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Database: PDB
Entry: 5A02
LinkDB: 5A02
Original site: 5A02 
HEADER    OXIDOREDUCTASE                          17-APR-15   5A02              
TITLE     CRYSTAL STRUCTURE OF ALDOSE-ALDOSE OXIDOREDUCTASE FROM CAULOBACTER    
TITLE    2 CRESCENTUS COMPLEXED WITH GLYCEROL                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALDOSE-ALDOSE OXIDOREDUCTASE;                              
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 EC: 1.1.99.-;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CAULOBACTER CRESCENTUS CB15;                    
SOURCE   3 ORGANISM_TAXID: 190650;                                              
SOURCE   4 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   5 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 4932                                        
KEYWDS    OXIDOREDUCTASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.TABERMAN,J.ROUVINEN,T.PARKKINEN                                     
REVDAT   4   10-JAN-24 5A02    1       REMARK                                   
REVDAT   3   09-DEC-15 5A02    1       JRNL                                     
REVDAT   2   25-NOV-15 5A02    1       SOURCE                                   
REVDAT   1   21-OCT-15 5A02    0                                                
JRNL        AUTH   H.TABERMAN,M.ANDBERG,A.KOIVULA,N.HAKULINEN,M.PENTTILA,       
JRNL        AUTH 2 J.ROUVINEN,T.PARKKINEN                                       
JRNL        TITL   STRUCTURE AND FUNCTION OF CAULOBACTER CRESCENTUS             
JRNL        TITL 2 ALDOSE-ALDOSE OXIDOREDUCTASE.                                
JRNL        REF    BIOCHEM.J.                    V. 472   297 2015              
JRNL        REFN                   ISSN 0264-6021                               
JRNL        PMID   26438878                                                     
JRNL        DOI    10.1042/BJ20150681                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.23                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.370                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 208065                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.161                           
REMARK   3   R VALUE            (WORKING SET) : 0.160                           
REMARK   3   FREE R VALUE                     : 0.187                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 10403                           
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 48.2403 -  6.2102    0.99     6700   353  0.1676 0.1745        
REMARK   3     2  6.2102 -  4.9308    0.99     6619   348  0.1724 0.1859        
REMARK   3     3  4.9308 -  4.3079    1.00     6622   348  0.1327 0.1477        
REMARK   3     4  4.3079 -  3.9142    1.00     6606   348  0.1266 0.1368        
REMARK   3     5  3.9142 -  3.6338    0.99     6608   348  0.1300 0.1545        
REMARK   3     6  3.6338 -  3.4196    1.00     6592   347  0.1362 0.1722        
REMARK   3     7  3.4196 -  3.2484    1.00     6609   348  0.1412 0.1606        
REMARK   3     8  3.2484 -  3.1070    1.00     6610   348  0.1442 0.1682        
REMARK   3     9  3.1070 -  2.9874    1.00     6587   346  0.1508 0.1762        
REMARK   3    10  2.9874 -  2.8843    1.00     6596   348  0.1613 0.2028        
REMARK   3    11  2.8843 -  2.7942    1.00     6594   347  0.1595 0.1844        
REMARK   3    12  2.7942 -  2.7143    0.99     6603   347  0.1581 0.2117        
REMARK   3    13  2.7143 -  2.6429    1.00     6549   345  0.1675 0.2133        
REMARK   3    14  2.6429 -  2.5784    1.00     6629   349  0.1646 0.2057        
REMARK   3    15  2.5784 -  2.5198    1.00     6567   345  0.1646 0.1862        
REMARK   3    16  2.5198 -  2.4661    1.00     6577   346  0.1714 0.2221        
REMARK   3    17  2.4661 -  2.4168    1.00     6594   348  0.1739 0.2145        
REMARK   3    18  2.4168 -  2.3712    1.00     6610   347  0.1727 0.2057        
REMARK   3    19  2.3712 -  2.3289    1.00     6568   346  0.1722 0.2105        
REMARK   3    20  2.3289 -  2.2894    1.00     6579   346  0.1774 0.2112        
REMARK   3    21  2.2894 -  2.2525    1.00     6572   346  0.1734 0.2180        
REMARK   3    22  2.2525 -  2.2178    0.99     6619   349  0.1817 0.2154        
REMARK   3    23  2.2178 -  2.1852    1.00     6526   343  0.1814 0.2029        
REMARK   3    24  2.1852 -  2.1544    1.00     6578   346  0.1826 0.2211        
REMARK   3    25  2.1544 -  2.1253    1.00     6649   350  0.1923 0.2355        
REMARK   3    26  2.1253 -  2.0977    1.00     6548   345  0.1974 0.2267        
REMARK   3    27  2.0977 -  2.0715    1.00     6530   344  0.2054 0.2470        
REMARK   3    28  2.0715 -  2.0465    1.00     6623   348  0.2067 0.2513        
REMARK   3    29  2.0465 -  2.0227    1.00     6556   345  0.2215 0.2505        
REMARK   3    30  2.0227 -  2.0000    0.98     6442   339  0.2369 0.2502        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.180            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.300           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.74                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.11                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008          16326                                  
REMARK   3   ANGLE     :  1.073          22158                                  
REMARK   3   CHIRALITY :  0.045           2384                                  
REMARK   3   PLANARITY :  0.005           2884                                  
REMARK   3   DIHEDRAL  : 13.392           6076                                  
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 5A02 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-APR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1290063618.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-AUG-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 208164                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
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 1H6A                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MES PH 6.5, MAGNESIUM SULPHATE,          
REMARK 280  GLYCEROL                                                            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       76.79500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7140 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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: 7650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.5 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F                                  
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     ALA A     1                                                      
REMARK 465     GLN A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     GLN B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     GLY B     4                                                      
REMARK 465     ALA C     1                                                      
REMARK 465     GLN C     2                                                      
REMARK 465     PRO C     3                                                      
REMARK 465     GLY C     4                                                      
REMARK 465     ALA D     1                                                      
REMARK 465     GLN D     2                                                      
REMARK 465     PRO D     3                                                      
REMARK 465     GLY D     4                                                      
REMARK 465     ALA E     1                                                      
REMARK 465     GLN E     2                                                      
REMARK 465     PRO E     3                                                      
REMARK 465     GLY E     4                                                      
REMARK 465     ALA F     1                                                      
REMARK 465     GLN F     2                                                      
REMARK 465     PRO F     3                                                      
REMARK 465     GLY F     4                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B  2055     O    HOH B  2168              1.95            
REMARK 500   O    HOH A  2079     O    HOH A  2190              1.96            
REMARK 500   O    HOH C  2066     O    HOH C  2180              2.10            
REMARK 500   O    HOH E  2137     O    HOH E  2138              2.12            
REMARK 500   O    HOH E  2005     O    HOH E  2012              2.12            
REMARK 500   O    HOH F  2069     O    HOH F  2203              2.13            
REMARK 500   O    HOH C  2079     O    HOH C  2218              2.13            
REMARK 500   O    HOH B  2101     O    HOH F  2124              2.13            
REMARK 500   O    HOH B  2266     O    HOH F  2010              2.13            
REMARK 500   NE   ARG F   332     O    HOH F  2219              2.15            
REMARK 500   O    HOH A  2097     O    HOH A  2233              2.15            
REMARK 500   O    HOH F  2183     O    HOH F  2206              2.16            
REMARK 500   O    HOH A  2277     O    HOH B  2163              2.17            
REMARK 500   O    HOH D  2034     O    HOH D  2095              2.19            
REMARK 500   O    HOH B  2212     O    HOH B  2213              2.19            
REMARK 500   O    HOH A  2090     O    HOH A  2213              2.19            
REMARK 500   O    HOH B  2132     O    HOH B  2133              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 223      -74.95    -87.46                                   
REMARK 500    ASN A 248       97.01   -164.85                                   
REMARK 500    ASP A 262      105.92   -160.92                                   
REMARK 500    ASP B 167      103.49    -30.63                                   
REMARK 500    ILE B 186      -34.18   -131.25                                   
REMARK 500    ASP B 223      -74.85    -91.73                                   
REMARK 500    ASN B 248       95.54   -160.80                                   
REMARK 500    LEU B 276       57.64   -119.36                                   
REMARK 500    ILE C 186      -37.13   -130.22                                   
REMARK 500    ASP C 223      -73.23    -91.46                                   
REMARK 500    LEU C 276      -85.40   -126.15                                   
REMARK 500    ASP D 223      -75.00    -88.94                                   
REMARK 500    LEU D 276      -84.89   -122.53                                   
REMARK 500    ASP E 223      -76.83    -87.22                                   
REMARK 500    ASN E 248       94.71   -160.75                                   
REMARK 500    ASP F 167      109.27    -45.09                                   
REMARK 500    ASP F 223      -75.79    -86.94                                   
REMARK 500    ASN F 248       95.58   -164.15                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 1340                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 1340                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP C 1340                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP D 1340                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP E 1340                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP F 1340                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 1341                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 1342                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1341                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1341                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1341                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 1341                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 1341                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 1342                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1342                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1342                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 1343                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 1344                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 1342                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 1343                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 1344                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 1343                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 1345                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1344                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1343                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1345                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1342                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1343                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1344                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 1346                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5A03   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ALDOSE-ALDOSE OXIDOREDUCTASE FROM CAULOBACTER   
REMARK 900 CRESCENTUS COMPLEXED WITH XYLOSE                                     
REMARK 900 RELATED ID: 5A04   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ALDOSE-ALDOSE OXIDOREDUCTASE FROM CAULOBACTER   
REMARK 900 CRESCENTUS COMPLEXED WITH GLUCOSE                                    
REMARK 900 RELATED ID: 5A05   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ALDOSE-ALDOSE OXIDOREDUCTASE FROM CAULOBACTER   
REMARK 900 CRESCENTUS COMPLEXED WITH MALTOTRIOSE                                
REMARK 900 RELATED ID: 5A06   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ALDOSE-ALDOSE OXIDOREDUCTASE FROM CAULOBACTER   
REMARK 900 CRESCENTUS COMPLEXED WITH SORBITOL                                   
DBREF  5A02 A    1   339  PDB    5A02     5A02             1    339             
DBREF  5A02 B    1   339  PDB    5A02     5A02             1    339             
DBREF  5A02 C    1   339  PDB    5A02     5A02             1    339             
DBREF  5A02 D    1   339  PDB    5A02     5A02             1    339             
DBREF  5A02 E    1   339  PDB    5A02     5A02             1    339             
DBREF  5A02 F    1   339  PDB    5A02     5A02             1    339             
SEQRES   1 A  339  ALA GLN PRO GLY ARG LYS LEU GLY TYR ALA ILE LEU GLY          
SEQRES   2 A  339  LEU GLY TYR TYR ALA THR ARG ILE ILE MET PRO ARG PHE          
SEQRES   3 A  339  ALA GLU CYS GLU HIS SER ARG LEU ALA ALA LEU VAL SER          
SEQRES   4 A  339  GLY THR PRO GLU LYS LEU LYS THR TYR GLY GLU GLN TYR          
SEQRES   5 A  339  GLY ILE PRO GLU THR HIS ARG TYR SER TYR GLU THR PHE          
SEQRES   6 A  339  ASP ARG ILE ILE ASP ASN PRO ASP VAL ASP ILE VAL TYR          
SEQRES   7 A  339  VAL ILE THR PRO ASN SER LEU HIS ARG PRO PHE THR GLU          
SEQRES   8 A  339  ARG ALA ALA ARG ALA GLY LYS HIS VAL MET CYS GLU LYS          
SEQRES   9 A  339  PRO MET ALA ASN THR VAL ALA ASP CYS GLU ALA MET ILE          
SEQRES  10 A  339  ALA ALA CYS LYS LYS ALA GLY ARG LYS LEU MET ILE GLY          
SEQRES  11 A  339  TYR ARG SER ARG PHE GLN ALA HIS ASN ILE GLU ALA ILE          
SEQRES  12 A  339  LYS LEU VAL ARG ASP GLY ALA LEU GLY PRO VAL ARG THR          
SEQRES  13 A  339  VAL VAL THR ASP HIS GLY PHE THR ILE GLY ASP PRO LYS          
SEQRES  14 A  339  GLN TRP ARG LEU ASN ARG ALA LEU ALA GLY GLY GLY SER          
SEQRES  15 A  339  LEU MET ASP ILE GLY ILE TYR SER LEU ASN ALA ALA ARG          
SEQRES  16 A  339  TYR LEU THR GLY GLU GLU PRO VAL ALA VAL ASN ALA VAL          
SEQRES  17 A  339  GLU SER THR ASP ARG SER ASP PRO ARG PHE GLY GLU VAL          
SEQRES  18 A  339  GLU ASP ILE ILE ASN PHE GLN LEU LEU PHE PRO SER GLY          
SEQRES  19 A  339  ALA THR ALA ASN CYS VAL SER ALA TYR SER VAL ASN CYS          
SEQRES  20 A  339  ASN ARG TYR ARG VAL SER GLY PRO LYS GLY TRP VAL GLU          
SEQRES  21 A  339  ILE ASP PRO ALA THR SER TYR GLN GLY GLN ALA MET ARG          
SEQRES  22 A  339  ALA GLN LEU GLY GLY PRO PRO ALA PRO ARG GLU PRO ALA          
SEQRES  23 A  339  PRO GLN PRO LYS ASN GLN PHE SER ALA GLN LEU ASP HIS          
SEQRES  24 A  339  LEU SER GLU CYS ILE LEU THR GLY ARG GLU PRO ILE VAL          
SEQRES  25 A  339  GLY GLY ASP ASP GLY LEU LYS ASP LEU ARG VAL ILE GLU          
SEQRES  26 A  339  ALA ILE TYR ARG ALA ALA ARG GLU GLY ARG THR VAL LYS          
SEQRES  27 A  339  LEU                                                          
SEQRES   1 B  339  ALA GLN PRO GLY ARG LYS LEU GLY TYR ALA ILE LEU GLY          
SEQRES   2 B  339  LEU GLY TYR TYR ALA THR ARG ILE ILE MET PRO ARG PHE          
SEQRES   3 B  339  ALA GLU CYS GLU HIS SER ARG LEU ALA ALA LEU VAL SER          
SEQRES   4 B  339  GLY THR PRO GLU LYS LEU LYS THR TYR GLY GLU GLN TYR          
SEQRES   5 B  339  GLY ILE PRO GLU THR HIS ARG TYR SER TYR GLU THR PHE          
SEQRES   6 B  339  ASP ARG ILE ILE ASP ASN PRO ASP VAL ASP ILE VAL TYR          
SEQRES   7 B  339  VAL ILE THR PRO ASN SER LEU HIS ARG PRO PHE THR GLU          
SEQRES   8 B  339  ARG ALA ALA ARG ALA GLY LYS HIS VAL MET CYS GLU LYS          
SEQRES   9 B  339  PRO MET ALA ASN THR VAL ALA ASP CYS GLU ALA MET ILE          
SEQRES  10 B  339  ALA ALA CYS LYS LYS ALA GLY ARG LYS LEU MET ILE GLY          
SEQRES  11 B  339  TYR ARG SER ARG PHE GLN ALA HIS ASN ILE GLU ALA ILE          
SEQRES  12 B  339  LYS LEU VAL ARG ASP GLY ALA LEU GLY PRO VAL ARG THR          
SEQRES  13 B  339  VAL VAL THR ASP HIS GLY PHE THR ILE GLY ASP PRO LYS          
SEQRES  14 B  339  GLN TRP ARG LEU ASN ARG ALA LEU ALA GLY GLY GLY SER          
SEQRES  15 B  339  LEU MET ASP ILE GLY ILE TYR SER LEU ASN ALA ALA ARG          
SEQRES  16 B  339  TYR LEU THR GLY GLU GLU PRO VAL ALA VAL ASN ALA VAL          
SEQRES  17 B  339  GLU SER THR ASP ARG SER ASP PRO ARG PHE GLY GLU VAL          
SEQRES  18 B  339  GLU ASP ILE ILE ASN PHE GLN LEU LEU PHE PRO SER GLY          
SEQRES  19 B  339  ALA THR ALA ASN CYS VAL SER ALA TYR SER VAL ASN CYS          
SEQRES  20 B  339  ASN ARG TYR ARG VAL SER GLY PRO LYS GLY TRP VAL GLU          
SEQRES  21 B  339  ILE ASP PRO ALA THR SER TYR GLN GLY GLN ALA MET ARG          
SEQRES  22 B  339  ALA GLN LEU GLY GLY PRO PRO ALA PRO ARG GLU PRO ALA          
SEQRES  23 B  339  PRO GLN PRO LYS ASN GLN PHE SER ALA GLN LEU ASP HIS          
SEQRES  24 B  339  LEU SER GLU CYS ILE LEU THR GLY ARG GLU PRO ILE VAL          
SEQRES  25 B  339  GLY GLY ASP ASP GLY LEU LYS ASP LEU ARG VAL ILE GLU          
SEQRES  26 B  339  ALA ILE TYR ARG ALA ALA ARG GLU GLY ARG THR VAL LYS          
SEQRES  27 B  339  LEU                                                          
SEQRES   1 C  339  ALA GLN PRO GLY ARG LYS LEU GLY TYR ALA ILE LEU GLY          
SEQRES   2 C  339  LEU GLY TYR TYR ALA THR ARG ILE ILE MET PRO ARG PHE          
SEQRES   3 C  339  ALA GLU CYS GLU HIS SER ARG LEU ALA ALA LEU VAL SER          
SEQRES   4 C  339  GLY THR PRO GLU LYS LEU LYS THR TYR GLY GLU GLN TYR          
SEQRES   5 C  339  GLY ILE PRO GLU THR HIS ARG TYR SER TYR GLU THR PHE          
SEQRES   6 C  339  ASP ARG ILE ILE ASP ASN PRO ASP VAL ASP ILE VAL TYR          
SEQRES   7 C  339  VAL ILE THR PRO ASN SER LEU HIS ARG PRO PHE THR GLU          
SEQRES   8 C  339  ARG ALA ALA ARG ALA GLY LYS HIS VAL MET CYS GLU LYS          
SEQRES   9 C  339  PRO MET ALA ASN THR VAL ALA ASP CYS GLU ALA MET ILE          
SEQRES  10 C  339  ALA ALA CYS LYS LYS ALA GLY ARG LYS LEU MET ILE GLY          
SEQRES  11 C  339  TYR ARG SER ARG PHE GLN ALA HIS ASN ILE GLU ALA ILE          
SEQRES  12 C  339  LYS LEU VAL ARG ASP GLY ALA LEU GLY PRO VAL ARG THR          
SEQRES  13 C  339  VAL VAL THR ASP HIS GLY PHE THR ILE GLY ASP PRO LYS          
SEQRES  14 C  339  GLN TRP ARG LEU ASN ARG ALA LEU ALA GLY GLY GLY SER          
SEQRES  15 C  339  LEU MET ASP ILE GLY ILE TYR SER LEU ASN ALA ALA ARG          
SEQRES  16 C  339  TYR LEU THR GLY GLU GLU PRO VAL ALA VAL ASN ALA VAL          
SEQRES  17 C  339  GLU SER THR ASP ARG SER ASP PRO ARG PHE GLY GLU VAL          
SEQRES  18 C  339  GLU ASP ILE ILE ASN PHE GLN LEU LEU PHE PRO SER GLY          
SEQRES  19 C  339  ALA THR ALA ASN CYS VAL SER ALA TYR SER VAL ASN CYS          
SEQRES  20 C  339  ASN ARG TYR ARG VAL SER GLY PRO LYS GLY TRP VAL GLU          
SEQRES  21 C  339  ILE ASP PRO ALA THR SER TYR GLN GLY GLN ALA MET ARG          
SEQRES  22 C  339  ALA GLN LEU GLY GLY PRO PRO ALA PRO ARG GLU PRO ALA          
SEQRES  23 C  339  PRO GLN PRO LYS ASN GLN PHE SER ALA GLN LEU ASP HIS          
SEQRES  24 C  339  LEU SER GLU CYS ILE LEU THR GLY ARG GLU PRO ILE VAL          
SEQRES  25 C  339  GLY GLY ASP ASP GLY LEU LYS ASP LEU ARG VAL ILE GLU          
SEQRES  26 C  339  ALA ILE TYR ARG ALA ALA ARG GLU GLY ARG THR VAL LYS          
SEQRES  27 C  339  LEU                                                          
SEQRES   1 D  339  ALA GLN PRO GLY ARG LYS LEU GLY TYR ALA ILE LEU GLY          
SEQRES   2 D  339  LEU GLY TYR TYR ALA THR ARG ILE ILE MET PRO ARG PHE          
SEQRES   3 D  339  ALA GLU CYS GLU HIS SER ARG LEU ALA ALA LEU VAL SER          
SEQRES   4 D  339  GLY THR PRO GLU LYS LEU LYS THR TYR GLY GLU GLN TYR          
SEQRES   5 D  339  GLY ILE PRO GLU THR HIS ARG TYR SER TYR GLU THR PHE          
SEQRES   6 D  339  ASP ARG ILE ILE ASP ASN PRO ASP VAL ASP ILE VAL TYR          
SEQRES   7 D  339  VAL ILE THR PRO ASN SER LEU HIS ARG PRO PHE THR GLU          
SEQRES   8 D  339  ARG ALA ALA ARG ALA GLY LYS HIS VAL MET CYS GLU LYS          
SEQRES   9 D  339  PRO MET ALA ASN THR VAL ALA ASP CYS GLU ALA MET ILE          
SEQRES  10 D  339  ALA ALA CYS LYS LYS ALA GLY ARG LYS LEU MET ILE GLY          
SEQRES  11 D  339  TYR ARG SER ARG PHE GLN ALA HIS ASN ILE GLU ALA ILE          
SEQRES  12 D  339  LYS LEU VAL ARG ASP GLY ALA LEU GLY PRO VAL ARG THR          
SEQRES  13 D  339  VAL VAL THR ASP HIS GLY PHE THR ILE GLY ASP PRO LYS          
SEQRES  14 D  339  GLN TRP ARG LEU ASN ARG ALA LEU ALA GLY GLY GLY SER          
SEQRES  15 D  339  LEU MET ASP ILE GLY ILE TYR SER LEU ASN ALA ALA ARG          
SEQRES  16 D  339  TYR LEU THR GLY GLU GLU PRO VAL ALA VAL ASN ALA VAL          
SEQRES  17 D  339  GLU SER THR ASP ARG SER ASP PRO ARG PHE GLY GLU VAL          
SEQRES  18 D  339  GLU ASP ILE ILE ASN PHE GLN LEU LEU PHE PRO SER GLY          
SEQRES  19 D  339  ALA THR ALA ASN CYS VAL SER ALA TYR SER VAL ASN CYS          
SEQRES  20 D  339  ASN ARG TYR ARG VAL SER GLY PRO LYS GLY TRP VAL GLU          
SEQRES  21 D  339  ILE ASP PRO ALA THR SER TYR GLN GLY GLN ALA MET ARG          
SEQRES  22 D  339  ALA GLN LEU GLY GLY PRO PRO ALA PRO ARG GLU PRO ALA          
SEQRES  23 D  339  PRO GLN PRO LYS ASN GLN PHE SER ALA GLN LEU ASP HIS          
SEQRES  24 D  339  LEU SER GLU CYS ILE LEU THR GLY ARG GLU PRO ILE VAL          
SEQRES  25 D  339  GLY GLY ASP ASP GLY LEU LYS ASP LEU ARG VAL ILE GLU          
SEQRES  26 D  339  ALA ILE TYR ARG ALA ALA ARG GLU GLY ARG THR VAL LYS          
SEQRES  27 D  339  LEU                                                          
SEQRES   1 E  339  ALA GLN PRO GLY ARG LYS LEU GLY TYR ALA ILE LEU GLY          
SEQRES   2 E  339  LEU GLY TYR TYR ALA THR ARG ILE ILE MET PRO ARG PHE          
SEQRES   3 E  339  ALA GLU CYS GLU HIS SER ARG LEU ALA ALA LEU VAL SER          
SEQRES   4 E  339  GLY THR PRO GLU LYS LEU LYS THR TYR GLY GLU GLN TYR          
SEQRES   5 E  339  GLY ILE PRO GLU THR HIS ARG TYR SER TYR GLU THR PHE          
SEQRES   6 E  339  ASP ARG ILE ILE ASP ASN PRO ASP VAL ASP ILE VAL TYR          
SEQRES   7 E  339  VAL ILE THR PRO ASN SER LEU HIS ARG PRO PHE THR GLU          
SEQRES   8 E  339  ARG ALA ALA ARG ALA GLY LYS HIS VAL MET CYS GLU LYS          
SEQRES   9 E  339  PRO MET ALA ASN THR VAL ALA ASP CYS GLU ALA MET ILE          
SEQRES  10 E  339  ALA ALA CYS LYS LYS ALA GLY ARG LYS LEU MET ILE GLY          
SEQRES  11 E  339  TYR ARG SER ARG PHE GLN ALA HIS ASN ILE GLU ALA ILE          
SEQRES  12 E  339  LYS LEU VAL ARG ASP GLY ALA LEU GLY PRO VAL ARG THR          
SEQRES  13 E  339  VAL VAL THR ASP HIS GLY PHE THR ILE GLY ASP PRO LYS          
SEQRES  14 E  339  GLN TRP ARG LEU ASN ARG ALA LEU ALA GLY GLY GLY SER          
SEQRES  15 E  339  LEU MET ASP ILE GLY ILE TYR SER LEU ASN ALA ALA ARG          
SEQRES  16 E  339  TYR LEU THR GLY GLU GLU PRO VAL ALA VAL ASN ALA VAL          
SEQRES  17 E  339  GLU SER THR ASP ARG SER ASP PRO ARG PHE GLY GLU VAL          
SEQRES  18 E  339  GLU ASP ILE ILE ASN PHE GLN LEU LEU PHE PRO SER GLY          
SEQRES  19 E  339  ALA THR ALA ASN CYS VAL SER ALA TYR SER VAL ASN CYS          
SEQRES  20 E  339  ASN ARG TYR ARG VAL SER GLY PRO LYS GLY TRP VAL GLU          
SEQRES  21 E  339  ILE ASP PRO ALA THR SER TYR GLN GLY GLN ALA MET ARG          
SEQRES  22 E  339  ALA GLN LEU GLY GLY PRO PRO ALA PRO ARG GLU PRO ALA          
SEQRES  23 E  339  PRO GLN PRO LYS ASN GLN PHE SER ALA GLN LEU ASP HIS          
SEQRES  24 E  339  LEU SER GLU CYS ILE LEU THR GLY ARG GLU PRO ILE VAL          
SEQRES  25 E  339  GLY GLY ASP ASP GLY LEU LYS ASP LEU ARG VAL ILE GLU          
SEQRES  26 E  339  ALA ILE TYR ARG ALA ALA ARG GLU GLY ARG THR VAL LYS          
SEQRES  27 E  339  LEU                                                          
SEQRES   1 F  339  ALA GLN PRO GLY ARG LYS LEU GLY TYR ALA ILE LEU GLY          
SEQRES   2 F  339  LEU GLY TYR TYR ALA THR ARG ILE ILE MET PRO ARG PHE          
SEQRES   3 F  339  ALA GLU CYS GLU HIS SER ARG LEU ALA ALA LEU VAL SER          
SEQRES   4 F  339  GLY THR PRO GLU LYS LEU LYS THR TYR GLY GLU GLN TYR          
SEQRES   5 F  339  GLY ILE PRO GLU THR HIS ARG TYR SER TYR GLU THR PHE          
SEQRES   6 F  339  ASP ARG ILE ILE ASP ASN PRO ASP VAL ASP ILE VAL TYR          
SEQRES   7 F  339  VAL ILE THR PRO ASN SER LEU HIS ARG PRO PHE THR GLU          
SEQRES   8 F  339  ARG ALA ALA ARG ALA GLY LYS HIS VAL MET CYS GLU LYS          
SEQRES   9 F  339  PRO MET ALA ASN THR VAL ALA ASP CYS GLU ALA MET ILE          
SEQRES  10 F  339  ALA ALA CYS LYS LYS ALA GLY ARG LYS LEU MET ILE GLY          
SEQRES  11 F  339  TYR ARG SER ARG PHE GLN ALA HIS ASN ILE GLU ALA ILE          
SEQRES  12 F  339  LYS LEU VAL ARG ASP GLY ALA LEU GLY PRO VAL ARG THR          
SEQRES  13 F  339  VAL VAL THR ASP HIS GLY PHE THR ILE GLY ASP PRO LYS          
SEQRES  14 F  339  GLN TRP ARG LEU ASN ARG ALA LEU ALA GLY GLY GLY SER          
SEQRES  15 F  339  LEU MET ASP ILE GLY ILE TYR SER LEU ASN ALA ALA ARG          
SEQRES  16 F  339  TYR LEU THR GLY GLU GLU PRO VAL ALA VAL ASN ALA VAL          
SEQRES  17 F  339  GLU SER THR ASP ARG SER ASP PRO ARG PHE GLY GLU VAL          
SEQRES  18 F  339  GLU ASP ILE ILE ASN PHE GLN LEU LEU PHE PRO SER GLY          
SEQRES  19 F  339  ALA THR ALA ASN CYS VAL SER ALA TYR SER VAL ASN CYS          
SEQRES  20 F  339  ASN ARG TYR ARG VAL SER GLY PRO LYS GLY TRP VAL GLU          
SEQRES  21 F  339  ILE ASP PRO ALA THR SER TYR GLN GLY GLN ALA MET ARG          
SEQRES  22 F  339  ALA GLN LEU GLY GLY PRO PRO ALA PRO ARG GLU PRO ALA          
SEQRES  23 F  339  PRO GLN PRO LYS ASN GLN PHE SER ALA GLN LEU ASP HIS          
SEQRES  24 F  339  LEU SER GLU CYS ILE LEU THR GLY ARG GLU PRO ILE VAL          
SEQRES  25 F  339  GLY GLY ASP ASP GLY LEU LYS ASP LEU ARG VAL ILE GLU          
SEQRES  26 F  339  ALA ILE TYR ARG ALA ALA ARG GLU GLY ARG THR VAL LYS          
SEQRES  27 F  339  LEU                                                          
HET    NAP  A1340      48                                                       
HET    GOL  A1341       6                                                       
HET    GOL  A1342       6                                                       
HET    SO4  A1343       5                                                       
HET    NAP  B1340      48                                                       
HET    GOL  B1341       6                                                       
HET    GOL  B1342       6                                                       
HET    NAP  C1340      48                                                       
HET    GOL  C1341       6                                                       
HET    SO4  C1342       5                                                       
HET    SO4  C1343       5                                                       
HET    SO4  C1344       5                                                       
HET    NAP  D1340      48                                                       
HET    GOL  D1341       6                                                       
HET    GOL  D1342       6                                                       
HET    GOL  D1343       6                                                       
HET    SO4  D1344       5                                                       
HET    SO4  D1345       5                                                       
HET    NAP  E1340      48                                                       
HET    GOL  E1341       6                                                       
HET    GOL  E1342       6                                                       
HET    GOL  E1343       6                                                       
HET    GOL  E1344       6                                                       
HET    SO4  E1345       5                                                       
HET    SO4  E1346       5                                                       
HET    NAP  F1340      48                                                       
HET    GOL  F1341       6                                                       
HET    GOL  F1342       6                                                       
HET    GOL  F1343       6                                                       
HET    GOL  F1344       6                                                       
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   7  NAP    6(C21 H28 N7 O17 P3)                                         
FORMUL   8  GOL    16(C3 H8 O3)                                                 
FORMUL  10  SO4    8(O4 S 2-)                                                   
FORMUL  37  HOH   *1550(H2 O)                                                   
HELIX    1   1 GLY A   15  ILE A   21  1                                   7    
HELIX    2   2 ILE A   22  CYS A   29  5                                   8    
HELIX    3   3 THR A   41  GLY A   53  1                                  13    
HELIX    4   4 PRO A   55  THR A   57  5                                   3    
HELIX    5   5 THR A   64  ASN A   71  5                                   8    
HELIX    6   6 PRO A   82  SER A   84  5                                   3    
HELIX    7   7 LEU A   85  ALA A   96  1                                  12    
HELIX    8   8 THR A  109  ALA A  123  1                                  15    
HELIX    9   9 TYR A  131  PHE A  135  5                                   5    
HELIX   10  10 GLN A  136  ASP A  148  1                                  13    
HELIX   11  11 GLN A  170  LEU A  173  5                                   4    
HELIX   12  12 ASN A  174  GLY A  179  1                                   6    
HELIX   13  13 GLY A  181  ILE A  186  1                                   6    
HELIX   14  14 ILE A  186  GLY A  199  1                                  14    
HELIX   15  15 ASN A  291  GLY A  307  1                                  17    
HELIX   16  16 GLY A  313  GLY A  334  1                                  22    
HELIX   17  17 GLY B   15  ILE B   21  1                                   7    
HELIX   18  18 ILE B   22  CYS B   29  5                                   8    
HELIX   19  19 THR B   41  GLY B   53  1                                  13    
HELIX   20  20 PRO B   55  THR B   57  5                                   3    
HELIX   21  21 THR B   64  ASN B   71  5                                   8    
HELIX   22  22 PRO B   82  SER B   84  5                                   3    
HELIX   23  23 LEU B   85  ALA B   96  1                                  12    
HELIX   24  24 THR B  109  ALA B  123  1                                  15    
HELIX   25  25 TYR B  131  PHE B  135  5                                   5    
HELIX   26  26 GLN B  136  ASP B  148  1                                  13    
HELIX   27  27 GLN B  170  LEU B  173  5                                   4    
HELIX   28  28 ASN B  174  GLY B  179  1                                   6    
HELIX   29  29 GLY B  181  ILE B  186  1                                   6    
HELIX   30  30 ILE B  186  GLY B  199  1                                  14    
HELIX   31  31 ASN B  291  GLY B  307  1                                  17    
HELIX   32  32 GLY B  313  GLY B  334  1                                  22    
HELIX   33  33 GLY C   15  ILE C   21  1                                   7    
HELIX   34  34 ILE C   22  CYS C   29  5                                   8    
HELIX   35  35 THR C   41  GLY C   53  1                                  13    
HELIX   36  36 PRO C   55  THR C   57  5                                   3    
HELIX   37  37 THR C   64  ASN C   71  5                                   8    
HELIX   38  38 PRO C   82  SER C   84  5                                   3    
HELIX   39  39 LEU C   85  ALA C   96  1                                  12    
HELIX   40  40 THR C  109  ALA C  123  1                                  15    
HELIX   41  41 TYR C  131  PHE C  135  5                                   5    
HELIX   42  42 GLN C  136  ASP C  148  1                                  13    
HELIX   43  43 GLN C  170  LEU C  173  5                                   4    
HELIX   44  44 ASN C  174  GLY C  179  1                                   6    
HELIX   45  45 GLY C  181  ILE C  186  1                                   6    
HELIX   46  46 ILE C  186  GLY C  199  1                                  14    
HELIX   47  47 ASN C  291  GLY C  307  1                                  17    
HELIX   48  48 GLY C  313  GLY C  334  1                                  22    
HELIX   49  49 GLY D   15  ILE D   21  1                                   7    
HELIX   50  50 ILE D   22  CYS D   29  5                                   8    
HELIX   51  51 THR D   41  GLY D   53  1                                  13    
HELIX   52  52 PRO D   55  THR D   57  5                                   3    
HELIX   53  53 THR D   64  ASN D   71  5                                   8    
HELIX   54  54 PRO D   82  SER D   84  5                                   3    
HELIX   55  55 LEU D   85  ALA D   96  1                                  12    
HELIX   56  56 THR D  109  ALA D  123  1                                  15    
HELIX   57  57 TYR D  131  PHE D  135  5                                   5    
HELIX   58  58 GLN D  136  ASP D  148  1                                  13    
HELIX   59  59 GLN D  170  LEU D  173  5                                   4    
HELIX   60  60 ASN D  174  GLY D  179  1                                   6    
HELIX   61  61 GLY D  181  ILE D  186  1                                   6    
HELIX   62  62 ILE D  186  GLY D  199  1                                  14    
HELIX   63  63 ASN D  291  GLY D  307  1                                  17    
HELIX   64  64 GLY D  313  GLY D  334  1                                  22    
HELIX   65  65 GLY E   15  ILE E   21  1                                   7    
HELIX   66  66 ILE E   22  CYS E   29  5                                   8    
HELIX   67  67 THR E   41  TYR E   52  1                                  12    
HELIX   68  68 PRO E   55  THR E   57  5                                   3    
HELIX   69  69 THR E   64  ASN E   71  5                                   8    
HELIX   70  70 PRO E   82  SER E   84  5                                   3    
HELIX   71  71 LEU E   85  ALA E   96  1                                  12    
HELIX   72  72 THR E  109  ALA E  123  1                                  15    
HELIX   73  73 TYR E  131  PHE E  135  5                                   5    
HELIX   74  74 GLN E  136  GLY E  149  1                                  14    
HELIX   75  75 GLN E  170  LEU E  173  5                                   4    
HELIX   76  76 ASN E  174  GLY E  179  1                                   6    
HELIX   77  77 GLY E  181  ILE E  186  1                                   6    
HELIX   78  78 ILE E  186  GLY E  199  1                                  14    
HELIX   79  79 ASN E  291  GLY E  307  1                                  17    
HELIX   80  80 GLY E  313  GLY E  334  1                                  22    
HELIX   81  81 GLY F   15  ILE F   21  1                                   7    
HELIX   82  82 ILE F   22  CYS F   29  5                                   8    
HELIX   83  83 THR F   41  GLY F   53  1                                  13    
HELIX   84  84 PRO F   55  THR F   57  5                                   3    
HELIX   85  85 THR F   64  ASN F   71  5                                   8    
HELIX   86  86 PRO F   82  SER F   84  5                                   3    
HELIX   87  87 LEU F   85  ALA F   96  1                                  12    
HELIX   88  88 THR F  109  GLY F  124  1                                  16    
HELIX   89  89 TYR F  131  PHE F  135  5                                   5    
HELIX   90  90 GLN F  136  ASP F  148  1                                  13    
HELIX   91  91 GLN F  170  LEU F  173  5                                   4    
HELIX   92  92 ASN F  174  GLY F  179  1                                   6    
HELIX   93  93 GLY F  181  ILE F  186  1                                   6    
HELIX   94  94 ILE F  186  GLY F  199  1                                  14    
HELIX   95  95 ASN F  291  GLY F  307  1                                  17    
HELIX   96  96 GLY F  313  GLY F  334  1                                  22    
SHEET    1  AA 6 ARG A  59  TYR A  60  0                                        
SHEET    2  AA 6 SER A  32  VAL A  38  1  O  LEU A  37   N  TYR A  60           
SHEET    3  AA 6 LEU A   7  LEU A  12  1  O  LEU A   7   N  ARG A  33           
SHEET    4  AA 6 ILE A  76  VAL A  79  1  O  ILE A  76   N  ALA A  10           
SHEET    5  AA 6 HIS A  99  CYS A 102  1  O  HIS A  99   N  VAL A  77           
SHEET    6  AA 6 LEU A 127  ILE A 129  1  O  MET A 128   N  CYS A 102           
SHEET    1  AB 9 ALA A 281  PRO A 282  0                                        
SHEET    2  AB 9 MET A 272  GLN A 275 -1  O  ALA A 274   N  ALA A 281           
SHEET    3  AB 9 GLY A 257  ILE A 261 -1  O  TRP A 258   N  GLN A 275           
SHEET    4  AB 9 CYS A 247  GLY A 254 -1  O  TYR A 250   N  ILE A 261           
SHEET    5  AB 9 THR A 156  GLY A 162 -1  O  THR A 156   N  SER A 253           
SHEET    6  AB 9 THR A 236  ALA A 242  1  O  THR A 236   N  VAL A 157           
SHEET    7  AB 9 ILE A 224  LEU A 230 -1  N  ILE A 225   O  SER A 241           
SHEET    8  AB 9 ALA A 204  SER A 210 -1  O  ALA A 204   N  LEU A 230           
SHEET    9  AB 9 VAL A 337  LYS A 338 -1  O  VAL A 337   N  VAL A 205           
SHEET    1  BA 6 ARG B  59  TYR B  60  0                                        
SHEET    2  BA 6 SER B  32  VAL B  38  1  O  LEU B  37   N  TYR B  60           
SHEET    3  BA 6 LEU B   7  LEU B  12  1  O  LEU B   7   N  ARG B  33           
SHEET    4  BA 6 ILE B  76  VAL B  79  1  O  ILE B  76   N  ALA B  10           
SHEET    5  BA 6 HIS B  99  CYS B 102  1  O  HIS B  99   N  VAL B  77           
SHEET    6  BA 6 LEU B 127  ILE B 129  1  O  MET B 128   N  CYS B 102           
SHEET    1  BB 9 ALA B 281  PRO B 282  0                                        
SHEET    2  BB 9 MET B 272  GLN B 275 -1  O  ALA B 274   N  ALA B 281           
SHEET    3  BB 9 GLY B 257  ILE B 261 -1  O  TRP B 258   N  GLN B 275           
SHEET    4  BB 9 CYS B 247  GLY B 254 -1  O  TYR B 250   N  ILE B 261           
SHEET    5  BB 9 THR B 156  GLY B 162 -1  O  THR B 156   N  SER B 253           
SHEET    6  BB 9 THR B 236  ALA B 242  1  O  THR B 236   N  VAL B 157           
SHEET    7  BB 9 ILE B 224  LEU B 230 -1  N  ILE B 225   O  SER B 241           
SHEET    8  BB 9 ALA B 204  SER B 210 -1  O  ALA B 204   N  LEU B 230           
SHEET    9  BB 9 VAL B 337  LYS B 338 -1  O  VAL B 337   N  VAL B 205           
SHEET    1  CA 6 ARG C  59  TYR C  60  0                                        
SHEET    2  CA 6 SER C  32  VAL C  38  1  O  LEU C  37   N  TYR C  60           
SHEET    3  CA 6 LEU C   7  LEU C  12  1  O  LEU C   7   N  ARG C  33           
SHEET    4  CA 6 ILE C  76  VAL C  79  1  O  ILE C  76   N  ALA C  10           
SHEET    5  CA 6 HIS C  99  CYS C 102  1  O  HIS C  99   N  VAL C  77           
SHEET    6  CA 6 LEU C 127  ILE C 129  1  O  MET C 128   N  CYS C 102           
SHEET    1  CB 9 ALA C 281  PRO C 282  0                                        
SHEET    2  CB 9 MET C 272  GLN C 275 -1  O  ALA C 274   N  ALA C 281           
SHEET    3  CB 9 GLY C 257  ILE C 261 -1  O  TRP C 258   N  GLN C 275           
SHEET    4  CB 9 CYS C 247  GLY C 254 -1  O  TYR C 250   N  ILE C 261           
SHEET    5  CB 9 THR C 156  GLY C 162 -1  O  THR C 156   N  SER C 253           
SHEET    6  CB 9 THR C 236  ALA C 242  1  O  THR C 236   N  VAL C 157           
SHEET    7  CB 9 ILE C 224  LEU C 230 -1  N  ILE C 225   O  SER C 241           
SHEET    8  CB 9 ALA C 204  SER C 210 -1  O  ALA C 204   N  LEU C 230           
SHEET    9  CB 9 VAL C 337  LYS C 338 -1  O  VAL C 337   N  VAL C 205           
SHEET    1  DA 6 ARG D  59  TYR D  60  0                                        
SHEET    2  DA 6 SER D  32  VAL D  38  1  O  LEU D  37   N  TYR D  60           
SHEET    3  DA 6 LEU D   7  LEU D  12  1  O  LEU D   7   N  ARG D  33           
SHEET    4  DA 6 ILE D  76  VAL D  79  1  O  ILE D  76   N  ALA D  10           
SHEET    5  DA 6 HIS D  99  CYS D 102  1  O  HIS D  99   N  VAL D  77           
SHEET    6  DA 6 LEU D 127  ILE D 129  1  O  MET D 128   N  CYS D 102           
SHEET    1  DB 9 ALA D 281  PRO D 282  0                                        
SHEET    2  DB 9 MET D 272  GLN D 275 -1  O  ALA D 274   N  ALA D 281           
SHEET    3  DB 9 GLY D 257  ILE D 261 -1  O  TRP D 258   N  GLN D 275           
SHEET    4  DB 9 CYS D 247  GLY D 254 -1  O  TYR D 250   N  ILE D 261           
SHEET    5  DB 9 THR D 156  GLY D 162 -1  O  THR D 156   N  SER D 253           
SHEET    6  DB 9 THR D 236  ALA D 242  1  O  THR D 236   N  VAL D 157           
SHEET    7  DB 9 ILE D 224  LEU D 230 -1  N  ILE D 225   O  SER D 241           
SHEET    8  DB 9 ALA D 204  SER D 210 -1  O  ALA D 204   N  LEU D 230           
SHEET    9  DB 9 VAL D 337  LYS D 338 -1  O  VAL D 337   N  VAL D 205           
SHEET    1  EA 6 ARG E  59  TYR E  60  0                                        
SHEET    2  EA 6 SER E  32  VAL E  38  1  O  LEU E  37   N  TYR E  60           
SHEET    3  EA 6 LEU E   7  LEU E  12  1  O  LEU E   7   N  ARG E  33           
SHEET    4  EA 6 ILE E  76  VAL E  79  1  O  ILE E  76   N  ALA E  10           
SHEET    5  EA 6 HIS E  99  CYS E 102  1  O  HIS E  99   N  VAL E  77           
SHEET    6  EA 6 LEU E 127  ILE E 129  1  O  MET E 128   N  CYS E 102           
SHEET    1  EB 9 ALA E 281  ARG E 283  0                                        
SHEET    2  EB 9 MET E 272  LEU E 276 -1  O  MET E 272   N  ARG E 283           
SHEET    3  EB 9 GLY E 257  ILE E 261 -1  O  TRP E 258   N  GLN E 275           
SHEET    4  EB 9 CYS E 247  GLY E 254 -1  O  TYR E 250   N  ILE E 261           
SHEET    5  EB 9 THR E 156  GLY E 162 -1  O  THR E 156   N  SER E 253           
SHEET    6  EB 9 THR E 236  ALA E 242  1  O  THR E 236   N  VAL E 157           
SHEET    7  EB 9 ILE E 224  LEU E 230 -1  N  ILE E 225   O  SER E 241           
SHEET    8  EB 9 ALA E 204  SER E 210 -1  O  ALA E 204   N  LEU E 230           
SHEET    9  EB 9 VAL E 337  LYS E 338 -1  O  VAL E 337   N  VAL E 205           
SHEET    1  FA 6 ARG F  59  TYR F  60  0                                        
SHEET    2  FA 6 SER F  32  VAL F  38  1  O  LEU F  37   N  TYR F  60           
SHEET    3  FA 6 LEU F   7  LEU F  12  1  O  LEU F   7   N  ARG F  33           
SHEET    4  FA 6 ILE F  76  VAL F  79  1  O  ILE F  76   N  ALA F  10           
SHEET    5  FA 6 HIS F  99  CYS F 102  1  O  HIS F  99   N  VAL F  77           
SHEET    6  FA 6 LEU F 127  ILE F 129  1  O  MET F 128   N  CYS F 102           
SHEET    1  FB 9 ALA F 281  PRO F 282  0                                        
SHEET    2  FB 9 MET F 272  LEU F 276 -1  O  ALA F 274   N  ALA F 281           
SHEET    3  FB 9 GLY F 257  ILE F 261 -1  O  TRP F 258   N  GLN F 275           
SHEET    4  FB 9 CYS F 247  GLY F 254 -1  O  TYR F 250   N  ILE F 261           
SHEET    5  FB 9 THR F 156  GLY F 162 -1  O  THR F 156   N  SER F 253           
SHEET    6  FB 9 THR F 236  ALA F 242  1  O  THR F 236   N  VAL F 157           
SHEET    7  FB 9 ILE F 224  LEU F 230 -1  N  ILE F 225   O  SER F 241           
SHEET    8  FB 9 ALA F 204  SER F 210 -1  O  ALA F 204   N  LEU F 230           
SHEET    9  FB 9 VAL F 337  LYS F 338 -1  O  VAL F 337   N  VAL F 205           
CISPEP   1 LYS A  104    PRO A  105          0       -15.60                     
CISPEP   2 ASP A  262    PRO A  263          0         0.62                     
CISPEP   3 LYS B  104    PRO B  105          0       -12.89                     
CISPEP   4 ASP B  262    PRO B  263          0        -1.05                     
CISPEP   5 LYS C  104    PRO C  105          0       -13.01                     
CISPEP   6 ASP C  262    PRO C  263          0         0.59                     
CISPEP   7 LYS D  104    PRO D  105          0       -15.62                     
CISPEP   8 ASP D  262    PRO D  263          0        -0.35                     
CISPEP   9 LYS E  104    PRO E  105          0       -13.98                     
CISPEP  10 ASP E  262    PRO E  263          0         1.14                     
CISPEP  11 LYS F  104    PRO F  105          0       -11.93                     
CISPEP  12 ASP F  262    PRO F  263          0         2.12                     
SITE     1 AC1 36 GLY A  13  LEU A  14  GLY A  15  TYR A  16                    
SITE     2 AC1 36 TYR A  17  SER A  39  GLY A  40  THR A  41                    
SITE     3 AC1 36 LYS A  44  TYR A  62  ILE A  80  THR A  81                    
SITE     4 AC1 36 PRO A  82  ASN A  83  LEU A  85  HIS A  86                    
SITE     5 AC1 36 GLU A 103  LYS A 104  GLY A 130  ARG A 132                    
SITE     6 AC1 36 TRP A 171  ARG A 172  TYR A 189  TYR A 267                    
SITE     7 AC1 36 GOL A1341  HOH A2002  HOH A2009  HOH A2045                    
SITE     8 AC1 36 HOH A2101  HOH A2147  HOH A2191  HOH A2193                    
SITE     9 AC1 36 HOH A2311  HOH A2312  HOH A2313  HOH A2314                    
SITE     1 AC2 38 GLY B  13  LEU B  14  GLY B  15  TYR B  16                    
SITE     2 AC2 38 TYR B  17  SER B  39  GLY B  40  THR B  41                    
SITE     3 AC2 38 LYS B  44  TYR B  62  ILE B  80  THR B  81                    
SITE     4 AC2 38 PRO B  82  ASN B  83  LEU B  85  HIS B  86                    
SITE     5 AC2 38 GLU B 103  LYS B 104  GLY B 130  ARG B 132                    
SITE     6 AC2 38 TRP B 171  ARG B 172  TYR B 189  TYR B 267                    
SITE     7 AC2 38 GOL B1342  HOH B2002  HOH B2005  HOH B2025                    
SITE     8 AC2 38 HOH B2076  HOH B2169  HOH B2172  HOH B2288                    
SITE     9 AC2 38 HOH B2289  HOH B2290  HOH B2291  ASP C  66                    
SITE    10 AC2 38 HOH C2054  HOH C2056                                          
SITE     1 AC3 37 GLU B  63  HOH B2059  HOH B2061  GLY C  13                    
SITE     2 AC3 37 LEU C  14  GLY C  15  TYR C  16  TYR C  17                    
SITE     3 AC3 37 SER C  39  GLY C  40  THR C  41  LYS C  44                    
SITE     4 AC3 37 TYR C  62  ILE C  80  THR C  81  PRO C  82                    
SITE     5 AC3 37 ASN C  83  LEU C  85  HIS C  86  GLU C 103                    
SITE     6 AC3 37 LYS C 104  PRO C 105  GLY C 130  ARG C 132                    
SITE     7 AC3 37 TRP C 171  ARG C 172  TYR C 189  TYR C 267                    
SITE     8 AC3 37 GOL C1341  SO4 C1344  HOH C2003  HOH C2006                    
SITE     9 AC3 37 HOH C2025  HOH C2070  HOH C2152  HOH C2273                    
SITE    10 AC3 37 HOH C2274                                                     
SITE     1 AC4 31 LEU D  14  GLY D  15  TYR D  16  TYR D  17                    
SITE     2 AC4 31 SER D  39  GLY D  40  THR D  41  LYS D  44                    
SITE     3 AC4 31 TYR D  62  ILE D  80  THR D  81  PRO D  82                    
SITE     4 AC4 31 ASN D  83  LEU D  85  HIS D  86  GLU D 103                    
SITE     5 AC4 31 LYS D 104  GLY D 130  ARG D 132  TRP D 171                    
SITE     6 AC4 31 ARG D 172  TYR D 189  TYR D 267  GOL D1341                    
SITE     7 AC4 31 HOH D2002  HOH D2006  HOH D2060  HOH D2135                    
SITE     8 AC4 31 HOH D2138  HOH D2211  HOH D2212                               
SITE     1 AC5 34 GLY E  13  LEU E  14  GLY E  15  TYR E  16                    
SITE     2 AC5 34 TYR E  17  SER E  39  GLY E  40  THR E  41                    
SITE     3 AC5 34 LYS E  44  TYR E  62  ILE E  80  THR E  81                    
SITE     4 AC5 34 PRO E  82  ASN E  83  LEU E  85  HIS E  86                    
SITE     5 AC5 34 GLU E 103  LYS E 104  GLY E 130  ARG E 132                    
SITE     6 AC5 34 TRP E 171  ARG E 172  TYR E 189  TYR E 267                    
SITE     7 AC5 34 GOL E1341  SO4 E1346  HOH E2001  HOH E2006                    
SITE     8 AC5 34 HOH E2052  HOH E2129  HOH E2131  HOH E2214                    
SITE     9 AC5 34 HOH E2215  HOH E2216                                          
SITE     1 AC6 37 LEU F  14  GLY F  15  TYR F  16  TYR F  17                    
SITE     2 AC6 37 SER F  39  GLY F  40  THR F  41  LYS F  44                    
SITE     3 AC6 37 TYR F  62  ILE F  80  THR F  81  PRO F  82                    
SITE     4 AC6 37 ASN F  83  LEU F  85  HIS F  86  GLU F 103                    
SITE     5 AC6 37 LYS F 104  GLY F 130  ARG F 132  TRP F 171                    
SITE     6 AC6 37 ARG F 172  TYR F 189  TYR F 267  GOL F1342                    
SITE     7 AC6 37 HOH F2002  HOH F2005  HOH F2025  HOH F2055                    
SITE     8 AC6 37 HOH F2090  HOH F2133  HOH F2136  HOH F2223                    
SITE     9 AC6 37 HOH F2224  HOH F2225  HOH F2226  HOH F2227                    
SITE    10 AC6 37 HOH F2228                                                     
SITE     1 AC7  6 HIS F 138  MET F 272  ARG F 283  GLU F 284                    
SITE     2 AC7  6 HOH F2192  HOH F2230                                          
SITE     1 AC8  7 LYS F 104  PHE F 163  ARG F 172  ASP F 185                    
SITE     2 AC8  7 TYR F 189  NAP F1340  HOH F2135                               
SITE     1 AC9  9 HIS B 138  GLN B 270  ALA B 271  MET B 272                    
SITE     2 AC9  9 PRO B 282  ARG B 283  GLU B 284  HOH B2248                    
SITE     3 AC9  9 PRO C 279                                                     
SITE     1 BC1  7 LYS C 104  PHE C 163  ARG C 172  ASP C 185                    
SITE     2 BC1  7 TYR C 189  NAP C1340  HOH C2275                               
SITE     1 BC2  7 LYS A 104  PHE A 163  ARG A 172  ASP A 185                    
SITE     2 BC2  7 TYR A 189  NAP A1340  HOH A2315                               
SITE     1 BC3  7 LYS D 104  PHE D 163  ARG D 172  ASP D 185                    
SITE     2 BC3  7 TYR D 189  NAP D1340  HOH D2137                               
SITE     1 BC4  7 LYS E 104  PHE E 163  ARG E 172  ASP E 185                    
SITE     2 BC4  7 TYR E 189  NAP E1340  HOH E2217                               
SITE     1 BC5  6 LEU A 230  LYS A 338  HOH A2308  GLU E 209                    
SITE     2 BC5  6 ALA E 331  HOH E2218                                          
SITE     1 BC6  7 LYS B 104  PHE B 163  ARG B 172  ASP B 185                    
SITE     2 BC6  7 TYR B 189  NAP B1340  HOH B2171                               
SITE     1 BC7  7 TYR A  48  GLN A  51  HOH A2010  HOH A2011                    
SITE     2 BC7  7 HOH A2316  HOH A2317  PRO F 282                               
SITE     1 BC8  6 GLN E 136  ALA E 137  TYR E 267  GLN E 292                    
SITE     2 BC8  6 HOH E2095  HOH E2219                                          
SITE     1 BC9  7 ARG A 155  PRO A 255  HOH A2174  ASP E 212                    
SITE     2 BC9  7 ASP E 215  SER E 244  HOH E2164                               
SITE     1 CC1  6 ARG B 155  HOH B2156  ASP D 212  ASP D 215                    
SITE     2 CC1  6 SER D 244  HOH D2167                                          
SITE     1 CC2  8 ARG C 155  PRO C 255  HOH C2138  ASP F 212                    
SITE     2 CC2  8 ASP F 215  ARG F 217  SER F 244  HOH F2232                    
SITE     1 CC3  6 LYS C 338  HOH C2272  VAL F 208  GLU F 209                    
SITE     2 CC3  6 ALA F 331  HOH F2233                                          
SITE     1 CC4  6 ARG B 251  TRP B 258  GLU B 260  ARG B 273                    
SITE     2 CC4  6 ASP D 262  PRO D 263                                          
SITE     1 CC5  5 ILE E 165  GLY E 166  ASP E 167  GLN E 170                    
SITE     2 CC5  5 HOH E2128                                                     
SITE     1 CC6  3 LYS D 290  ASN D 291  HOH D2185                               
SITE     1 CC7  5 ILE A 165  GLY A 166  ASP A 167  GLN A 170                    
SITE     2 CC7  5 HOH A2189                                                     
SITE     1 CC8  4 ILE D 165  GLY D 166  ASP D 167  GLN D 170                    
SITE     1 CC9  4 ILE C 165  GLY C 166  ASP C 167  GLN C 170                    
SITE     1 DC1  4 GLU C  28  LYS C 290  ASN C 291  HOH C2248                    
SITE     1 DC2  6 HOH B2061  GLN C 170  TRP C 171  NAP C1340                    
SITE     2 DC2  6 HOH C2152  HOH C2274                                          
SITE     1 DC3  6 GLN E 170  TRP E 171  NAP E1340  HOH E2126                    
SITE     2 DC3  6 HOH E2129  HOH E2216                                          
CRYST1  101.310  153.590  108.010  90.00 109.85  90.00 P 1 21 1     12          
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      0.009871  0.000000  0.003563        0.00000                         
SCALE2      0.000000  0.006511  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009843        0.00000                         
MTRIX1   1  0.222400 -0.676100 -0.702400       70.85670    1                    
MTRIX2   1 -0.751400 -0.577900  0.318400       24.39160    1                    
MTRIX3   1 -0.621200  0.457000 -0.636600       63.42170    1                    
MTRIX1   2 -0.059300 -0.819800  0.569600       24.25470    1                    
MTRIX2   2  0.828600 -0.358600 -0.429900       -9.55710    1                    
MTRIX3   2  0.556700  0.446400  0.700600      -18.51880    1                    
MTRIX1   3 -0.199400  0.736600 -0.646200       58.40950    1                    
MTRIX2   3  0.660100 -0.588400 -0.467000       -2.96390    1                    
MTRIX3   3 -0.724300 -0.333400 -0.603600       66.63540    1                    
MTRIX1   4 -0.982500  0.186100 -0.011600       83.39430    1                    
MTRIX2   4  0.184200  0.958700 -0.216700       -2.63010    1                    
MTRIX3   4 -0.029200 -0.215000 -0.976200       47.09970    1                    
MTRIX1   5 -0.334800  0.543800  0.769600       16.62680    1                    
MTRIX2   5 -0.542300 -0.779100  0.314500       19.91380    1                    
MTRIX3   5  0.770600 -0.312100  0.555700      -21.50360    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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