GenomeNet

Database: PDB
Entry: 2VL2
LinkDB: 2VL2
Original site: 2VL2 
HEADER    OXIDOREDUCTASE                          08-JAN-08   2VL2              
TITLE     OXIDIZED AND REDUCED FORMS OF HUMAN PEROXIREDOXIN 5                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEROXIREDOXIN-5;                                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 2-162;                                            
COMPND   5 SYNONYM: PRX-V, PEROXISOMAL ANTIOXIDANT ENZYME, PLP, THIOREDOXIN     
COMPND   6 REDUCTASE, THIOREDOXIN PEROXIDASE PMP20, ANTIOXIDANT ENZYME B166,    
COMPND   7 AOEB166, TPX TYPE VI, LIVER TISSUE 2D-PAGE SPOT 71B, ALU COREPRESSOR 
COMPND   8 1, HUMAN PEROXIREDOXIN 5;                                            
COMPND   9 EC: 1.11.1.15;                                                       
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: PEROXIREDOXIN-5;                                           
COMPND  13 CHAIN: C;                                                            
COMPND  14 FRAGMENT: RESIDUES 2-162;                                            
COMPND  15 SYNONYM: PRX-V, PEROXISOMAL ANTIOXIDANT ENZYME, PLP, THIOREDOXIN     
COMPND  16 REDUCTASE, THIOREDOXIN PEROXIDASE PMP20, ANTIOXIDANT ENZYME B166,    
COMPND  17 AOEB166, TPX TYPE VI, LIVER TISSUE 2D-PAGE SPOT 71B, ALU COREPRESSOR 
COMPND  18 1, HUMAN PEROXIREDOXIN 5;                                            
COMPND  19 EC: 1.11.1.15;                                                       
COMPND  20 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI M15;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 1007065;                                    
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PQE-30;                                   
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 ORGAN: LUNG;                                                         
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI M15;                             
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 1007065;                                    
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PQE-30                                    
KEYWDS    THIOREDOXIN PEROXIDASE, ALTERNATIVE INITIATION, ANTIOXIDANT ENZYME,   
KEYWDS   2 REDOX-ACTIVE CENTER, CYTOPLASM, PEROXIDASE, PEROXISOME, ANTIOXIDANT, 
KEYWDS   3 POLYMORPHISM, MITOCHONDRION, PEROXIREDOXIN, OXIDOREDUCTASE, TRANSIT  
KEYWDS   4 PEPTIDE, THIOREDOXIN FOLD                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.SMEETS,J.P.DECLERCQ                                                 
REVDAT   5   24-JUL-19 2VL2    1       REMARK                                   
REVDAT   4   10-JUL-19 2VL2    1       REMARK LINK                              
REVDAT   3   24-OCT-18 2VL2    1       SOURCE REMARK                            
REVDAT   2   24-FEB-09 2VL2    1       VERSN                                    
REVDAT   1   26-AUG-08 2VL2    0                                                
JRNL        AUTH   A.SMEETS,C.MARCHAND,D.LINARD,B.KNOOPS,J.P.DECLERCQ           
JRNL        TITL   THE CRYSTAL STRUCTURES OF OXIDIZED FORMS OF HUMAN            
JRNL        TITL 2 PEROXIREDOXIN 5 WITH AN INTRAMOLECULAR DISULFIDE BOND        
JRNL        TITL 3 CONFIRM THE PROPOSED ENZYMATIC MECHANISM FOR ATYPICAL 2-CYS  
JRNL        TITL 4 PEROXIREDOXINS.                                              
JRNL        REF    ARCH.BIOCHEM.BIOPHYS.         V. 477    98 2008              
JRNL        REFN                   ISSN 0003-9861                               
JRNL        PMID   18489898                                                     
JRNL        DOI    10.1016/J.ABB.2008.04.036                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.93 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.93                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 57.50                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 42806                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2157                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.37                                          
REMARK   3   B_SOL              : 51.32                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.970           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.57                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.99                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.37180                                              
REMARK   3    B22 (A**2) : -1.44060                                             
REMARK   3    B33 (A**2) : -4.93120                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           3660                                  
REMARK   3   ANGLE     :  1.018           4949                                  
REMARK   3   CHIRALITY :  0.072            571                                  
REMARK   3   PLANARITY :  0.004            650                                  
REMARK   3   DIHEDRAL  : 17.827           1337                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2VL2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-JAN-08.                  
REMARK 100 THE DEPOSITION ID IS D_1290034901.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-SEP-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
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                       : X11                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8156                             
REMARK 200  MONOCHROMATOR                  : SI 111, HORIZONTALLY FOCUSSING     
REMARK 200  OPTICS                         : MIRROR 2 BENT, VERTICALLY          
REMARK 200                                   FOCUSSING                          
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42806                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.920                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 57.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.6                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.03000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.92                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1HD2                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NACL 0.1M TRIS PH 8 0.1M PEG 3350 20%    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
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   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
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       73.32150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       73.32150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       39.53350            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       51.00800            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       39.53350            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       51.00800            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       73.32150            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       39.53350            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       51.00800            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       73.32150            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       39.53350            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       51.00800            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 1830 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       73.32150            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 970 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 16810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
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 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 A2032  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     ARG A   -10                                                      
REMARK 465     GLY A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     ARG B   -10                                                      
REMARK 465     GLY B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     HIS B    -7                                                      
REMARK 465     HIS B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     ARG C   -10                                                      
REMARK 465     GLY C    -9                                                      
REMARK 465     SER C    -8                                                      
REMARK 465     HIS C    -7                                                      
REMARK 465     HIS C    -6                                                      
REMARK 465     HIS C    -5                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     HIS C    -3                                                      
REMARK 465     HIS C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     SER C     0                                                      
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      -58.32   -133.28                                   
REMARK 500    ASP A 113     -156.81    -86.48                                   
REMARK 500    THR A 150      -99.30   -135.78                                   
REMARK 500    THR B  50      -60.35   -129.92                                   
REMARK 500    ASP B 113     -159.12    -79.38                                   
REMARK 500    ASP B 134       66.91     35.63                                   
REMARK 500    THR B 150      -99.05   -137.09                                   
REMARK 500    CYS C  47       76.26     41.86                                   
REMARK 500    HIS C  51     -168.63   -113.87                                   
REMARK 500    ASP C 113     -164.28    -74.29                                   
REMARK 500    THR C 147      -51.00     68.35                                   
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 A2035        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH C2017        DISTANCE =  6.25 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEZ A1162                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEZ B1162                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1OC3   RELATED DB: PDB                                   
REMARK 900 HUMAN PEROXIREDOXIN 5                                                
REMARK 900 RELATED ID: 1H4O   RELATED DB: PDB                                   
REMARK 900 MONOCLINIC FORM OF HUMAN PEROXIREDOXIN 5                             
REMARK 900 RELATED ID: 1HD2   RELATED DB: PDB                                   
REMARK 900 HUMAN PEROXIREDOXIN 5                                                
REMARK 900 RELATED ID: 1URM   RELATED DB: PDB                                   
REMARK 900 HUMAN PEROXIREDOXIN 5, C47S MUTANT                                   
REMARK 900 RELATED ID: 2VL3   RELATED DB: PDB                                   
REMARK 900 OXIDIZED AND REDUCED FORMS OF HUMAN PEROXIREDOXIN 5                  
DBREF  2VL2 A  -10     0  PDB    2VL2     2VL2           -10      0             
DBREF  2VL2 A    1   161  UNP    P30044   PRDX5_HUMAN      2    162             
DBREF  2VL2 B  -10     0  PDB    2VL2     2VL2           -10      0             
DBREF  2VL2 B    1   161  UNP    P30044   PRDX5_HUMAN      2    162             
DBREF  2VL2 C  -10     0  PDB    2VL2     2VL2           -10      0             
DBREF  2VL2 C    1   161  UNP    P30044   PRDX5_HUMAN      2    162             
SEQRES   1 A  172  ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA PRO          
SEQRES   2 A  172  ILE LYS VAL GLY ASP ALA ILE PRO ALA VAL GLU VAL PHE          
SEQRES   3 A  172  GLU GLY GLU PRO GLY ASN LYS VAL ASN LEU ALA GLU LEU          
SEQRES   4 A  172  PHE LYS GLY LYS LYS GLY VAL LEU PHE GLY VAL PRO GLY          
SEQRES   5 A  172  ALA PHE THR PRO GLY CYS SER LYS THR HIS LEU PRO GLY          
SEQRES   6 A  172  PHE VAL GLU GLN ALA GLU ALA LEU LYS ALA LYS GLY VAL          
SEQRES   7 A  172  GLN VAL VAL ALA CYS LEU SER VAL ASN ASP ALA PHE VAL          
SEQRES   8 A  172  THR GLY GLU TRP GLY ARG ALA HIS LYS ALA GLU GLY LYS          
SEQRES   9 A  172  VAL ARG LEU LEU ALA ASP PRO THR GLY ALA PHE GLY LYS          
SEQRES  10 A  172  GLU THR ASP LEU LEU LEU ASP ASP SER LEU VAL SER ILE          
SEQRES  11 A  172  PHE GLY ASN ARG ARG LEU LYS ARG PHE SER MET VAL VAL          
SEQRES  12 A  172  GLN ASP GLY ILE VAL LYS ALA LEU ASN VAL GLU PRO ASP          
SEQRES  13 A  172  GLY THR GLY LEU THR CSO SER LEU ALA PRO ASN ILE ILE          
SEQRES  14 A  172  SER GLN LEU                                                  
SEQRES   1 B  172  ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA PRO          
SEQRES   2 B  172  ILE LYS VAL GLY ASP ALA ILE PRO ALA VAL GLU VAL PHE          
SEQRES   3 B  172  GLU GLY GLU PRO GLY ASN LYS VAL ASN LEU ALA GLU LEU          
SEQRES   4 B  172  PHE LYS GLY LYS LYS GLY VAL LEU PHE GLY VAL PRO GLY          
SEQRES   5 B  172  ALA PHE THR PRO GLY CYS SER LYS THR HIS LEU PRO GLY          
SEQRES   6 B  172  PHE VAL GLU GLN ALA GLU ALA LEU LYS ALA LYS GLY VAL          
SEQRES   7 B  172  GLN VAL VAL ALA CYS LEU SER VAL ASN ASP ALA PHE VAL          
SEQRES   8 B  172  THR GLY GLU TRP GLY ARG ALA HIS LYS ALA GLU GLY LYS          
SEQRES   9 B  172  VAL ARG LEU LEU ALA ASP PRO THR GLY ALA PHE GLY LYS          
SEQRES  10 B  172  GLU THR ASP LEU LEU LEU ASP ASP SER LEU VAL SER ILE          
SEQRES  11 B  172  PHE GLY ASN ARG ARG LEU LYS ARG PHE SER MET VAL VAL          
SEQRES  12 B  172  GLN ASP GLY ILE VAL LYS ALA LEU ASN VAL GLU PRO ASP          
SEQRES  13 B  172  GLY THR GLY LEU THR CSO SER LEU ALA PRO ASN ILE ILE          
SEQRES  14 B  172  SER GLN LEU                                                  
SEQRES   1 C  172  ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA PRO          
SEQRES   2 C  172  ILE LYS VAL GLY ASP ALA ILE PRO ALA VAL GLU VAL PHE          
SEQRES   3 C  172  GLU GLY GLU PRO GLY ASN LYS VAL ASN LEU ALA GLU LEU          
SEQRES   4 C  172  PHE LYS GLY LYS LYS GLY VAL LEU PHE GLY VAL PRO GLY          
SEQRES   5 C  172  ALA PHE THR PRO GLY CYS SER LYS THR HIS LEU PRO GLY          
SEQRES   6 C  172  PHE VAL GLU GLN ALA GLU ALA LEU LYS ALA LYS GLY VAL          
SEQRES   7 C  172  GLN VAL VAL ALA CYS LEU SER VAL ASN ASP ALA PHE VAL          
SEQRES   8 C  172  THR GLY GLU TRP GLY ARG ALA HIS LYS ALA GLU GLY LYS          
SEQRES   9 C  172  VAL ARG LEU LEU ALA ASP PRO THR GLY ALA PHE GLY LYS          
SEQRES  10 C  172  GLU THR ASP LEU LEU LEU ASP ASP SER LEU VAL SER ILE          
SEQRES  11 C  172  PHE GLY ASN ARG ARG LEU LYS ARG PHE SER MET VAL VAL          
SEQRES  12 C  172  GLN ASP GLY ILE VAL LYS ALA LEU ASN VAL GLU PRO ASP          
SEQRES  13 C  172  GLY THR GLY LEU THR CYS SER LEU ALA PRO ASN ILE ILE          
SEQRES  14 C  172  SER GLN LEU                                                  
MODRES 2VL2 CSO A  151  CYS  S-HYDROXYCYSTEINE                                  
MODRES 2VL2 CSO B  151  CYS  S-HYDROXYCYSTEINE                                  
HET    CSO  A 151       7                                                       
HET    CSO  B 151       7                                                       
HET    BEZ  A1162       9                                                       
HET    BEZ  B1162       9                                                       
HETNAM     CSO S-HYDROXYCYSTEINE                                                
HETNAM     BEZ BENZOIC ACID                                                     
FORMUL   1  CSO    2(C3 H7 N O3 S)                                              
FORMUL   4  BEZ    2(C7 H6 O2)                                                  
FORMUL   6  HOH   *390(H2 O)                                                    
HELIX    1   1 LEU A   25  LYS A   30  1                                   6    
HELIX    2   2 THR A   44  THR A   50  1                                   7    
HELIX    3   3 THR A   50  GLN A   58  1                                   9    
HELIX    4   4 GLN A   58  ALA A   64  1                                   7    
HELIX    5   5 ASP A   77  HIS A   88  1                                  12    
HELIX    6   6 GLY A  102  ASP A  109  1                                   8    
HELIX    7   7 ASP A  113  SER A  115  5                                   3    
HELIX    8   8 LEU A  116  GLY A  121  1                                   6    
HELIX    9   9 LEU A  153  GLN A  160  1                                   8    
HELIX   10  10 LEU B   25  LYS B   30  1                                   6    
HELIX   11  11 THR B   44  THR B   50  1                                   7    
HELIX   12  12 THR B   50  GLN B   58  1                                   9    
HELIX   13  13 GLN B   58  LYS B   65  1                                   8    
HELIX   14  14 ASP B   77  HIS B   88  1                                  12    
HELIX   15  15 GLY B  102  ASP B  109  1                                   8    
HELIX   16  16 ASP B  113  SER B  115  5                                   3    
HELIX   17  17 LEU B  116  GLY B  121  1                                   6    
HELIX   18  18 LEU B  153  SER B  159  1                                   7    
HELIX   19  19 LEU C   25  LYS C   30  1                                   6    
HELIX   20  20 CYS C   47  THR C   50  5                                   4    
HELIX   21  21 HIS C   51  GLN C   58  1                                   8    
HELIX   22  22 GLN C   58  ALA C   64  1                                   7    
HELIX   23  23 ASP C   77  HIS C   88  1                                  12    
HELIX   24  24 GLY C  102  ASP C  109  1                                   8    
HELIX   25  25 LEU C  116  GLY C  121  1                                   6    
HELIX   26  26 ASN C  156  LEU C  161  5                                   6    
SHEET    1  AA 2 GLU A  13  PHE A  15  0                                        
SHEET    2  AA 2 LYS A  22  ASN A  24 -1  O  VAL A  23   N  VAL A  14           
SHEET    1  AB 5 ARG A  95  ALA A  98  0                                        
SHEET    2  AB 5 VAL A  67  SER A  74  1  O  VAL A  70   N  ARG A  95           
SHEET    3  AB 5 LYS A  33  GLY A  38  1  O  LYS A  33   N  GLN A  68           
SHEET    4  AB 5 PHE A 128  GLN A 133 -1  O  PHE A 128   N  GLY A  38           
SHEET    5  AB 5 ILE A 136  VAL A 142 -1  O  ILE A 136   N  GLN A 133           
SHEET    1  BA 2 GLU B  13  PHE B  15  0                                        
SHEET    2  BA 2 LYS B  22  ASN B  24 -1  O  VAL B  23   N  VAL B  14           
SHEET    1  BB 5 ARG B  95  ALA B  98  0                                        
SHEET    2  BB 5 VAL B  69  SER B  74  1  O  VAL B  70   N  ARG B  95           
SHEET    3  BB 5 LYS B  33  VAL B  39  1  O  VAL B  35   N  ALA B  71           
SHEET    4  BB 5 PHE B 128  GLN B 133 -1  O  PHE B 128   N  GLY B  38           
SHEET    5  BB 5 ILE B 136  VAL B 142 -1  O  ILE B 136   N  GLN B 133           
SHEET    1  CA 2 GLU C  13  PHE C  15  0                                        
SHEET    2  CA 2 LYS C  22  ASN C  24 -1  O  VAL C  23   N  VAL C  14           
SHEET    1  CB 5 ARG C  95  ALA C  98  0                                        
SHEET    2  CB 5 VAL C  69  SER C  74  1  O  VAL C  70   N  ARG C  95           
SHEET    3  CB 5 LYS C  33  GLY C  38  1  O  VAL C  35   N  ALA C  71           
SHEET    4  CB 5 PHE C 128  GLN C 133 -1  O  PHE C 128   N  GLY C  38           
SHEET    5  CB 5 ILE C 136  VAL C 142 -1  O  ILE C 136   N  GLN C 133           
SSBOND   1 CYS C   47    CYS C  151                          1555   1555  2.04  
LINK         C   THR A 150                 N   CSO A 151     1555   1555  1.33  
LINK         C   CSO A 151                 N   SER A 152     1555   1555  1.33  
LINK         C   THR B 150                 N   CSO B 151     1555   1555  1.33  
LINK         C   CSO B 151                 N   SER B 152     1555   1555  1.33  
SITE     1 AC1  7 THR A  44  PRO A  45  GLY A  46  CYS A  47                    
SITE     2 AC1  7 THR A 147  HOH A2129  ALA C  64                               
SITE     1 AC2 11 LYS A  63  ALA A  64  GLY A  66  PRO B  40                    
SITE     2 AC2 11 THR B  44  PRO B  45  GLY B  46  LEU B 116                    
SITE     3 AC2 11 PHE B 120  THR B 147  HOH B2125                               
CRYST1   79.067  102.016  146.643  90.00  90.00  90.00 C 2 2 21     16          
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      0.012648  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009802  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006819        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system