GenomeNet

Database: PDB
Entry: 3QE3
LinkDB: 3QE3
Original site: 3QE3 
HEADER    OXIDOREDUCTASE                          19-JAN-11   3QE3              
TITLE     SHEEP LIVER SORBITOL DEHYDROGENASE                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SORBITOL DEHYDROGENASE;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: L-IDITOL 2-DEHYDROGENASE;                                   
COMPND   5 EC: 1.1.1.14;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: OVIS ARIES;                                     
SOURCE   3 ORGANISM_COMMON: SHEEP;                                              
SOURCE   4 ORGANISM_TAXID: 9940;                                                
SOURCE   5 ORGAN: LIVER;                                                        
SOURCE   6 GENE: SORD;                                                          
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    MEDIUM CHAIN DEHYDROGENASE/REDUCTASE ENZYMES, OXIDOREDUCTASE          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.H.YENNAWAR,H.P.YENNAWAR                                             
REVDAT   2   27-MAR-13 3QE3    1       JRNL   VERSN                             
REVDAT   1   27-APR-11 3QE3    0                                                
JRNL        AUTH   H.YENNAWAR,M.MOLLER,R.GILLILAN,N.YENNAWAR                    
JRNL        TITL   X-RAY CRYSTAL STRUCTURE AND SMALL-ANGLE X-RAY SCATTERING OF  
JRNL        TITL 2 SHEEP LIVER SORBITOL DEHYDROGENASE.                          
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  67   440 2011              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   21543846                                                     
JRNL        DOI    10.1107/S0907444911007815                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 27476                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1391                            
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 20.0029 -  4.0830    0.99     2759   161  0.1556 0.1841        
REMARK   3     2  4.0830 -  3.2453    0.99     2666   118  0.1578 0.2048        
REMARK   3     3  3.2453 -  2.8363    0.99     2666   142  0.1917 0.2202        
REMARK   3     4  2.8363 -  2.5776    0.99     2604   156  0.2136 0.2637        
REMARK   3     5  2.5776 -  2.3932    0.99     2572   137  0.2133 0.2735        
REMARK   3     6  2.3932 -  2.2523    0.97     2554   132  0.2207 0.2935        
REMARK   3     7  2.2523 -  2.1396    0.98     2562   144  0.2249 0.2726        
REMARK   3     8  2.1396 -  2.0466    0.99     2588   140  0.2311 0.2868        
REMARK   3     9  2.0466 -  1.9679    0.97     2561   125  0.2291 0.2671        
REMARK   3    10  1.9679 -  1.9000    0.98     2553   136  0.3035 0.3240        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.95                                          
REMARK   3   K_SOL              : 0.37                                          
REMARK   3   B_SOL              : 40.68                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.250            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.710           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.00660                                             
REMARK   3    B22 (A**2) : 6.48260                                              
REMARK   3    B33 (A**2) : -5.47600                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
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           2711                                  
REMARK   3   ANGLE     :  1.077           3676                                  
REMARK   3   CHIRALITY :  0.071            422                                  
REMARK   3   PLANARITY :  0.005            478                                  
REMARK   3   DIHEDRAL  : 11.604            998                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: all                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  20.0700  28.2796  75.8717              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1311 T22:   0.1741                                     
REMARK   3      T33:   0.0830 T12:  -0.0390                                     
REMARK   3      T13:   0.0246 T23:   0.0128                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5126 L22:   0.5968                                     
REMARK   3      L33:   1.8648 L12:  -0.0507                                     
REMARK   3      L13:  -0.3983 L23:  -0.3229                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1156 S12:  -0.0593 S13:  -0.0784                       
REMARK   3      S21:   0.0178 S22:   0.0527 S23:   0.0087                       
REMARK   3      S31:   0.3136 S32:  -0.3611 S33:   0.0562                       
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 3QE3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JAN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB063528.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : VARIMAX HF OPTIC                   
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944+                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27863                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 2.300                              
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.93                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1PL8                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LITHIUM ACETATE DYHYDRATE, 20%     
REMARK 280  PEG3350, PH 7.0, LASER-INDUCED NUCLEATION, SITTING DROP,            
REMARK 280  TEMPERATURE 294.0K                                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       33.87450            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       42.94050            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       59.94400            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       33.87450            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       42.94050            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       59.94400            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       33.87450            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       42.94050            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       59.94400            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       33.87450            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       42.94050            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       59.94400            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13250 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 48440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -223.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       67.74900            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       85.88100            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000       67.74900            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000      119.88800            
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000       85.88100            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000      119.88800            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 481  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 533  LIES ON A SPECIAL POSITION.                          
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     LYS A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     ALA A     4                                                      
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    PRO A  15      106.67    -47.81                                   
REMARK 500    HIS A  38      -60.33   -121.59                                   
REMARK 500    ARG A 108       55.81   -119.75                                   
REMARK 500    SER A 223      -91.68   -131.41                                   
REMARK 500    ARG A 297     -110.06     60.65                                   
REMARK 500    LEU A 342      -83.92   -116.83                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 356  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 470   O                                                      
REMARK 620 2 GLU A  69   OE2  90.6                                              
REMARK 620 3 HIS A  68   NE2 127.6 120.6                                        
REMARK 620 4 CYS A  43   SG  112.3  95.1 105.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 356                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 357                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 358                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 359                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 360                 
DBREF  3QE3 A    1   355  UNP    P07846   DHSO_SHEEP       1    354             
SEQADV 3QE3 HIS A   52  UNP  P07846              INSERTION                      
SEQRES   1 A  355  ALA LYS PRO ALA ALA GLU ASN LEU SER LEU VAL VAL HIS          
SEQRES   2 A  355  GLY PRO GLY ASP LEU ARG LEU GLU ASN TYR PRO ILE PRO          
SEQRES   3 A  355  GLU PRO GLY PRO ASN GLU VAL LEU LEU LYS MET HIS SER          
SEQRES   4 A  355  VAL GLY ILE CYS GLY SER ASP VAL HIS TYR TRP GLN HIS          
SEQRES   5 A  355  GLY ARG ILE GLY ASP PHE VAL VAL LYS LYS PRO MET VAL          
SEQRES   6 A  355  LEU GLY HIS GLU ALA SER GLY THR VAL VAL LYS VAL GLY          
SEQRES   7 A  355  SER LEU VAL ARG HIS LEU GLN PRO GLY ASP ARG VAL ALA          
SEQRES   8 A  355  ILE GLN PRO GLY ALA PRO ARG GLN THR ASP GLU PHE CYS          
SEQRES   9 A  355  LYS ILE GLY ARG TYR ASN LEU SER PRO THR ILE PHE PHE          
SEQRES  10 A  355  CYS ALA THR PRO PRO ASP ASP GLY ASN LEU CYS ARG PHE          
SEQRES  11 A  355  TYR LYS HIS ASN ALA ASN PHE CYS TYR LYS LEU PRO ASP          
SEQRES  12 A  355  ASN VAL THR PHE GLU GLU GLY ALA LEU ILE GLU PRO LEU          
SEQRES  13 A  355  SER VAL GLY ILE HIS ALA CYS ARG ARG ALA GLY VAL THR          
SEQRES  14 A  355  LEU GLY ASN LYS VAL LEU VAL CYS GLY ALA GLY PRO ILE          
SEQRES  15 A  355  GLY LEU VAL ASN LEU LEU ALA ALA LYS ALA MET GLY ALA          
SEQRES  16 A  355  ALA GLN VAL VAL VAL THR ASP LEU SER ALA SER ARG LEU          
SEQRES  17 A  355  SER LYS ALA LYS GLU VAL GLY ALA ASP PHE ILE LEU GLU          
SEQRES  18 A  355  ILE SER ASN GLU SER PRO GLU GLU ILE ALA LYS LYS VAL          
SEQRES  19 A  355  GLU GLY LEU LEU GLY SER LYS PRO GLU VAL THR ILE GLU          
SEQRES  20 A  355  CYS THR GLY VAL GLU THR SER ILE GLN ALA GLY ILE TYR          
SEQRES  21 A  355  ALA THR HIS SER GLY GLY THR LEU VAL LEU VAL GLY LEU          
SEQRES  22 A  355  GLY SER GLU MET THR SER VAL PRO LEU VAL HIS ALA ALA          
SEQRES  23 A  355  THR ARG GLU VAL ASP ILE LYS GLY VAL PHE ARG TYR CYS          
SEQRES  24 A  355  ASN THR TRP PRO MET ALA ILE SER MET LEU ALA SER LYS          
SEQRES  25 A  355  SER VAL ASN VAL LYS PRO LEU VAL THR HIS ARG PHE PRO          
SEQRES  26 A  355  LEU GLU LYS ALA LEU GLU ALA PHE GLU THR SER LYS LYS          
SEQRES  27 A  355  GLY LEU GLY LEU LYS VAL MET ILE LYS CYS ASP PRO SER          
SEQRES  28 A  355  ASP GLN ASN PRO                                              
HET     ZN  A 356       1                                                       
HET    GOL  A 357       6                                                       
HET    ACY  A 358       4                                                       
HET    ACY  A 359       4                                                       
HET    ACY  A 360       4                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     GOL GLYCEROL                                                         
HETNAM     ACY ACETIC ACID                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  GOL    C3 H8 O3                                                     
FORMUL   4  ACY    3(C2 H4 O2)                                                  
FORMUL   7  HOH   *214(H2 O)                                                    
HELIX    1   1 CYS A   43  GLY A   53  1                                  11    
HELIX    2   2 ASP A  101  ILE A  106  1                                   6    
HELIX    3   3 ARG A  108  SER A  112  5                                   5    
HELIX    4   4 THR A  146  GLY A  167  1                                  22    
HELIX    5   5 GLY A  180  MET A  193  1                                  14    
HELIX    6   6 SER A  204  GLY A  215  1                                  12    
HELIX    7   7 SER A  226  GLY A  239  1                                  14    
HELIX    8   8 VAL A  251  THR A  262  1                                  12    
HELIX    9   9 PRO A  281  ARG A  288  1                                   8    
HELIX   10  10 THR A  301  SER A  311  1                                  11    
HELIX   11  11 VAL A  316  PRO A  318  5                                   3    
HELIX   12  12 LYS A  328  GLY A  339  1                                  12    
SHEET    1   A 3 ASP A  17  ASN A  22  0                                        
SHEET    2   A 3 LEU A   8  GLY A  14 -1  N  SER A   9   O  GLU A  21           
SHEET    3   A 3 MET A  64  VAL A  65 -1  O  MET A  64   N  VAL A  12           
SHEET    1   B 5 PHE A 130  ASN A 134  0                                        
SHEET    2   B 5 GLU A  32  ILE A  42 -1  N  LEU A  35   O  TYR A 131           
SHEET    3   B 5 GLU A  69  VAL A  77 -1  O  THR A  73   N  LYS A  36           
SHEET    4   B 5 ARG A  89  ILE A  92 -1  O  VAL A  90   N  GLY A  72           
SHEET    5   B 5 CYS A 138  LYS A 140 -1  O  TYR A 139   N  ALA A  91           
SHEET    1   C 4 PHE A 130  ASN A 134  0                                        
SHEET    2   C 4 GLU A  32  ILE A  42 -1  N  LEU A  35   O  TYR A 131           
SHEET    3   C 4 LYS A 343  LYS A 347 -1  O  ILE A 346   N  VAL A  40           
SHEET    4   C 4 VAL A 320  PRO A 325  1  N  PHE A 324   O  LYS A 347           
SHEET    1   D 2 ARG A  54  ILE A  55  0                                        
SHEET    2   D 2 PHE A  58  VAL A  59 -1  O  PHE A  58   N  ILE A  55           
SHEET    1   E 2 GLY A  95  ALA A  96  0                                        
SHEET    2   E 2 PHE A 116  PHE A 117 -1  O  PHE A 116   N  ALA A  96           
SHEET    1   F 6 PHE A 218  GLU A 221  0                                        
SHEET    2   F 6 GLN A 197  ASP A 202  1  N  VAL A 200   O  LEU A 220           
SHEET    3   F 6 LYS A 173  CYS A 177  1  N  VAL A 176   O  VAL A 199           
SHEET    4   F 6 VAL A 244  GLU A 247  1  O  ILE A 246   N  LEU A 175           
SHEET    5   F 6 THR A 267  LEU A 270  1  O  VAL A 269   N  GLU A 247           
SHEET    6   F 6 ASP A 291  GLY A 294  1  O  ASP A 291   N  LEU A 268           
LINK        ZN    ZN A 356                 O   HOH A 470     1555   1555  2.03  
LINK         OE2 GLU A  69                ZN    ZN A 356     1555   1555  2.07  
LINK         NE2 HIS A  68                ZN    ZN A 356     1555   1555  2.10  
LINK         SG  CYS A  43                ZN    ZN A 356     1555   1555  2.40  
CISPEP   1 PRO A  121    PRO A  122          0         8.38                     
SITE     1 AC1  5 CYS A  43  HIS A  68  GLU A  69  GLU A 154                    
SITE     2 AC1  5 HOH A 470                                                     
SITE     1 AC2  5 TYR A  49  THR A 120  ARG A 297  ACY A 359                    
SITE     2 AC2  5 HOH A 489                                                     
SITE     1 AC3  3 GLN A 197  ALA A 310  HOH A 424                               
SITE     1 AC4  6 HIS A  68  GLU A 154  VAL A 158  GOL A 357                    
SITE     2 AC4  6 HOH A 470  HOH A 489                                          
SITE     1 AC5  3 GLU A  32  HIS A 133  ASN A 134                               
CRYST1   67.749   85.881  119.888  90.00  90.00  90.00 I 2 2 2       8          
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      0.014760  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011644  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008341        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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