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Database: PDB
Entry: 1HD2
LinkDB: 1HD2
Original site: 1HD2 
HEADER    ANTIOXIDANT ENZYME                      06-NOV-00   1HD2              
TITLE     HUMAN PEROXIREDOXIN 5                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEROXIREDOXIN 5 RESIDUES 54-214;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 54-214;                                           
COMPND   5 SYNONYM: PRDX5, PRXV, AOEB166, PMP20, ARC1;                          
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 ORGAN: LUNG;                                                         
SOURCE   6 ORGANELLE: MITOCHONDRIA-CYTOSOL-PEROXISOME;                          
SOURCE   7 CELLULAR_LOCATION: MITOCHONDRIA-CYTOSOL-PEROXISOME;                  
SOURCE   8 GENE: PRDX5, AOEB166, PMP20, ARC1;                                   
SOURCE   9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 1007065;                                    
SOURCE  11 EXPRESSION_SYSTEM_STRAIN: M15;                                       
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PQE-30                                    
KEYWDS    ANTIOXIDANT ENZYME, PEROXIREDOXIN, THIOREDOXIN PEROXIDASE,            
KEYWDS   2 THIOREDOXIN FOLD                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.P.DECLERCQ,C.EVRARD                                                 
REVDAT   6   04-MAR-20 1HD2    1       REMARK                                   
REVDAT   5   24-JUL-19 1HD2    1       REMARK                                   
REVDAT   4   22-MAY-19 1HD2    1       REMARK                                   
REVDAT   3   15-APR-15 1HD2    1       SOURCE JRNL   REMARK VERSN               
REVDAT   3 2                   1       DBREF  FORMUL                            
REVDAT   2   24-FEB-09 1HD2    1       VERSN                                    
REVDAT   1   28-AUG-01 1HD2    0                                                
JRNL        AUTH   J.P.DECLERCQ,C.EVRARD,A.CLIPPE,D.V.STRICHT,A.BERNARD,        
JRNL        AUTH 2 B.KNOOPS                                                     
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN PEROXIREDOXIN 5, A NOVEL TYPE OF  
JRNL        TITL 2 MAMMALIAN PEROXIREDOXIN AT 1.5 A RESOLUTION.                 
JRNL        REF    J.MOL.BIOL.                   V. 311   751 2001              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   11518528                                                     
JRNL        DOI    10.1006/JMBI.2001.4853                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   B.KNOOPS,A.CLIPPE,C.BOGARD,K.ARSALANE,R.WATTIEZ,C.HERMANS,   
REMARK   1  AUTH 2 E.DUCONSEILLE,P.FALMAGNE,A.BERNARD                           
REMARK   1  TITL   CLONING AND CHARACTERIZATION OF AOEB166, A NOVEL MAMMALIAN   
REMARK   1  TITL 2 ANTIOXIDANT ENZYME OF THE PEROXIREDOXIN FAMILY               
REMARK   1  REF    J.BIOL.CHEM.                  V. 274 30451 1999              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  PMID   10521424                                                     
REMARK   1  DOI    10.1074/JBC.274.43.30451                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 16.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   CROSS-VALIDATION METHOD           : FREE R-VALUE                   
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.133                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.133                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.165                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 2256                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 45181                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.126                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.126                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.157                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 2086                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 41443                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 1190                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 14                                            
REMARK   3   SOLVENT ATOMS      : 221                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 1424.5                  
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 1059.0                  
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 2                       
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 12850                   
REMARK   3   NUMBER OF RESTRAINTS                     : 15197                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.015                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.026                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.028                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.075                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.075                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.043                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.004                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.058                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.103                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-2          
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: ANISOTROPIC REFINEMENT REDUCED FREE R     
REMARK   3  (NO CUTOFF) BY 0.037                                                
REMARK   4                                                                      
REMARK   4 1HD2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-NOV-00.                  
REMARK 100 THE DEPOSITION ID IS D_1290005525.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-SEP-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.30                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X31                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1,0.9175,0.9169,0.855            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : TOROIDAL MIRROR                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45181                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 16.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 8.500                              
REMARK 200  R MERGE                    (I) : 0.05100                            
REMARK 200  R SYM                      (I) : 0.05100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.72                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.24600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.24600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
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   (%): 63.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 1.6 M      
REMARK 280  AMMONIUM SULFATE, 0.1 M SODIUM CITRATE BUFFER PH 5.3, 0.2 M         
REMARK 280  POTASSIUM SODIUM TARTRATE, 1 MM DTT, 0.02 % (W/V) SODIUM AZIDE,     
REMARK 280  PH 5.30                                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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       61.66350            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       33.30350            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       33.30350            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       30.83175            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       33.30350            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       33.30350            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       92.49525            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       33.30350            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       33.30350            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       30.83175            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       33.30350            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       33.30350            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       92.49525            
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       61.66350            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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       66.60700            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000       66.60700            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       61.66350            
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 A2057  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    TRP A  84   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    TRP A  84   CD1 -  NE1 -  CE2 ANGL. DEV. =   8.0 DEGREES          
REMARK 500    TRP A  84   NE1 -  CE2 -  CZ2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ARG A  86   CD  -  NE  -  CZ  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    ARG A  95   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG A 127   NE  -  CZ  -  NH2 ANGL. DEV. =   8.2 DEGREES          
REMARK 500    THR A 150   CA  -  CB  -  OG1 ANGL. DEV. =  14.1 DEGREES          
REMARK 500    CYS A 151   C   -  N   -  CA  ANGL. DEV. =  17.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  50      -57.35   -123.76                                   
REMARK 500    ASP A 113     -148.01    -87.96                                   
REMARK 500    THR A 150     -106.99   -136.92                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2033        DISTANCE =  5.93 ANGSTROMS                       
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: KABSCH AND SANDER                              
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: KABSCH AND SANDER                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEZ A 201                 
DBREF  1HD2 A    1   161  UNP    Q9UKX4   PRDX5_HUMAN     54    214             
SEQRES   1 A  161  ALA PRO ILE LYS VAL GLY ASP ALA ILE PRO ALA VAL GLU          
SEQRES   2 A  161  VAL PHE GLU GLY GLU PRO GLY ASN LYS VAL ASN LEU ALA          
SEQRES   3 A  161  GLU LEU PHE LYS GLY LYS LYS GLY VAL LEU PHE GLY VAL          
SEQRES   4 A  161  PRO GLY ALA PHE THR PRO GLY CYS SER LYS THR HIS LEU          
SEQRES   5 A  161  PRO GLY PHE VAL GLU GLN ALA GLU ALA LEU LYS ALA LYS          
SEQRES   6 A  161  GLY VAL GLN VAL VAL ALA CYS LEU SER VAL ASN ASP ALA          
SEQRES   7 A  161  PHE VAL THR GLY GLU TRP GLY ARG ALA HIS LYS ALA GLU          
SEQRES   8 A  161  GLY LYS VAL ARG LEU LEU ALA ASP PRO THR GLY ALA PHE          
SEQRES   9 A  161  GLY LYS GLU THR ASP LEU LEU LEU ASP ASP SER LEU VAL          
SEQRES  10 A  161  SER ILE PHE GLY ASN ARG ARG LEU LYS ARG PHE SER MET          
SEQRES  11 A  161  VAL VAL GLN ASP GLY ILE VAL LYS ALA LEU ASN VAL GLU          
SEQRES  12 A  161  PRO ASP GLY THR GLY LEU THR CYS SER LEU ALA PRO ASN          
SEQRES  13 A  161  ILE ILE SER GLN LEU                                          
HET    BEZ  A 201       9                                                       
HET     BR  A 301       1                                                       
HET     BR  A 302       1                                                       
HET     BR  A 303       1                                                       
HET     BR  A 304       1                                                       
HET     BR  A 305       1                                                       
HETNAM     BEZ BENZOIC ACID                                                     
HETNAM      BR BROMIDE ION                                                      
FORMUL   2  BEZ    C7 H6 O2                                                     
FORMUL   3   BR    5(BR 1-)                                                     
FORMUL   8  HOH   *221(H2 O)                                                    
HELIX    1  H1 LEU A   25  PHE A   29  1                                   5    
HELIX    2  H2 THR A   44  ALA A   64  1                                  21    
HELIX    3  H3 ASP A   77  HIS A   88  1                                  12    
HELIX    4  H4 GLY A  102  ASP A  109  1                                   8    
HELIX    5  H5 LEU A  116  GLY A  121  1                                   6    
HELIX    6  H6 LEU A  153  LEU A  161  1                                   9    
SHEET    1  S1 1 VAL A  12  GLU A  16  0                                        
SHEET    1  S2 1 ASN A  21  ASN A  24  0                                        
SHEET    1  S5 1 ARG A  95  ASP A  99  0                                        
SHEET    1  S4 1 VAL A  69  SER A  74  0                                        
SHEET    1  S3 1 LYS A  32  VAL A  39  0                                        
SHEET    1  S6 1 ARG A 127  ASP A 134  0                                        
SHEET    1  S7 1 ILE A 136  GLU A 143  0                                        
SITE     1 AC1  3 LYS A  63  LYS A  93  SER A 118                               
SITE     1 AC2  2 GLN A 133  LEU A 149                                          
SITE     1 AC3  2 ALA A  90  GLU A  91                                          
SITE     1 AC4  3 GLN A  68  ASP A 113  SER A 115                               
SITE     1 AC5 11 PRO A  40  THR A  44  PRO A  45  GLY A  46                    
SITE     2 AC5 11 CYS A  47  LYS A  63  ALA A  64  GLY A  66                    
SITE     3 AC5 11 ARG A 127  THR A 147  HOH A2113                               
CRYST1   66.607   66.607  123.327  90.00  90.00  90.00 P 41 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      0.015013  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015013  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008108        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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