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Database: PDB
Entry: 1Q1N
LinkDB: 1Q1N
Original site: 1Q1N 
HEADER    OXIDOREDUCTASE                          22-JUL-03   1Q1N              
TITLE     APO AND HOLO STRUCTURES OF AN NADP(H)-DEPENDENT CINNAMYL ALCOHOL      
TITLE    2 DEHYDROGENASE FROM SACCHAROMYCES CEREVISIAE                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HYPOTHETICAL ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE PROTEIN  
COMPND   3 IN PRE5-FET4 INTERGENIC REGION;                                      
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: CINNAMYL ALCOHOL DEHYDROGENASE;                             
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 GENE: YMR318C (ADH6);                                                
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BJ2168;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PYES2-YMR318C                             
KEYWDS    ADH TOPOLOGY, NADP(H)-DEPENDENT, OXIDOREDUCTASE                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.VALENCIA,C.LARROY,W.F.OCHOA,X.PARES,I.FITA,J.A.BIOSCA               
REVDAT   4   14-FEB-24 1Q1N    1       REMARK LINK                              
REVDAT   3   24-FEB-09 1Q1N    1       VERSN                                    
REVDAT   2   17-AUG-04 1Q1N    1       JRNL                                     
REVDAT   1   03-AUG-04 1Q1N    0                                                
JRNL        AUTH   E.VALENCIA,C.LARROY,W.F.OCHOA,X.PARES,I.FITA,J.A.BIOSCA      
JRNL        TITL   APO AND HOLO STRUCTURES OF AN NADP(H)-DEPENDENT CINNAMYL     
JRNL        TITL 2 ALCOHOL DEHYDROGENASE FROM SACCHAROMYCES CEREVISIAE          
JRNL        REF    J.MOL.BIOL.                   V. 341  1049 2004              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   15289102                                                     
JRNL        DOI    10.1016/J.JMB.2004.06.037                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   E.VALENCIA,A.ROSELL,C.LARROY,J.FARRES,J.A.BIOSCA,I.FITA,     
REMARK   1  AUTH 2 X.PARES,W.F.OCHOA                                            
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF            
REMARK   1  TITL 2 NADP(H)-DEPENDENT ALCOHOL DEHYDROGENASES FROM SACCHAROMYCES  
REMARK   1  TITL 3 CEREVISIAE AND RANA PEREZI                                   
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  59   334 2003              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  DOI    10.1107/S090744490201661X                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 5.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 11225                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.240                           
REMARK   3   FREE R VALUE                     : 0.283                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1117                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2780                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
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) : -9.02100                                             
REMARK   3    B22 (A**2) : -9.02100                                             
REMARK   3    B33 (A**2) : 18.04200                                             
REMARK   3    B12 (A**2) : -13.75400                                            
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1Q1N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-03.                  
REMARK 100 THE DEPOSITION ID IS D_1000019803.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-JUN-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.28197                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15485                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 78.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULFATE, PH 8.0, VAPOR       
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       99.43333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       49.71667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       49.71667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       99.43333            
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 300 REMARK: THE BIOLOGICAL UNIT IS GENERATED BY CHAIN A (X,Y,Z (1_555),  
REMARK 300 Y,X,1-Z (4_556)).                                                    
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 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 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      149.15000            
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    SER A   2      170.51    -51.34                                   
REMARK 500    TYR A   3      -94.47    -35.10                                   
REMARK 500    PRO A   4      -80.05     -4.57                                   
REMARK 500    ALA A  42      143.15   -175.68                                   
REMARK 500    PRO A  63      172.08    -58.23                                   
REMARK 500    HIS A  68       40.56   -151.61                                   
REMARK 500    LYS A  76      109.43    176.78                                   
REMARK 500    ASN A  82        1.75   -161.47                                   
REMARK 500    CYS A 103      170.69    -57.64                                   
REMARK 500    ASP A 109       54.88     71.40                                   
REMARK 500    ASN A 110       39.05   -142.01                                   
REMARK 500    LYS A 116       31.58    -96.83                                   
REMARK 500    SER A 122        1.34     81.59                                   
REMARK 500    SER A 131      125.54    -37.67                                   
REMARK 500    GLN A 132     -138.14   -116.40                                   
REMARK 500    CYS A 163      -74.45   -132.39                                   
REMARK 500    LEU A 188       63.27    -66.48                                   
REMARK 500    SER A 212     -155.07    -79.91                                   
REMARK 500    ASP A 235       79.55   -159.23                                   
REMARK 500    PHE A 241      133.46    -33.08                                   
REMARK 500    GLU A 279       94.70    -45.57                                   
REMARK 500    GLN A 280      -44.45     -4.43                                   
REMARK 500    HIS A 281       -6.59    -58.60                                   
REMARK 500    LEU A 291       45.38    -73.37                                   
REMARK 500    LEU A 301     -135.70     31.95                                   
REMARK 500    ASP A 318       76.82     42.68                                   
REMARK 500    ALA A 331      -71.30    -84.47                                   
REMARK 500    PHE A 337      -72.36    -56.79                                   
REMARK 500    GLU A 338      -62.74    -26.76                                   
REMARK 500    ARG A 346       38.42    -77.86                                   
REMARK 500    TYR A 347      -62.92    101.04                                   
REMARK 500    LYS A 356       59.12   -104.63                                   
REMARK 500    GLU A 357      -25.49   -151.30                                   
REMARK 500    SER A 359     -151.45     54.01                                   
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 A1502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  46   SG                                                     
REMARK 620 2 HIS A  68   NE2  89.6                                              
REMARK 620 3 CYS A 163   SG   99.7  81.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 100   SG                                                     
REMARK 620 2 CYS A 103   SG  103.4                                              
REMARK 620 3 CYS A 106   SG  106.5  85.5                                        
REMARK 620 4 CYS A 114   SG  112.0 131.7 113.2                                  
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 1501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1502                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1PIW   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN IN A HETERODIMERIC FORM                             
REMARK 900 RELATED ID: 1PS0   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH NADP                                 
DBREF  1Q1N A    1   360  UNP    Q04894   ADH6_YEAST       1    360             
SEQRES   1 A  360  MET SER TYR PRO GLU LYS PHE GLU GLY ILE ALA ILE GLN          
SEQRES   2 A  360  SER HIS GLU ASP TRP LYS ASN PRO LYS LYS THR LYS TYR          
SEQRES   3 A  360  ASP PRO LYS PRO PHE TYR ASP HIS ASP ILE ASP ILE LYS          
SEQRES   4 A  360  ILE GLU ALA CYS GLY VAL CYS GLY SER ASP ILE HIS CYS          
SEQRES   5 A  360  ALA ALA GLY HIS TRP GLY ASN MET LYS MET PRO LEU VAL          
SEQRES   6 A  360  VAL GLY HIS GLU ILE VAL GLY LYS VAL VAL LYS LEU GLY          
SEQRES   7 A  360  PRO LYS SER ASN SER GLY LEU LYS VAL GLY GLN ARG VAL          
SEQRES   8 A  360  GLY VAL GLY ALA GLN VAL PHE SER CYS LEU GLU CYS ASP          
SEQRES   9 A  360  ARG CYS LYS ASN ASP ASN GLU PRO TYR CYS THR LYS PHE          
SEQRES  10 A  360  VAL THR THR TYR SER GLN PRO TYR GLU ASP GLY TYR VAL          
SEQRES  11 A  360  SER GLN GLY GLY TYR ALA ASN TYR VAL ARG VAL HIS GLU          
SEQRES  12 A  360  HIS PHE VAL VAL PRO ILE PRO GLU ASN ILE PRO SER HIS          
SEQRES  13 A  360  LEU ALA ALA PRO LEU LEU CYS GLY GLY LEU THR VAL TYR          
SEQRES  14 A  360  SER PRO LEU VAL ARG ASN GLY CYS GLY PRO GLY LYS LYS          
SEQRES  15 A  360  VAL GLY ILE VAL GLY LEU GLY GLY ILE GLY SER MET GLY          
SEQRES  16 A  360  THR LEU ILE SER LYS ALA MET GLY ALA GLU THR TYR VAL          
SEQRES  17 A  360  ILE SER ARG SER SER ARG LYS ARG GLU ASP ALA MET LYS          
SEQRES  18 A  360  MET GLY ALA ASP HIS TYR ILE ALA THR LEU GLU GLU GLY          
SEQRES  19 A  360  ASP TRP GLY GLU LYS TYR PHE ASP THR PHE ASP LEU ILE          
SEQRES  20 A  360  VAL VAL CYS ALA SER SER LEU THR ASP ILE ASP PHE ASN          
SEQRES  21 A  360  ILE MET PRO LYS ALA MET LYS VAL GLY GLY ARG ILE VAL          
SEQRES  22 A  360  SER ILE SER ILE PRO GLU GLN HIS GLU MET LEU SER LEU          
SEQRES  23 A  360  LYS PRO TYR GLY LEU LYS ALA VAL SER ILE SER TYR SER          
SEQRES  24 A  360  ALA LEU GLY SER ILE LYS GLU LEU ASN GLN LEU LEU LYS          
SEQRES  25 A  360  LEU VAL SER GLU LYS ASP ILE LYS ILE TRP VAL GLU THR          
SEQRES  26 A  360  LEU PRO VAL GLY GLU ALA GLY VAL HIS GLU ALA PHE GLU          
SEQRES  27 A  360  ARG MET GLU LYS GLY ASP VAL ARG TYR ARG PHE THR LEU          
SEQRES  28 A  360  VAL GLY TYR ASP LYS GLU PHE SER ASP                          
HET     ZN  A1501       1                                                       
HET     ZN  A1502       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   2   ZN    2(ZN 2+)                                                     
HELIX    1   1 SER A   14  TRP A   18  5                                   5    
HELIX    2   2 CYS A   46  ALA A   54  1                                   9    
HELIX    3   3 CYS A  103  ASN A  108  1                                   6    
HELIX    4   4 ASN A  110  CYS A  114  5                                   5    
HELIX    5   5 HIS A  144  VAL A  146  5                                   3    
HELIX    6   6 PRO A  154  LEU A  162  5                                   9    
HELIX    7   7 CYS A  163  ASN A  175  1                                  13    
HELIX    8   8 GLY A  189  MET A  202  1                                  14    
HELIX    9   9 LYS A  215  MET A  222  1                                   8    
HELIX   10  10 LEU A  231  GLU A  233  5                                   3    
HELIX   11  11 ASP A  235  TYR A  240  1                                   6    
HELIX   12  12 ILE A  261  LYS A  264  5                                   4    
HELIX   13  13 LYS A  287  LEU A  291  5                                   5    
HELIX   14  14 SER A  303  LYS A  317  1                                  15    
HELIX   15  15 GLY A  329  GLY A  343  1                                  15    
HELIX   16  16 TYR A  354  SER A  359  1                                   6    
SHEET    1   A 2 PHE A   7  ALA A  11  0                                        
SHEET    2   A 2 LYS A  22  TYR A  26 -1  O  TYR A  26   N  PHE A   7           
SHEET    1   B 5 TYR A 138  HIS A 142  0                                        
SHEET    2   B 5 ASP A  35  VAL A  45 -1  N  ILE A  38   O  VAL A 139           
SHEET    3   B 5 ILE A  70  LEU A  77 -1  O  LYS A  73   N  LYS A  39           
SHEET    4   B 5 ARG A  90  VAL A  93 -1  O  VAL A  91   N  GLY A  72           
SHEET    5   B 5 VAL A 147  PRO A 148 -1  O  VAL A 147   N  GLY A  92           
SHEET    1   C 4 TYR A 138  HIS A 142  0                                        
SHEET    2   C 4 ASP A  35  VAL A  45 -1  N  ILE A  38   O  VAL A 139           
SHEET    3   C 4 ARG A 348  VAL A 352 -1  O  PHE A 349   N  VAL A  45           
SHEET    4   C 4 VAL A 323  PRO A 327  1  N  GLU A 324   O  ARG A 348           
SHEET    1   D 2 GLN A  96  PHE A  98  0                                        
SHEET    2   D 2 VAL A 118  THR A 119 -1  O  VAL A 118   N  PHE A  98           
SHEET    1   E 6 HIS A 226  ALA A 229  0                                        
SHEET    2   E 6 GLU A 205  SER A 210  1  N  VAL A 208   O  HIS A 226           
SHEET    3   E 6 LYS A 182  VAL A 186  1  N  VAL A 183   O  TYR A 207           
SHEET    4   E 6 PHE A 244  VAL A 249  1  O  VAL A 248   N  GLY A 184           
SHEET    5   E 6 MET A 266  SER A 274  1  O  LYS A 267   N  PHE A 244           
SHEET    6   E 6 SER A 295  TYR A 298  1  O  SER A 295   N  ILE A 272           
LINK         SG  CYS A  46                ZN    ZN A1502     1555   1555  2.57  
LINK         NE2 HIS A  68                ZN    ZN A1502     1555   1555  2.36  
LINK         SG  CYS A 100                ZN    ZN A1501     1555   1555  2.39  
LINK         SG  CYS A 103                ZN    ZN A1501     1555   1555  2.44  
LINK         SG  CYS A 106                ZN    ZN A1501     1555   1555  2.35  
LINK         SG  CYS A 114                ZN    ZN A1501     1555   1555  2.58  
LINK         SG  CYS A 163                ZN    ZN A1502     1555   1555  2.45  
CISPEP   1 MET A   62    PRO A   63          0         0.07                     
SITE     1 AC1  4 CYS A 100  CYS A 103  CYS A 106  CYS A 114                    
SITE     1 AC2  4 CYS A  46  SER A  48  HIS A  68  CYS A 163                    
CRYST1  101.900  101.900  149.150  90.00  90.00 120.00 P 32 2 1      6          
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      0.009814  0.005666  0.000000        0.00000                         
SCALE2      0.000000  0.011332  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006705        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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