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Database: PDB
Entry: 3ZOA
LinkDB: 3ZOA
Original site: 3ZOA 
HEADER    HYDROLASE                               21-FEB-13   3ZOA              
TITLE     THE STRUCTURE OF TREHALOSE SYNTHASE (TRES) OF MYCOBACTERIUM           
TITLE    2 SMEGMATIS IN COMPLEX WITH ACARBOSE                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TREHALOSE SYNTHASE/AMYLASE TRES;                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: MALTOSE ALPHA-D-GLUCOSYLTRANSFERASE, MTASE;                 
COMPND   5 EC: 3.2.1.1, 5.4.99.16                                               
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS;                        
SOURCE   3 ORGANISM_TAXID: 1772                                                 
KEYWDS    HYDROLASE, GLYCOHYDROLASE, DRUG DESIGN, TUBERCULOSIS                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.CANER,N.NGUYEN,A.AGUDA,R.ZHANG,Y.T.PAN,S.G.WITHERS,G.D.BRAYER       
REVDAT   2   07-AUG-13 3ZOA    1       JRNL                                     
REVDAT   1   17-JUL-13 3ZOA    0                                                
JRNL        AUTH   S.CANER,N.NGUYEN,A.AGUDA,R.ZHANG,Y.T.PAN,S.G.WITHERS,        
JRNL        AUTH 2 G.D.BRAYER                                                   
JRNL        TITL   THE STRUCTURE OF THE MYCOBACTERIUM SMEGMATIS TREHALOSE       
JRNL        TITL 2 SYNTHASE REVEALS AN UNUSUAL ACTIVE SITE CONFIGURATION AND    
JRNL        TITL 3 ACARBOSE-BINDING MODE.                                       
JRNL        REF    GLYCOBIOLOGY                  V.  23  1075 2013              
JRNL        REFN                   ISSN 0959-6658                               
JRNL        PMID   23735230                                                     
JRNL        DOI    10.1093/GLYCOB/CWT044                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.1_1168)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.816                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.99                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.98                          
REMARK   3   NUMBER OF REFLECTIONS             : 143053                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1658                          
REMARK   3   R VALUE            (WORKING SET) : 0.1650                          
REMARK   3   FREE R VALUE                     : 0.1981                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.5                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 3600                            
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 34.8224 -  5.4738    1.00     5538   145  0.1606 0.1816        
REMARK   3     2  5.4738 -  4.3474    1.00     5487   145  0.1334 0.1538        
REMARK   3     3  4.3474 -  3.7986    1.00     5457   139  0.1334 0.1623        
REMARK   3     4  3.7986 -  3.4517    1.00     5455   146  0.1461 0.1755        
REMARK   3     5  3.4517 -  3.2044    1.00     5475   141  0.1644 0.2106        
REMARK   3     6  3.2044 -  3.0156    1.00     5506   142  0.1733 0.1973        
REMARK   3     7  3.0156 -  2.8647    1.00     5464   140  0.1793 0.2180        
REMARK   3     8  2.8647 -  2.7400    1.00     5490   145  0.1737 0.2075        
REMARK   3     9  2.7400 -  2.6346    1.00     5488   140  0.1700 0.1931        
REMARK   3    10  2.6346 -  2.5437    1.00     5427   145  0.1744 0.2111        
REMARK   3    11  2.5437 -  2.4642    1.00     5457   137  0.1732 0.2230        
REMARK   3    12  2.4642 -  2.3938    1.00     5471   137  0.1750 0.2047        
REMARK   3    13  2.3938 -  2.3308    1.00     5480   143  0.1766 0.2347        
REMARK   3    14  2.3308 -  2.2739    1.00     5455   140  0.1838 0.2318        
REMARK   3    15  2.2739 -  2.2222    1.00     5458   145  0.1723 0.2300        
REMARK   3    16  2.2222 -  2.1749    1.00     5471   138  0.1812 0.2264        
REMARK   3    17  2.1749 -  2.1314    1.00     5487   137  0.1867 0.2112        
REMARK   3    18  2.1314 -  2.0912    1.00     5431   142  0.1850 0.2196        
REMARK   3    19  2.0912 -  2.0539    0.93     5101   127  0.1907 0.2205        
REMARK   3    20  2.0539 -  2.0191    0.93     5049   128  0.1917 0.2322        
REMARK   3    21  2.0191 -  1.9865    0.93     5110   133  0.2011 0.2365        
REMARK   3    22  1.9865 -  1.9559    0.94     5130   132  0.2012 0.2537        
REMARK   3    23  1.9559 -  1.9272    0.94     5141   130  0.2050 0.2654        
REMARK   3    24  1.9272 -  1.9000    0.94     5115   134  0.2111 0.2223        
REMARK   3    25  1.9000 -  1.8744    0.94     5124   133  0.2151 0.2863        
REMARK   3    26  1.8744 -  1.8500    0.94     5186   136  0.2130 0.2532        
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)     : 0.17             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.49            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.09                          
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      :  0.007           9533                                  
REMARK   3   ANGLE     :  1.113          13015                                  
REMARK   3   CHIRALITY :  0.079           1350                                  
REMARK   3   PLANARITY :  0.006           1721                                  
REMARK   3   DIHEDRAL  : 13.625           3471                                  
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 3ZOA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-FEB-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-55884.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JUL-12                          
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               : SSRL                               
REMARK 200  BEAMLINE                       : BL12-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS)                    
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 143054                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.85                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 7.0                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.00                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.6                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.68                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.83                               
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 2ZE0                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CACODYLATE BUFFER           
REMARK 280  PH 6.5, 0.2 M MGCL2, 10% PEG 1000, 100 MM ACARBOSE                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X,-Y,Z                                                 
REMARK 290       7555   -Y+1/2,X,Z+3/4                                          
REMARK 290       8555   Y,-X+1/2,Z+1/4                                          
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       63.59000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       63.59000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      108.47500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       63.59000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       54.23750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       63.59000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      162.71250            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       63.59000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       63.59000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      108.47500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       63.59000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000      162.71250            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       63.59000            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       54.23750            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4050 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 40560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -136.4 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     GLU A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     HIS A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     HIS A     9                                                      
REMARK 465     VAL A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     ALA A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     ILE A    14                                                      
REMARK 465     VAL A    15                                                      
REMARK 465     GLU A    16                                                      
REMARK 465     HIS A    17                                                      
REMARK 465     PRO A    18                                                      
REMARK 465     ASN A    19                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     GLU A    21                                                      
REMARK 465     ASP A    22                                                      
REMARK 465     PHE A    23                                                      
REMARK 465     GLY A    24                                                      
REMARK 465     HIS A    25                                                      
REMARK 465     ALA A    26                                                      
REMARK 465     ARG A    27                                                      
REMARK 465     THR A    28                                                      
REMARK 465     LEU A    29                                                      
REMARK 465     ARG A   514                                                      
REMARK 465     GLN A   515                                                      
REMARK 465     GLN A   516                                                      
REMARK 465     GLY A   517                                                      
REMARK 465     ASP A   518                                                      
REMARK 465     GLY A   519                                                      
REMARK 465     GLY A   520                                                      
REMARK 465     ALA A   521                                                      
REMARK 465     LYS A   522                                                      
REMARK 465     PRO A   587                                                      
REMARK 465     GLU A   588                                                      
REMARK 465     PRO A   589                                                      
REMARK 465     GLY A   590                                                      
REMARK 465     ALA A   591                                                      
REMARK 465     GLN A   592                                                      
REMARK 465     GLN A   593                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     HIS B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     GLN B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     SER B     8                                                      
REMARK 465     HIS B     9                                                      
REMARK 465     VAL B    10                                                      
REMARK 465     GLU B    11                                                      
REMARK 465     ALA B    12                                                      
REMARK 465     GLY B    13                                                      
REMARK 465     ILE B    14                                                      
REMARK 465     VAL B    15                                                      
REMARK 465     GLU B    16                                                      
REMARK 465     GLU B   588                                                      
REMARK 465     PRO B   589                                                      
REMARK 465     GLY B   590                                                      
REMARK 465     ALA B   591                                                      
REMARK 465     GLN B   592                                                      
REMARK 465     GLN B   593                                                      
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    ASP A  32       85.66   -153.10                                   
REMARK 500    SER A  86      144.31   -170.04                                   
REMARK 500    PHE A 194     -143.76   -101.35                                   
REMARK 500    GLU A 293     -114.71   -120.22                                   
REMARK 500    ASP A 351      112.86   -160.49                                   
REMARK 500    ALA B  20      -58.05     56.37                                   
REMARK 500    PHE B 194     -143.50   -104.68                                   
REMARK 500    GLU B 293     -118.18   -119.52                                   
REMARK 500    LEU B 338       56.85    -93.44                                   
REMARK 500    ARG B 434      132.47    -38.09                                   
REMARK 500    ARG B 514     -171.14    -68.29                                   
REMARK 500    GLN B 515     -156.18    174.33                                   
REMARK 500    GLN B 516     -109.77     15.29                                   
REMARK 500    ASP B 518     -123.60    -68.04                                   
REMARK 500    HIS B 575       18.54     59.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1588  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU A 235   O                                                      
REMARK 620 2 HOH A2233   O    78.0                                              
REMARK 620 3 GLU A 237   OE2  80.7  73.5                                        
REMARK 620 4 ASN A 132   OD1 113.5 144.6 139.6                                  
REMARK 620 5 HOH A2125   O    84.5  75.7 148.0  72.4                            
REMARK 620 6 ASP A 200   OD2 166.0  88.9  90.8  80.2  97.4                      
REMARK 620 7 TYR A 234   O    76.9 143.2  76.2  71.2 127.5 112.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B1590  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B 132   OD1                                                    
REMARK 620 2 TYR B 234   O    72.1                                              
REMARK 620 3 LEU B 235   O   110.7  76.8                                        
REMARK 620 4 GLU B 237   OE2 141.5  77.5  84.1                                  
REMARK 620 5 HOH B2135   O    71.9 126.5  80.6 146.7                            
REMARK 620 6 HOH B2216   O   141.7 143.7  77.1  75.1  72.7                      
REMARK 620 7 ASP B 200   OD2  77.0 113.4 169.1  94.4  95.2  92.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1593  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2024   O                                                      
REMARK 620 2 ASP A  51   OD1 172.1                                              
REMARK 620 3 ASN A  53   OD1  93.8  83.3                                        
REMARK 620 4 ASP A  55   OD1  85.5  86.7  81.3                                  
REMARK 620 5 ILE A  57   O    95.0  87.3 169.9  94.5                            
REMARK 620 6 ASP A  59   OD2  94.8  92.6  90.9 172.2  93.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1592  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE B  57   O                                                      
REMARK 620 2 ASP B  59   OD2  95.9                                              
REMARK 620 3 ASP B  51   OD1  87.5  95.9                                        
REMARK 620 4 ASN B  53   OD1 169.1  89.0  82.3                                  
REMARK 620 5 ASP B  55   OD1  93.0 171.1  85.1  82.3                            
REMARK 620 6 HOH B2031   O    98.9  92.4 169.0  90.6  85.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AA" 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 700                                                                      
REMARK 700 THE SHEETS PRESENTED AS "BA" 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 ACR A1587                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1588                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1589                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1588                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B1590                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1589                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1590                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1591                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1591                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1592                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B1592                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A1593                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3ZO9   RELATED DB: PDB                                   
REMARK 900  NOVEL ACTIVE SITE AND INHIBITION SITES IDENTIFIED IN                
REMARK 900  TREHALOSE SYNTHASE                                                  
DBREF  3ZOA A    1   593  UNP    A0R6E0   TRES_MYCS2       1    593             
DBREF  3ZOA B    1   593  UNP    A0R6E0   TRES_MYCS2       1    593             
SEQRES   1 A  593  MET GLU GLU HIS THR GLN GLY SER HIS VAL GLU ALA GLY          
SEQRES   2 A  593  ILE VAL GLU HIS PRO ASN ALA GLU ASP PHE GLY HIS ALA          
SEQRES   3 A  593  ARG THR LEU PRO THR ASP THR ASN TRP PHE LYS HIS ALA          
SEQRES   4 A  593  VAL PHE TYR GLU VAL LEU VAL ARG ALA PHE TYR ASP SER          
SEQRES   5 A  593  ASN ALA ASP GLY ILE GLY ASP LEU ARG GLY LEU THR GLU          
SEQRES   6 A  593  LYS LEU ASP TYR ILE LYS TRP LEU GLY VAL ASP CYS LEU          
SEQRES   7 A  593  TRP LEU PRO PRO PHE TYR ASP SER PRO LEU ARG ASP GLY          
SEQRES   8 A  593  GLY TYR ASP ILE ARG ASP PHE TYR LYS VAL LEU PRO GLU          
SEQRES   9 A  593  PHE GLY THR VAL ASP ASP PHE VAL THR LEU LEU ASP ALA          
SEQRES  10 A  593  ALA HIS ARG ARG GLY ILE ARG ILE ILE THR ASP LEU VAL          
SEQRES  11 A  593  MET ASN HIS THR SER ASP GLN HIS GLU TRP PHE GLN GLU          
SEQRES  12 A  593  SER ARG HIS ASN PRO ASP GLY PRO TYR GLY ASP PHE TYR          
SEQRES  13 A  593  VAL TRP SER ASP THR SER ASP ARG TYR PRO ASP ALA ARG          
SEQRES  14 A  593  ILE ILE PHE VAL ASP THR GLU GLU SER ASN TRP THR PHE          
SEQRES  15 A  593  ASP PRO VAL ARG ARG GLN PHE TYR TRP HIS ARG PHE PHE          
SEQRES  16 A  593  SER HIS GLN PRO ASP LEU ASN TYR ASP ASN PRO ALA VAL          
SEQRES  17 A  593  GLN GLU ALA MET LEU ASP VAL LEU ARG PHE TRP LEU ASP          
SEQRES  18 A  593  LEU GLY ILE ASP GLY PHE ARG LEU ASP ALA VAL PRO TYR          
SEQRES  19 A  593  LEU PHE GLU ARG GLU GLY THR ASN CYS GLU ASN LEU PRO          
SEQRES  20 A  593  GLU THR HIS ALA PHE LEU LYS ARG CYS ARG LYS ALA ILE          
SEQRES  21 A  593  ASP ASP GLU TYR PRO GLY ARG VAL LEU LEU ALA GLU ALA          
SEQRES  22 A  593  ASN GLN TRP PRO ALA ASP VAL VAL ALA TYR PHE GLY ASP          
SEQRES  23 A  593  PRO ASP THR GLY GLY ASP GLU CYS HIS MET ALA PHE HIS          
SEQRES  24 A  593  PHE PRO LEU MET PRO ARG ILE PHE MET ALA VAL ARG ARG          
SEQRES  25 A  593  GLU SER ARG PHE PRO ILE SER GLU ILE LEU ALA GLN THR          
SEQRES  26 A  593  PRO PRO ILE PRO ASP THR ALA GLN TRP GLY ILE PHE LEU          
SEQRES  27 A  593  ARG ASN HIS ASP GLU LEU THR LEU GLU MET VAL THR ASP          
SEQRES  28 A  593  GLU GLU ARG ASP TYR MET TYR ALA GLU TYR ALA LYS ASP          
SEQRES  29 A  593  PRO ARG MET LYS ALA ASN VAL GLY ILE ARG ARG ARG LEU          
SEQRES  30 A  593  ALA PRO LEU LEU GLU ASN ASP ARG ASN GLN ILE GLU LEU          
SEQRES  31 A  593  PHE THR ALA LEU LEU LEU SER LEU PRO GLY SER PRO VAL          
SEQRES  32 A  593  LEU TYR TYR GLY ASP GLU ILE GLY MET GLY ASP ILE ILE          
SEQRES  33 A  593  TRP LEU GLY ASP ARG ASP SER VAL ARG THR PRO MET GLN          
SEQRES  34 A  593  TRP THR PRO ASP ARG ASN ALA GLY PHE SER LYS ALA THR          
SEQRES  35 A  593  PRO GLY ARG LEU TYR LEU PRO PRO ASN GLN ASP ALA VAL          
SEQRES  36 A  593  TYR GLY TYR HIS SER VAL ASN VAL GLU ALA GLN LEU ASP          
SEQRES  37 A  593  SER SER SER SER LEU LEU ASN TRP THR ARG ASN MET LEU          
SEQRES  38 A  593  ALA VAL ARG SER ARG HIS ASP ALA PHE ALA VAL GLY THR          
SEQRES  39 A  593  PHE ARG GLU LEU GLY GLY SER ASN PRO SER VAL LEU ALA          
SEQRES  40 A  593  TYR ILE ARG GLU VAL THR ARG GLN GLN GLY ASP GLY GLY          
SEQRES  41 A  593  ALA LYS THR ASP ALA VAL LEU CYS VAL ASN ASN LEU SER          
SEQRES  42 A  593  ARG PHE PRO GLN PRO ILE GLU LEU ASN LEU GLN GLN TRP          
SEQRES  43 A  593  ALA GLY TYR ILE PRO VAL GLU MET THR GLY TYR VAL GLU          
SEQRES  44 A  593  PHE PRO SER ILE GLY GLN LEU PRO TYR LEU LEU THR LEU          
SEQRES  45 A  593  PRO GLY HIS GLY PHE TYR TRP PHE GLN LEU ARG GLU PRO          
SEQRES  46 A  593  ASP PRO GLU PRO GLY ALA GLN GLN                              
SEQRES   1 B  593  MET GLU GLU HIS THR GLN GLY SER HIS VAL GLU ALA GLY          
SEQRES   2 B  593  ILE VAL GLU HIS PRO ASN ALA GLU ASP PHE GLY HIS ALA          
SEQRES   3 B  593  ARG THR LEU PRO THR ASP THR ASN TRP PHE LYS HIS ALA          
SEQRES   4 B  593  VAL PHE TYR GLU VAL LEU VAL ARG ALA PHE TYR ASP SER          
SEQRES   5 B  593  ASN ALA ASP GLY ILE GLY ASP LEU ARG GLY LEU THR GLU          
SEQRES   6 B  593  LYS LEU ASP TYR ILE LYS TRP LEU GLY VAL ASP CYS LEU          
SEQRES   7 B  593  TRP LEU PRO PRO PHE TYR ASP SER PRO LEU ARG ASP GLY          
SEQRES   8 B  593  GLY TYR ASP ILE ARG ASP PHE TYR LYS VAL LEU PRO GLU          
SEQRES   9 B  593  PHE GLY THR VAL ASP ASP PHE VAL THR LEU LEU ASP ALA          
SEQRES  10 B  593  ALA HIS ARG ARG GLY ILE ARG ILE ILE THR ASP LEU VAL          
SEQRES  11 B  593  MET ASN HIS THR SER ASP GLN HIS GLU TRP PHE GLN GLU          
SEQRES  12 B  593  SER ARG HIS ASN PRO ASP GLY PRO TYR GLY ASP PHE TYR          
SEQRES  13 B  593  VAL TRP SER ASP THR SER ASP ARG TYR PRO ASP ALA ARG          
SEQRES  14 B  593  ILE ILE PHE VAL ASP THR GLU GLU SER ASN TRP THR PHE          
SEQRES  15 B  593  ASP PRO VAL ARG ARG GLN PHE TYR TRP HIS ARG PHE PHE          
SEQRES  16 B  593  SER HIS GLN PRO ASP LEU ASN TYR ASP ASN PRO ALA VAL          
SEQRES  17 B  593  GLN GLU ALA MET LEU ASP VAL LEU ARG PHE TRP LEU ASP          
SEQRES  18 B  593  LEU GLY ILE ASP GLY PHE ARG LEU ASP ALA VAL PRO TYR          
SEQRES  19 B  593  LEU PHE GLU ARG GLU GLY THR ASN CYS GLU ASN LEU PRO          
SEQRES  20 B  593  GLU THR HIS ALA PHE LEU LYS ARG CYS ARG LYS ALA ILE          
SEQRES  21 B  593  ASP ASP GLU TYR PRO GLY ARG VAL LEU LEU ALA GLU ALA          
SEQRES  22 B  593  ASN GLN TRP PRO ALA ASP VAL VAL ALA TYR PHE GLY ASP          
SEQRES  23 B  593  PRO ASP THR GLY GLY ASP GLU CYS HIS MET ALA PHE HIS          
SEQRES  24 B  593  PHE PRO LEU MET PRO ARG ILE PHE MET ALA VAL ARG ARG          
SEQRES  25 B  593  GLU SER ARG PHE PRO ILE SER GLU ILE LEU ALA GLN THR          
SEQRES  26 B  593  PRO PRO ILE PRO ASP THR ALA GLN TRP GLY ILE PHE LEU          
SEQRES  27 B  593  ARG ASN HIS ASP GLU LEU THR LEU GLU MET VAL THR ASP          
SEQRES  28 B  593  GLU GLU ARG ASP TYR MET TYR ALA GLU TYR ALA LYS ASP          
SEQRES  29 B  593  PRO ARG MET LYS ALA ASN VAL GLY ILE ARG ARG ARG LEU          
SEQRES  30 B  593  ALA PRO LEU LEU GLU ASN ASP ARG ASN GLN ILE GLU LEU          
SEQRES  31 B  593  PHE THR ALA LEU LEU LEU SER LEU PRO GLY SER PRO VAL          
SEQRES  32 B  593  LEU TYR TYR GLY ASP GLU ILE GLY MET GLY ASP ILE ILE          
SEQRES  33 B  593  TRP LEU GLY ASP ARG ASP SER VAL ARG THR PRO MET GLN          
SEQRES  34 B  593  TRP THR PRO ASP ARG ASN ALA GLY PHE SER LYS ALA THR          
SEQRES  35 B  593  PRO GLY ARG LEU TYR LEU PRO PRO ASN GLN ASP ALA VAL          
SEQRES  36 B  593  TYR GLY TYR HIS SER VAL ASN VAL GLU ALA GLN LEU ASP          
SEQRES  37 B  593  SER SER SER SER LEU LEU ASN TRP THR ARG ASN MET LEU          
SEQRES  38 B  593  ALA VAL ARG SER ARG HIS ASP ALA PHE ALA VAL GLY THR          
SEQRES  39 B  593  PHE ARG GLU LEU GLY GLY SER ASN PRO SER VAL LEU ALA          
SEQRES  40 B  593  TYR ILE ARG GLU VAL THR ARG GLN GLN GLY ASP GLY GLY          
SEQRES  41 B  593  ALA LYS THR ASP ALA VAL LEU CYS VAL ASN ASN LEU SER          
SEQRES  42 B  593  ARG PHE PRO GLN PRO ILE GLU LEU ASN LEU GLN GLN TRP          
SEQRES  43 B  593  ALA GLY TYR ILE PRO VAL GLU MET THR GLY TYR VAL GLU          
SEQRES  44 B  593  PHE PRO SER ILE GLY GLN LEU PRO TYR LEU LEU THR LEU          
SEQRES  45 B  593  PRO GLY HIS GLY PHE TYR TRP PHE GLN LEU ARG GLU PRO          
SEQRES  46 B  593  ASP PRO GLU PRO GLY ALA GLN GLN                              
HET    ACR  A1587      44                                                       
HET     CL  B1588       1                                                       
HET     CL  B1589       1                                                       
HET     CA  A1588       1                                                       
HET     CA  B1590       1                                                       
HET     CL  A1589       1                                                       
HET     CL  A1590       1                                                       
HET     CL  A1591       1                                                       
HET     CL  B1591       1                                                       
HET     CL  A1592       1                                                       
HET     MG  B1592       1                                                       
HET     MG  A1593       1                                                       
HETNAM     ACR ALPHA-ACARBOSE                                                   
HETNAM      CL CHLORIDE ION                                                     
HETNAM      CA CALCIUM ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     ACR 1,4-DEOXY-4-((5-HYDROXYMETHYL-2,3,4-                             
HETSYN   2 ACR  TRIHYDROXYCYCLOHEX-5,6-ENYL)AMINO)FRUCTOSE                      
FORMUL   2  ACR    C25 H43 N O18                                                
FORMUL   3   CL    7(CL 1-)                                                     
FORMUL   4   CA    2(CA 2+)                                                     
FORMUL   5   MG    2(MG 2+)                                                     
FORMUL   6  HOH   *944(H2 O)                                                    
HELIX    1   1 ASN A   34  ALA A   39  1                                   6    
HELIX    2   2 LEU A   45  TYR A   50  1                                   6    
HELIX    3   3 ASP A   59  LYS A   66  1                                   8    
HELIX    4   4 LYS A   66  GLY A   74  1                                   9    
HELIX    5   5 PRO A  103  GLY A  106  5                                   4    
HELIX    6   6 THR A  107  ARG A  121  1                                  15    
HELIX    7   7 HIS A  138  ASN A  147  1                                  10    
HELIX    8   8 ASN A  205  GLY A  223  1                                  19    
HELIX    9   9 VAL A  232  LEU A  235  5                                   4    
HELIX   10  10 LEU A  246  TYR A  264  1                                  19    
HELIX   11  11 TRP A  276  VAL A  281  1                                   6    
HELIX   12  12 ALA A  282  GLY A  285  5                                   4    
HELIX   13  13 ASP A  286  GLY A  290  5                                   5    
HELIX   14  14 PRO A  301  GLU A  313  1                                  13    
HELIX   15  15 ARG A  315  GLN A  324  1                                  10    
HELIX   16  16 GLU A  360  LYS A  363  5                                   4    
HELIX   17  17 ASP A  364  ASN A  370  1                                   7    
HELIX   18  18 ARG A  376  LEU A  381  1                                   6    
HELIX   19  19 ASP A  384  LEU A  398  1                                  15    
HELIX   20  20 ILE A  415  GLY A  419  5                                   5    
HELIX   21  21 ARG A  421  ARG A  425  5                                   5    
HELIX   22  22 ASP A  433  PHE A  438  5                                   6    
HELIX   23  23 THR A  442  LEU A  446  5                                   5    
HELIX   24  24 ASN A  462  ASP A  468  1                                   7    
HELIX   25  25 SER A  472  ARG A  486  1                                  15    
HELIX   26  26 HIS A  487  GLY A  493  1                                   7    
HELIX   27  27 LEU A  543  ALA A  547  5                                   5    
HELIX   28  28 ASN B   34  ALA B   39  1                                   6    
HELIX   29  29 LEU B   45  TYR B   50  1                                   6    
HELIX   30  30 ASP B   59  LYS B   66  1                                   8    
HELIX   31  31 LYS B   66  GLY B   74  1                                   9    
HELIX   32  32 PRO B  103  GLY B  106  5                                   4    
HELIX   33  33 THR B  107  ARG B  121  1                                  15    
HELIX   34  34 HIS B  138  ASN B  147  1                                  10    
HELIX   35  35 ASN B  205  GLY B  223  1                                  19    
HELIX   36  36 VAL B  232  LEU B  235  5                                   4    
HELIX   37  37 LEU B  246  TYR B  264  1                                  19    
HELIX   38  38 TRP B  276  VAL B  281  1                                   6    
HELIX   39  39 ALA B  282  GLY B  285  5                                   4    
HELIX   40  40 ASP B  286  GLY B  290  5                                   5    
HELIX   41  41 PRO B  301  GLU B  313  1                                  13    
HELIX   42  42 ARG B  315  THR B  325  1                                  11    
HELIX   43  43 GLU B  360  LYS B  363  5                                   4    
HELIX   44  44 ASP B  364  ASN B  370  1                                   7    
HELIX   45  45 ARG B  376  LEU B  381  1                                   6    
HELIX   46  46 ASP B  384  LEU B  398  1                                  15    
HELIX   47  47 GLY B  407  GLY B  411  5                                   5    
HELIX   48  48 ILE B  415  GLY B  419  5                                   5    
HELIX   49  49 ARG B  421  ARG B  425  5                                   5    
HELIX   50  50 ASP B  433  PHE B  438  5                                   6    
HELIX   51  51 THR B  442  LEU B  446  5                                   5    
HELIX   52  52 ASN B  462  ASP B  468  1                                   7    
HELIX   53  53 SER B  472  ARG B  486  1                                  15    
HELIX   54  54 HIS B  487  GLY B  493  1                                   7    
HELIX   55  55 GLY B  520  ASP B  524  5                                   5    
HELIX   56  56 LEU B  543  ALA B  547  5                                   5    
SHEET    1  AA 9 PHE A  41  GLU A  43  0                                        
SHEET    2  AA 9 CYS A  77  LEU A  80  1  O  CYS A  77   N  TYR A  42           
SHEET    3  AA 9 ARG A 124  VAL A 130  1  O  ARG A 124   N  LEU A  78           
SHEET    4  AA 9 GLY A 226  ASP A 230  1  O  GLY A 226   N  THR A 127           
SHEET    5  AA 9 VAL A 268  GLU A 272  1  O  VAL A 268   N  PHE A 227           
SHEET    6  AA 9 MET A 296  PHE A 298  1  O  MET A 296   N  ALA A 271           
SHEET    7  AA 9 GLN A 333  PHE A 337  1  O  GLN A 333   N  ALA A 297           
SHEET    8  AA 9 SER A 401  TYR A 405  1  O  SER A 401   N  ILE A 336           
SHEET    9  AA 9 PHE A  41  GLU A  43  1  O  PHE A  41   N  LEU A 404           
SHEET    1  AB 2 TYR A  84  ASP A  85  0                                        
SHEET    2  AB 2 ASP A  97  VAL A 101 -1  N  ASP A  97   O  ASP A  85           
SHEET    1  AC 3 TRP A 158  SER A 159  0                                        
SHEET    2  AC 3 PHE A 189  TRP A 191 -1  O  PHE A 189   N  SER A 159           
SHEET    3  AC 3 TRP A 180  PHE A 182 -1  O  THR A 181   N  TYR A 190           
SHEET    1  AD 5 THR A 494  GLU A 497  0                                        
SHEET    2  AD 5 VAL A 505  VAL A 512 -1  O  ILE A 509   N  ARG A 496           
SHEET    3  AD 5 ASP A 524  ASN A 531 -1  O  ASP A 524   N  VAL A 512           
SHEET    4  AD 5 PHE A 577  ARG A 583 -1  O  TYR A 578   N  VAL A 529           
SHEET    5  AD 5 ILE A 550  GLU A 553 -1  O  ILE A 550   N  ARG A 583           
SHEET    1  AE 2 GLN A 537  LEU A 541  0                                        
SHEET    2  AE 2 TYR A 568  LEU A 572 -1  O  TYR A 568   N  LEU A 541           
SHEET    1  BA 9 PHE B  41  GLU B  43  0                                        
SHEET    2  BA 9 CYS B  77  LEU B  80  1  O  CYS B  77   N  TYR B  42           
SHEET    3  BA 9 ARG B 124  VAL B 130  1  O  ARG B 124   N  LEU B  78           
SHEET    4  BA 9 GLY B 226  ASP B 230  1  O  GLY B 226   N  THR B 127           
SHEET    5  BA 9 VAL B 268  GLU B 272  1  O  VAL B 268   N  PHE B 227           
SHEET    6  BA 9 MET B 296  PHE B 298  1  O  MET B 296   N  ALA B 271           
SHEET    7  BA 9 GLN B 333  PHE B 337  1  O  GLN B 333   N  ALA B 297           
SHEET    8  BA 9 SER B 401  TYR B 405  1  O  SER B 401   N  ILE B 336           
SHEET    9  BA 9 PHE B  41  GLU B  43  1  O  PHE B  41   N  LEU B 404           
SHEET    1  BB 2 TYR B  84  ASP B  85  0                                        
SHEET    2  BB 2 ASP B  97  VAL B 101 -1  N  ASP B  97   O  ASP B  85           
SHEET    1  BC 3 TRP B 158  SER B 159  0                                        
SHEET    2  BC 3 GLN B 188  TRP B 191 -1  O  PHE B 189   N  SER B 159           
SHEET    3  BC 3 TRP B 180  ASP B 183 -1  O  THR B 181   N  TYR B 190           
SHEET    1  BD 5 ARG B 496  GLU B 497  0                                        
SHEET    2  BD 5 VAL B 505  ARG B 510 -1  O  ILE B 509   N  ARG B 496           
SHEET    3  BD 5 ALA B 525  ASN B 531 -1  O  VAL B 526   N  ARG B 510           
SHEET    4  BD 5 PHE B 577  ARG B 583 -1  O  TYR B 578   N  VAL B 529           
SHEET    5  BD 5 ILE B 550  GLU B 553 -1  O  ILE B 550   N  ARG B 583           
SHEET    1  BE 2 GLN B 537  LEU B 541  0                                        
SHEET    2  BE 2 TYR B 568  LEU B 572 -1  O  TYR B 568   N  LEU B 541           
LINK        CA    CA A1588                 O   LEU A 235     1555   1555  2.46  
LINK        CA    CA A1588                 O   HOH A2233     1555   1555  2.39  
LINK        CA    CA A1588                 OE2 GLU A 237     1555   1555  2.42  
LINK        CA    CA A1588                 OD1 ASN A 132     1555   1555  2.49  
LINK        CA    CA A1588                 O   HOH A2125     1555   1555  2.33  
LINK        CA    CA A1588                 OD2 ASP A 200     1555   1555  2.39  
LINK        CA    CA A1588                 O   TYR A 234     1555   1555  2.31  
LINK        MG    MG A1593                 OD2 ASP A  59     1555   1555  2.09  
LINK        MG    MG A1593                 O   ILE A  57     1555   1555  2.04  
LINK        MG    MG A1593                 OD1 ASP A  55     1555   1555  2.15  
LINK        MG    MG A1593                 OD1 ASN A  53     1555   1555  2.10  
LINK        MG    MG A1593                 OD1 ASP A  51     1555   1555  2.04  
LINK        MG    MG A1593                 O   HOH A2024     1555   1555  2.12  
LINK        CA    CA B1590                 OD2 ASP B 200     1555   1555  2.29  
LINK        CA    CA B1590                 O   HOH B2216     1555   1555  2.36  
LINK        CA    CA B1590                 O   HOH B2135     1555   1555  2.34  
LINK        CA    CA B1590                 OE2 GLU B 237     1555   1555  2.42  
LINK        CA    CA B1590                 O   LEU B 235     1555   1555  2.58  
LINK        CA    CA B1590                 O   TYR B 234     1555   1555  2.30  
LINK        CA    CA B1590                 OD1 ASN B 132     1555   1555  2.47  
LINK        MG    MG B1592                 OD2 ASP B  59     1555   1555  2.07  
LINK        MG    MG B1592                 OD1 ASP B  51     1555   1555  2.04  
LINK        MG    MG B1592                 OD1 ASN B  53     1555   1555  2.13  
LINK        MG    MG B1592                 OD1 ASP B  55     1555   1555  2.20  
LINK        MG    MG B1592                 O   HOH B2031     1555   1555  2.06  
LINK        MG    MG B1592                 O   ILE B  57     1555   1555  2.05  
SITE     1 AC1 12 TRP A 476  MET A 480  GLU A 553  MET A 554                    
SITE     2 AC1 12 THR A 555  TYR A 557  PHE A 577  TYR A 578                    
SITE     3 AC1 12 TRP A 579  HOH A2478  ARG B 534  PHE B 535                    
SITE     1 AC2  3 ARG B 228  ARG B 339  GLU B 343                               
SITE     1 AC3  4 ASN B 340  HIS B 341  ARG B 374  ARG B 375                    
SITE     1 AC4  7 ASN A 132  ASP A 200  TYR A 234  LEU A 235                    
SITE     2 AC4  7 GLU A 237  HOH A2125  HOH A2233                               
SITE     1 AC5  7 ASN B 132  ASP B 200  TYR B 234  LEU B 235                    
SITE     2 AC5  7 GLU B 237  HOH B2135  HOH B2216                               
SITE     1 AC6  5 ASN A 340  HIS A 341  ARG A 374  ARG A 375                    
SITE     2 AC6  5 HOH A2326                                                     
SITE     1 AC7  3 ARG A 228  ARG A 339  GLU A 343                               
SITE     1 AC8  4 VAL A  46  ARG A  47  PHE A 105  HOH A2011                    
SITE     1 AC9  4 VAL B  46  ARG B  47  PHE B 105  HOH B2017                    
SITE     1 BC1  3 VAL A 101  THR A 107  VAL A 108                               
SITE     1 BC2  6 ASP B  51  ASN B  53  ASP B  55  ILE B  57                    
SITE     2 BC2  6 ASP B  59  HOH B2031                                          
SITE     1 BC3  6 ASP A  51  ASN A  53  ASP A  55  ILE A  57                    
SITE     2 BC3  6 ASP A  59  HOH A2024                                          
CRYST1  127.180  127.180  216.950  90.00  90.00  90.00 I 41         16          
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      0.007863  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007863  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004609        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system