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Database: PDB
Entry: 1FW1
LinkDB: 1FW1
Original site: 1FW1 
HEADER    ISOMERASE/TRANSFERASE                   20-SEP-00   1FW1              
TITLE     GLUTATHIONE TRANSFERASE ZETA/MALEYLACETOACETATE ISOMERASE             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE TRANSFERASE ZETA;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MALEYLACETOACETATE ISOMERASE;                               
COMPND   5 EC: 5.2.1.2, 2.5.1.18;                                               
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    GLUTATHIONE TRANSFERASE, ISOMERASE-TRANSFERASE COMPLEX                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.POLEKHINA,P.G.BOARD,A.C.BLACKBURN,M.W.PARKER                        
REVDAT   4   13-JUL-11 1FW1    1       VERSN                                    
REVDAT   3   03-NOV-09 1FW1    1       HETATM REMARK                            
REVDAT   2   24-FEB-09 1FW1    1       VERSN                                    
REVDAT   1   26-SEP-01 1FW1    0                                                
JRNL        AUTH   G.POLEKHINA,P.G.BOARD,A.C.BLACKBURN,M.W.PARKER               
JRNL        TITL   CRYSTAL STRUCTURE OF MALEYLACETOACETATE                      
JRNL        TITL 2 ISOMERASE/GLUTATHIONE TRANSFERASE ZETA REVEALS THE MOLECULAR 
JRNL        TITL 3 BASIS FOR ITS REMARKABLE CATALYTIC PROMISCUITY.              
JRNL        REF    BIOCHEMISTRY                  V.  40  1567 2001              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   11327815                                                     
JRNL        DOI    10.1021/BI002249Z                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.C.BLACKBURN,E.WOOLLATT,G.R.SUTHERLAND,P.G.BOARD            
REMARK   1  TITL   CHARACTERIZATION AND CHROMOSOME LOCATION OF THE GENE GSTZ1   
REMARK   1  TITL 2 ENCODING THE HUMAN ZETA CLASS GLUTATHIONE TRANSFERASE AND    
REMARK   1  TITL 3 MALEYLACETOACETATE ISOMERASE                                 
REMARK   1  REF    CYTOGENET.CELL GENET.         V.  83   109 1998              
REMARK   1  REFN                   ISSN 0301-0171                               
REMARK   1  DOI    10.1159/000015145                                            
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   Z.TONG,P.G.BOARD,M.W.ANDERS                                  
REMARK   1  TITL   GLUTATHIONE TRANSFERASE ZETA CATALYSES THE OXYGENATION OF    
REMARK   1  TITL 2 THE CARCINOGEN DICHLOROACETIC ACID TO GLYOXYLIC ACID         
REMARK   1  REF    BIOCHEM.J.                    V. 331   371 1998              
REMARK   1  REFN                   ISSN 0264-6021                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.9                                              
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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.76                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1875438.060                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 22697                          
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) : 0.234                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.200                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 2317                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.02                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2977                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4390                       
REMARK   3   BIN FREE R VALUE                    : 0.4630                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.30                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 341                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.025                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1630                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 109                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -17.76000                                            
REMARK   3    B22 (A**2) : -17.76000                                            
REMARK   3    B33 (A**2) : 35.53000                                             
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.29                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.54                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.34                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.56                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.018                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.90                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.21                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 0.960 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.540 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.600 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.320 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.39                                                 
REMARK   3   BSOL        : 55.05                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : GSH_1.PAR                                      
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : GSH_1.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1FW1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-SEP-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB011949.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-MAR-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 9.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 14-BM-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
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   : 152479                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.04900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 35.3000                            
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) : 1.94                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.28600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, TERT-BUTANOL,          
REMARK 280  BICINE, GLUTATHIONE, PH 9.5, VAPOR DIFFUSION, HANGING DROP,         
REMARK 280  TEMPERATURE 22K, TEMPERATURE 295K                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 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   -Y+1/2,X+1/2,Z                                          
REMARK 290       4555   Y+1/2,-X+1/2,Z                                          
REMARK 290       5555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       6555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       50.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       50.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       50.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       50.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       50.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       50.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       50.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       50.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
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 ASSEMBLY IS A DIMER.                          
REMARK 300 THE DIMER CAN BE CREATED FROM MONOMER A                              
REMARK 300 THROUGH THE CRYSTALLOGRAPHIC 2-FOLD AXIS.                            
REMARK 300 THE SYMMETRY OPERATION TO BE USED IS Y,X,-Z.                         
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,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 5640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -91.0 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  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
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 326  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 327  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     MET A     1                                                      
REMARK 465     GLN A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     GLU A   213                                                      
REMARK 465     LEU A   214                                                      
REMARK 465     ARG A   215                                                      
REMARK 465     ALA A   216                                                      
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  65       27.31     47.19                                   
REMARK 500    GLN A  71      106.41     84.19                                   
REMARK 500    ILE A 110      -61.95   -125.74                                   
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 SO4 A 218                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT A 220                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH A 217                 
DBREF  1FW1 A    1   216  UNP    O43708   MAAI_HUMAN       1    216             
SEQRES   1 A  216  MET GLN ALA GLY LYS PRO ILE LEU TYR SER TYR PHE ARG          
SEQRES   2 A  216  SER SER CYS SER TRP ARG VAL ARG ILE ALA LEU ALA LEU          
SEQRES   3 A  216  LYS GLY ILE ASP TYR LYS THR VAL PRO ILE ASN LEU ILE          
SEQRES   4 A  216  LYS ASP GLY GLY GLN GLN PHE SER LYS ASP PHE GLN ALA          
SEQRES   5 A  216  LEU ASN PRO MET LYS GLN VAL PRO THR LEU LYS ILE ASP          
SEQRES   6 A  216  GLY ILE THR ILE HIS GLN SER LEU ALA ILE ILE GLU TYR          
SEQRES   7 A  216  LEU GLU GLU THR ARG PRO THR PRO ARG LEU LEU PRO GLN          
SEQRES   8 A  216  ASP PRO LYS LYS ARG ALA SER VAL ARG MET ILE SER ASP          
SEQRES   9 A  216  LEU ILE ALA GLY GLY ILE GLN PRO LEU GLN ASN LEU SER          
SEQRES  10 A  216  VAL LEU LYS GLN VAL GLY GLU GLU MET GLN LEU THR TRP          
SEQRES  11 A  216  ALA GLN ASN ALA ILE THR CYS GLY PHE ASN ALA LEU GLU          
SEQRES  12 A  216  GLN ILE LEU GLN SER THR ALA GLY ILE TYR CYS VAL GLY          
SEQRES  13 A  216  ASP GLU VAL THR MET ALA ASP LEU CYS LEU VAL PRO GLN          
SEQRES  14 A  216  VAL ALA ASN ALA GLU ARG PHE LYS VAL ASP LEU THR PRO          
SEQRES  15 A  216  TYR PRO THR ILE SER SER ILE ASN LYS ARG LEU LEU VAL          
SEQRES  16 A  216  LEU GLU ALA PHE GLN VAL SER HIS PRO CYS ARG GLN PRO          
SEQRES  17 A  216  ASP THR PRO THR GLU LEU ARG ALA                              
HET    SO4  A 218       5                                                       
HET    DTT  A 220       8                                                       
HET    GSH  A 217      20                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE                                   
HETNAM     GSH GLUTATHIONE                                                      
HETSYN     DTT 1,4-DITHIOTHREITOL                                               
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3  DTT    C4 H10 O2 S2                                                 
FORMUL   4  GSH    C10 H17 N3 O6 S                                              
FORMUL   5  HOH   *109(H2 O)                                                    
HELIX    1   1 SER A   14  LYS A   27  1                                  14    
HELIX    2   2 GLY A   43  PHE A   46  5                                   4    
HELIX    3   3 SER A   47  ASN A   54  1                                   8    
HELIX    4   4 GLN A   71  ARG A   83  1                                  13    
HELIX    5   5 ASP A   92  ILE A  110  1                                  19    
HELIX    6   6 GLN A  111  GLN A  114  5                                   4    
HELIX    7   7 ASN A  115  GLY A  123  1                                   9    
HELIX    8   8 GLY A  123  ALA A  150  1                                  28    
HELIX    9   9 THR A  160  PHE A  176  1                                  17    
HELIX   10  10 TYR A  183  VAL A  195  1                                  13    
HELIX   11  11 LEU A  196  GLN A  200  5                                   5    
HELIX   12  12 HIS A  203  GLN A  207  5                                   5    
SHEET    1   A 4 LYS A  32  PRO A  35  0                                        
SHEET    2   A 4 ILE A   7  SER A  10  1  N  LEU A   8   O  LYS A  32           
SHEET    3   A 4 THR A  61  ILE A  64 -1  O  THR A  61   N  TYR A   9           
SHEET    4   A 4 ILE A  67  HIS A  70 -1  N  ILE A  67   O  ILE A  64           
LINK         SG  CYS A 205                 S1  DTT A 220     1555   1555  2.04  
CISPEP   1 VAL A   59    PRO A   60          0         1.05                     
CISPEP   2 THR A   85    PRO A   86          0        -0.76                     
SITE     1 AC1 10 ARG A  13  SER A  15  GLN A 111  GLN A 114                    
SITE     2 AC1 10 ASN A 172  ARG A 175  GSH A 217  HOH A 229                    
SITE     3 AC1 10 HOH A 236  HOH A 288                                          
SITE     1 AC2  3 PHE A  12  CYS A 205  HOH A 322                               
SITE     1 AC3 22 SER A  14  CYS A  16  ARG A  19  LEU A  38                    
SITE     2 AC3 22 GLN A  45  GLN A  58  VAL A  59  PRO A  60                    
SITE     3 AC3 22 GLN A  71  SER A  72  GLN A 111  ASN A 115                    
SITE     4 AC3 22 LEU A 116  SER A 117  SO4 A 218  HOH A 221                    
SITE     5 AC3 22 HOH A 224  HOH A 226  HOH A 272  HOH A 274                    
SITE     6 AC3 22 HOH A 292  HOH A 328                                          
CRYST1  100.000  100.000   56.900  90.00  90.00  90.00 P 4 21 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      0.010000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017575        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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