          
SEQRES  23 C  479  TRP GLU ARG ARG GLY PHE ASN ILE LYS MET GLU ASP GLY          
SEQRES  24 C  479  ASP LEU ASP VAL LEU ARG GLU GLY THR CYS ASP TYR LEU          
SEQRES  25 C  479  GLY PHE SER TYR TYR MET THR ASN ALA VAL LYS ALA GLU          
SEQRES  26 C  479  GLY GLY THR GLY ASP ALA ILE SER GLY PHE GLU GLY SER          
SEQRES  27 C  479  VAL PRO ASN PRO TYR VAL LYS ALA SER ASP TRP GLY TRP          
SEQRES  28 C  479  GLN ILE ASP PRO VAL GLY LEU ARG TYR ALA LEU CYS GLU          
SEQRES  29 C  479  LEU TYR GLU ARG TYR GLN ARG PRO LEU PHE ILE VAL GLU          
SEQRES  30 C  479  ASN GLY PHE GLY ALA TYR ASP LYS VAL GLU GLU ASP GLY          
SEQRES  31 C  479  SER ILE ASN ASP ASP TYR ARG ILE ASP TYR LEU ARG ALA          
SEQRES  32 C  479  HIS ILE GLU GLU MET LYS LYS ALA VAL THR TYR ASP GLY          
SEQRES  33 C  479  VAL ASP LEU MET GLY TYR THR PRO TRP GLY CYS ILE ASP          
SEQRES  34 C  479  CYS VAL SER PHE THR THR GLY GLN TYR SER LYS ARG TYR          
SEQRES  35 C  479  GLY PHE ILE TYR VAL ASN LYS HIS ASP ASP GLY THR GLY          
SEQRES  36 C  479  ASP MET SER ARG SER ARG LYS LYS SER PHE ASN TRP TYR          
SEQRES  37 C  479  LYS GLU VAL ILE ALA SER ASN GLY GLU LYS LEU                  
SEQRES   1 D  479  MET ILE VAL LYS LYS LEU THR LEU PRO LYS ASP PHE LEU          
SEQRES   2 D  479  TRP GLY GLY ALA VAL ALA ALA HIS GLN VAL GLU GLY GLY          
SEQRES   3 D  479  TRP ASN LYS GLY GLY LYS GLY PRO SER ILE CYS ASP VAL          
SEQRES   4 D  479  LEU THR GLY GLY ALA HIS GLY VAL PRO ARG GLU ILE THR          
SEQRES   5 D  479  LYS GLU VAL LEU PRO GLY LYS TYR TYR PRO ASN HIS GLU          
SEQRES   6 D  479  ALA VAL ASP PHE TYR GLY HIS TYR LYS GLU ASP ILE LYS          
SEQRES   7 D  479  LEU PHE ALA GLU MET GLY PHE LYS CYS PHE ARG THR SER          
SEQRES   8 D  479  ILE ALA TRP THR ARG ILE PHE PRO LYS GLY ASP GLU ALA          
SEQRES   9 D  479  GLN PRO ASN GLU GLU GLY LEU LYS PHE TYR ASP ASP MET          
SEQRES  10 D  479  PHE ASP GLU LEU LEU LYS TYR ASN ILE GLU PRO VAL ILE          
SEQRES  11 D  479  THR LEU SER HIS PHE GLU MET PRO LEU HIS LEU VAL GLN          
SEQRES  12 D  479  GLN TYR GLY SER TRP THR ASN ARG LYS VAL VAL ASP PHE          
SEQRES  13 D  479  PHE VAL ARG PHE ALA GLU VAL VAL PHE GLU ARG TYR LYS          
SEQRES  14 D  479  HIS LYS VAL LYS TYR TRP MET THR PHE ASN GLU ILE ASN          
SEQRES  15 D  479  ASN GLN ARG ASN TRP ARG ALA PRO LEU PHE GLY TYR CYS          
SEQRES  16 D  479  CYS SER GLY VAL VAL TYR THR GLU HIS GLU ASN PRO GLU          
SEQRES  17 D  479  GLU THR MET TYR GLN VAL LEU HIS HIS GLN PHE VAL ALA          
SEQRES  18 D  479  SER ALA LEU ALA VAL LYS ALA ALA ARG ARG ILE ASN PRO          
SEQRES  19 D  479  GLU MET LYS VAL GLY CYS MET LEU ALA MET VAL PRO LEU          
SEQRES  20 D  479  TYR PRO TYR SER CYS ASN PRO ASP ASP VAL MET PHE ALA          
SEQRES  21 D  479  GLN GLU SER MET ARG GLU ARG TYR VAL PHE THR ASP VAL          
SEQRES  22 D  479  GLN LEU ARG GLY TYR TYR PRO SER TYR VAL LEU ASN GLU          
SEQRES  23 D  479  TRP GLU ARG ARG GLY PHE ASN ILE LYS MET GLU ASP GLY          
SEQRES  24 D  479  ASP LEU ASP VAL LEU ARG GLU GLY THR CYS ASP TYR LEU          
SEQRES  25 D  479  GLY PHE SER TYR TYR MET THR ASN ALA VAL LYS ALA GLU          
SEQRES  26 D  479  GLY GLY THR GLY ASP ALA ILE SER GLY PHE GLU GLY SER          
SEQRES  27 D  479  VAL PRO ASN PRO TYR VAL LYS ALA SER ASP TRP GLY TRP          
SEQRES  28 D  479  GLN ILE ASP PRO VAL GLY LEU ARG TYR ALA LEU CYS GLU          
SEQRES  29 D  479  LEU TYR GLU ARG TYR GLN ARG PRO LEU PHE ILE VAL GLU          
SEQRES  30 D  479  ASN GLY PHE GLY ALA TYR ASP LYS VAL GLU GLU ASP GLY          
SEQRES  31 D  479  SER ILE ASN ASP ASP TYR ARG ILE ASP TYR LEU ARG ALA          
SEQRES  32 D  479  HIS ILE GLU GLU MET LYS LYS ALA VAL THR TYR ASP GLY          
SEQRES  33 D  479  VAL ASP LEU MET GLY TYR THR PRO TRP GLY CYS ILE ASP          
SEQRES  34 D  479  CYS VAL SER PHE THR THR GLY GLN TYR SER LYS ARG TYR          
SEQRES  35 D  479  GLY PHE ILE TYR VAL ASN LYS HIS ASP ASP GLY THR GLY          
SEQRES  36 D  479  ASP MET SER ARG SER ARG LYS LYS SER PHE ASN TRP TYR          
SEQRES  37 D  479  LYS GLU VAL ILE ALA SER ASN GLY GLU LYS LEU                  
HET     BR  A1480       1                                                       
HET    SO4  A1481       5                                                       
HET     BR  A1482       1                                                       
HET     BR  A1483       1                                                       
HET     BR  B1480       1                                                       
HET     BR  B1481       1                                                       
HET     BR  B1482       1                                                       
HET     BR  B1483       1                                                       
HET    SO4  B1484       5                                                       
HET    SO4  B1485       5                                                       
HET     BR  B1486       1                                                       
HET     BR  B1487       1                                                       
HET     BR  C1480       1                                                       
HET     BR  C1481       1                                                       
HET    SO4  C1482       5                                                       
HET     BR  C1483       1                                                       
HET     BR  D1480       1                                                       
HET     BR  D1481       1                                                       
HET     BR  D1482       1                                                       
HET     BR  D1483       1                                                       
HET     BR  D1484       1                                                       
HET     BR  D1485       1                                                       
HET    SO4  D1486       5                                                       
HET     BR  D1487       1                                                       
HETNAM      BR BROMIDE ION                                                      
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5   BR    19(BR 1-)                                                    
FORMUL   6  SO4    5(O4 S 2-)                                                   
FORMUL   7  HOH   *1648(H2 O)                                                   
HELIX    1   1 ALA A   19  GLU A   24  1                                   6    
HELIX    2   2 TYR A   61  ALA A   66  1                                   6    
HELIX    3   3 ASP A   68  GLY A   84  1                                  17    
HELIX    4   4 ALA A   93  PHE A   98  1                                   6    
HELIX    5   5 ASN A  107  TYR A  124  1                                  18    
HELIX    6   6 PRO A  138  TYR A  145  1                                   8    
HELIX    7   7 GLY A  146  ASN A  150  5                                   5    
HELIX    8   8 ARG A  151  TYR A  168  1                                  18    
HELIX    9   9 ASN A  182  ASN A  186  5                                   5    
HELIX   10  10 LEU A  191  GLY A  198  1                                   8    
HELIX   11  11 VAL A  200  HIS A  204  5                                   5    
HELIX   12  12 ASN A  206  ASN A  233  1                                  28    
HELIX   13  13 ASN A  253  MET A  264  1                                  12    
HELIX   14  14 MET A  264  GLY A  277  1                                  14    
HELIX   15  15 PRO A  280  GLY A  291  1                                  12    
HELIX   16  16 GLY A  299  GLY A  307  1                                   9    
HELIX   17  17 ASP A  354  GLN A  370  1                                  17    
HELIX   18  18 ASP A  394  TYR A  414  1                                  21    
HELIX   19  19 LYS A  462  SER A  474  1                                  13    
HELIX   20  20 ALA B   19  GLU B   24  1                                   6    
HELIX   21  21 ILE B   36  VAL B   39  5                                   4    
HELIX   22  22 TYR B   61  ALA B   66  1                                   6    
HELIX   23  23 ASP B   68  GLY B   84  1                                  17    
HELIX   24  24 ALA B   93  PHE B   98  1                                   6    
HELIX   25  25 ASN B  107  TYR B  124  1                                  18    
HELIX   26  26 PRO B  138  GLY B  146  1                                   9    
HELIX   27  27 SER B  147  ASN B  150  5                                   4    
HELIX   28  28 ARG B  151  TYR B  168  1                                  18    
HELIX   29  29 GLU B  180  ASN B  186  5                                   7    
HELIX   30  30 LEU B  191  GLY B  198  1                                   8    
HELIX   31  31 VAL B  200  HIS B  204  5                                   5    
HELIX   32  32 ASN B  206  ASN B  233  1                                  28    
HELIX   33  33 ASN B  253  MET B  264  1                                  12    
HELIX   34  34 MET B  264  GLY B  277  1                                  14    
HELIX   35  35 PRO B  280  ARG B  290  1                                  11    
HELIX   36  36 GLY B  299  GLY B  307  1                                   9    
HELIX   37  37 ASP B  354  GLN B  370  1                                  17    
HELIX   38  38 ASP B  394  TYR B  414  1                                  21    
HELIX   39  39 LYS B  462  SER B  474  1                                  13    
HELIX   40  40 ALA C   19  GLU C   24  1                                   6    
HELIX   41  41 ASP C   68  GLY C   84  1                                  17    
HELIX   42  42 ALA C   93  PHE C   98  1                                   6    
HELIX   43  43 ASN C  107  TYR C  124  1                                  18    
HELIX   44  44 PRO C  138  GLY C  146  1                                   9    
HELIX   45  45 SER C  147  THR C  149  5                                   3    
HELIX   46  46 ASN C  150  TYR C  168  1                                  19    
HELIX   47  47 ASN C  182  ASN C  186  5                                   5    
HELIX   48  48 LEU C  191  GLY C  198  1                                   8    
HELIX   49  49 VAL C  200  HIS C  204  5                                   5    
HELIX   50  50 ASN C  206  ASN C  233  1                                  28    
HELIX   51  51 ASN C  253  MET C  264  1                                  12    
HELIX   52  52 MET C  264  GLY C  277  1                                  14    
HELIX   53  53 PRO C  280  GLY C  291  1                                  12    
HELIX   54  54 GLY C  299  GLY C  307  1                                   9    
HELIX   55  55 ASP C  354  GLN C  370  1                                  17    
HELIX   56  56 ASP C  394  TYR C  414  1                                  21    
HELIX   57  57 LYS C  462  SER C  474  1                                  13    
HELIX   58  58 ALA D   19  GLU D   24  1                                   6    
HELIX   59  59 ILE D   36  VAL D   39  5                                   4    
HELIX   60  60 TYR D   61  ALA D   66  1                                   6    
HELIX   61  61 ASP D   68  GLY D   84  1                                  17    
HELIX   62  62 ALA D   93  PHE D   98  1                                   6    
HELIX   63  63 ASN D  107  TYR D  124  1                                  18    
HELIX   64  64 PRO D  138  GLY D  146  1                                   9    
HELIX   65  65 SER D  147  ASN D  150  5                                   4    
HELIX   66  66 ARG D  151  TYR D  168  1                                  18    
HELIX   67  67 GLU D  180  ASN D  186  5                                   7    
HELIX   68  68 LEU D  191  GLY D  198  1                                   8    
HELIX   69  69 VAL D  200  HIS D  204  5                                   5    
HELIX   70  70 ASN D  206  ASN D  233  1                                  28    
HELIX   71  71 ASN D  253  MET D  264  1                                  12    
HELIX   72  72 MET D  264  GLY D  277  1                                  14    
HELIX   73  73 PRO D  280  GLY D  291  1                                  12    
HELIX   74  74 GLY D  299  GLY D  307  1                                   9    
HELIX   75  75 ASP D  354  GLN D  370  1                                  17    
HELIX   76  76 ASP D  394  TYR D  414  1                                  21    
HELIX   77  77 LYS D  462  SER D  474  1                                  13    
SHEET    1  AA 8 LEU A  13  TRP A  14  0                                        
SHEET    2  AA 8 LEU A 419  TYR A 422  1  O  MET A 420   N  LEU A  13           
SHEET    3  AA 8 LEU A 373  GLU A 377  1  O  LEU A 373   N  MET A 420           
SHEET    4  AA 8 LEU A 312  SER A 315  1  O  LEU A 312   N  PHE A 374           
SHEET    5  AA 8 LYS A 237  ALA A 243  1  O  CYS A 240   N  GLY A 313           
SHEET    6  AA 8 TYR A 174  PHE A 178  1  O  TRP A 175   N  GLY A 239           
SHEET    7  AA 8 GLU A 127  SER A 133  1  O  PRO A 128   N  TYR A 174           
SHEET    8  AA 8 CYS A  87  SER A  91  1  O  PHE A  88   N  VAL A 129           
SHEET    1  AB 3 LEU A 247  PRO A 249  0                                        
SHEET    2  AB 3 ASN A 320  VAL A 322  1  O  ASN A 320   N  TYR A 248           
SHEET    3  AB 3 SER A 338  VAL A 339 -1  O  VAL A 339   N  ALA A 321           
SHEET    1  AC 2 LYS A 345  ALA A 346  0                                        
SHEET    2  AC 2 GLN A 352  ILE A 353 -1  O  ILE A 353   N  LYS A 345           
SHEET    1  AD 2 ILE A 445  VAL A 447  0                                        
SHEET    2  AD 2 ARG A 459  ARG A 461 -1  O  SER A 460   N  TYR A 446           
SHEET    1  BA 8 LEU B  13  TRP B  14  0                                        
SHEET    2  BA 8 LEU B 419  TYR B 422  1  O  MET B 420   N  LEU B  13           
SHEET    3  BA 8 LEU B 373  GLU B 377  1  O  LEU B 373   N  MET B 420           
SHEET    4  BA 8 LEU B 312  SER B 315  1  O  LEU B 312   N  PHE B 374           
SHEET    5  BA 8 LYS B 237  ALA B 243  1  O  CYS B 240   N  GLY B 313           
SHEET    6  BA 8 TYR B 174  PHE B 178  1  O  TRP B 175   N  GLY B 239           
SHEET    7  BA 8 GLU B 127  SER B 133  1  O  PRO B 128   N  TYR B 174           
SHEET    8  BA 8 CYS B  87  SER B  91  1  O  PHE B  88   N  VAL B 129           
SHEET    1  BB 3 LEU B 247  PRO B 249  0                                        
SHEET    2  BB 3 ASN B 320  VAL B 322  1  O  ASN B 320   N  TYR B 248           
SHEET    3  BB 3 SER B 338  VAL B 339 -1  O  VAL B 339   N  ALA B 321           
SHEET    1  BC 2 ILE B 445  VAL B 447  0                                        
SHEET    2  BC 2 ARG B 459  ARG B 461 -1  O  SER B 460   N  TYR B 446           
SHEET    1  CA 9 LEU C  13  ALA C  17  0                                        
SHEET    2  CA 9 LEU C 419  TYR C 422  1  O  MET C 420   N  LEU C  13           
SHEET    3  CA 9 LEU C 373  GLU C 377  1  O  LEU C 373   N  MET C 420           
SHEET    4  CA 9 TYR C 311  SER C 315  1  O  LEU C 312   N  PHE C 374           
SHEET    5  CA 9 LYS C 237  ALA C 243  1  O  CYS C 240   N  GLY C 313           
SHEET    6  CA 9 TYR C 174  PHE C 178  1  O  TRP C 175   N  GLY C 239           
SHEET    7  CA 9 GLU C 127  SER C 133  1  O  PRO C 128   N  TYR C 174           
SHEET    8  CA 9 CYS C  87  SER C  91  1  O  PHE C  88   N  VAL C 129           
SHEET    9  CA 9 LEU C  13  ALA C  17  1  O  GLY C  16   N  ARG C  89           
SHEET    1  CB 2 LEU C 247  PRO C 249  0                                        
SHEET    2  CB 2 ASN C 320  VAL C 322  1  O  ASN C 320   N  TYR C 248           
SHEET    1  CC 2 ILE C 445  VAL C 447  0                                        
SHEET    2  CC 2 ARG C 459  ARG C 461 -1  O  SER C 460   N  TYR C 446           
SHEET    1  DA 9 LEU D  13  ALA D  17  0                                        
SHEET    2  DA 9 LEU D 419  TYR D 422  1  O  MET D 420   N  LEU D  13           
SHEET    3  DA 9 LEU D 373  GLU D 377  1  O  LEU D 373   N  MET D 420           
SHEET    4  DA 9 LEU D 312  SER D 315  1  O  LEU D 312   N  PHE D 374           
SHEET    5  DA 9 LYS D 237  ALA D 243  1  O  CYS D 240   N  GLY D 313           
SHEET    6  DA 9 TYR D 174  PHE D 178  1  O  TRP D 175   N  GLY D 239           
SHEET    7  DA 9 GLU D 127  SER D 133  1  O  PRO D 128   N  TYR D 174           
SHEET    8  DA 9 CYS D  87  SER D  91  1  O  PHE D  88   N  VAL D 129           
SHEET    9  DA 9 LEU D  13  ALA D  17  1  O  GLY D  16   N  ARG D  89           
SHEET    1  DB 3 LEU D 247  PRO D 249  0                                        
SHEET    2  DB 3 ASN D 320  VAL D 322  1  O  ASN D 320   N  TYR D 248           
SHEET    3  DB 3 SER D 338  VAL D 339 -1  O  VAL D 339   N  ALA D 321           
SHEET    1  DC 2 LYS D 345  ALA D 346  0                                        
SHEET    2  DC 2 GLN D 352  ILE D 353 -1  O  ILE D 353   N  LYS D 345           
SHEET    1  DD 2 ILE D 445  LYS D 449  0                                        
SHEET    2  DD 2 GLY D 455  ARG D 461 -1  N  ASP D 456   O  ASN D 448           
SITE     1 AC1  1 LYS A  53                                                     
SITE     1 AC2  9 TRP A 351  SER A 432  PHE A 433  THR A 434                    
SITE     2 AC2  9 LYS A 440  TYR A 442  HOH A2368  HOH A2369                    
SITE     3 AC2  9 HOH A2370                                                     
SITE     1 AC3  2 SER A 439  HIS A 450                                          
SITE     1 AC4  2 GLY A 299  LEU A 301                                          
SITE     1 AC5  1 ARG B 231                                                     
SITE     1 AC6  1 LYS B  53                                                     
SITE     1 AC7  2 PRO B 190  LEU B 191                                          
SITE     1 AC8 10 TRP B 351  SER B 432  PHE B 433  THR B 434                    
SITE     2 AC8 10 LYS B 440  TYR B 442  HOH B2354  HOH B2395                    
SITE     3 AC8 10 HOH B2396  HOH B2397                                          
SITE     1 AC9  4 LEU B 247  SER B 263  GLU B 336  HOH B2398                    
SITE     1 BC1  4 GLY B 299  ASP B 300  LEU B 301  HOH B2281                    
SITE     1 BC2  4 ASN B 206  GLU B 208  GLU B 209  PHE B 292                    
SITE     1 BC3  2 SER C 439  HIS C 450                                          
SITE     1 BC4  1 ALA C 104                                                     
SITE     1 BC5 10 TRP C 351  SER C 432  PHE C 433  THR C 434                    
SITE     2 BC5 10 LYS C 440  TYR C 442  HOH C2431  HOH C2477                    
SITE     3 BC5 10 HOH C2478  HOH C2479                                          
SITE     1 BC6  2 LYS D 410  TYR D 414                                          
SITE     1 BC7  2 GLU D 336  HOH D2292                                          
SITE     1 BC8  2 LYS C  53  LYS D 295                                          
SITE     1 BC9  4 SER D 439  HIS D 450  ASP D 451  HOH D2367                    
SITE     1 CC1  1 GLN D 144                                                     
SITE     1 CC2  2 PRO D 190  LEU D 191                                          
SITE     1 CC3  4 ASN D 206  GLU D 208  GLU D 209  HOH D2206                    
SITE     1 CC4  8 TRP D 351  PHE D 433  THR D 434  LYS D 440                    
SITE     2 CC4  8 TYR D 442  HOH D2398  HOH D2399  HOH D2400                    
SITE     1 CC5  3 GLY D 299  LEU D 301  HOH D2274                               
CRYST1   73.674   79.424   98.604  99.96 107.21 102.83 P 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      0.013573  0.003091  0.005169        0.00000                         
SCALE2      0.000000  0.012913  0.003423        0.00000                         
SCALE3      0.000000  0.000000  0.010984        0.00000                         
MTRIX1   1 -0.007992  0.623400 -0.781900       37.38000    1                    
MTRIX2   1  0.629300 -0.604500 -0.488400       62.28000    1                    
MTRIX3   1 -0.777100 -0.496000 -0.387500       97.55000    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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