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Database: PDB
Entry: 2VL9
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Original site: 2VL9 
HEADER    OXIDOREDUCTASE                          11-JAN-08   2VL9              
TITLE     OXIDIZED FORM OF HUMAN PEROXIREDOXIN 5                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEROXIREDOXIN-5;                                           
COMPND   3 CHAIN: A, B, C, D;                                                   
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 MUTATION: 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                                    
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   3   24-OCT-18 2VL9    1       SOURCE                                   
REVDAT   2   24-FEB-09 2VL9    1       VERSN                                    
REVDAT   1   26-AUG-08 2VL9    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.    2.70 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 : TWIN_LSQ_F                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 18076                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 923                             
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              : 170.4                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.500           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 79.53                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -6.42570                                             
REMARK   3    B22 (A**2) : -6.42570                                             
REMARK   3    B33 (A**2) : 12.66030                                             
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: 0.4790                                                   
REMARK   3   OPERATOR: -K,H+K,L                                                 
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           4836                                  
REMARK   3   ANGLE     :  1.636           6539                                  
REMARK   3   CHIRALITY :  0.104            760                                  
REMARK   3   PLANARITY :  0.007            853                                  
REMARK   3   DIHEDRAL  : 19.569           1766                                  
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: TWIN RATIO IS 50%. COMPUTED STRUCTURE     
REMARK   3  FACTORS ARE NOT DIRECTLY COMPARABLE TO THE DEPOSITED OBSERVED       
REMARK   3  STRUCTURE FACTORS.                                                  
REMARK   4                                                                      
REMARK   4 2VL9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-JAN-08.                  
REMARK 100 THE DEPOSITION ID IS D_1290034956.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-NOV-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM30A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979764                           
REMARK 200  MONOCHROMATOR                  : FIRST CRYSTAL FLAT AND N2          
REMARK 200                                   COOLED. SECOND ONE SAGITALLY BENT  
REMARK 200  OPTICS                         : TWO MIRRORS ARE USED FOR           
REMARK 200                                   VERTICAL 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   : 18076                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 4.050                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.05                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1OC3                                       
REMARK 200                                                                      
REMARK 200 REMARK: THE MODEL USED FOR THE MOLECULAR REPLACEMENT WAS A           
REMARK 200  SIMULATION CREATED FROM PDB ENTRY 1OC3                              
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000 20% SODIUM CACODYLATE 0.1 M     
REMARK 280  PH 6.5 SODIUM ACETATE 0.1 M 6-AMINOCAPROIC ACID 3% W/V              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       64.41800            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      128.83600            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      128.83600            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       64.41800            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 4570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 34250 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.6 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 73 TO SER                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, CYS 73 TO SER                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, CYS 73 TO SER                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, CYS 73 TO SER                         
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   -11                                                      
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     SER A     0                                                      
REMARK 465     MET B   -11                                                      
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     MET C   -11                                                      
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 465     MET D   -11                                                      
REMARK 465     ARG D   -10                                                      
REMARK 465     GLY D    -9                                                      
REMARK 465     SER D    -8                                                      
REMARK 465     HIS D    -7                                                      
REMARK 465     HIS D    -6                                                      
REMARK 465     HIS D    -5                                                      
REMARK 465     HIS D    -4                                                      
REMARK 465     HIS D    -3                                                      
REMARK 465     HIS D    -2                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     SER D     0                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PRO B  45   N     PRO B  45   CA     -0.117                       
REMARK 500    GLY B  46   CA    GLY B  46   C      -0.216                       
REMARK 500    GLY B  46   C     GLY B  46   O       0.175                       
REMARK 500    ALA D 154   C     ALA D 154   O       0.127                       
REMARK 500    ALA D 154   C     PRO D 155   N      -0.133                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    PRO B  45   CB  -  CA  -  C   ANGL. DEV. = -22.3 DEGREES          
REMARK 500    PRO B  45   N   -  CA  -  C   ANGL. DEV. =  31.2 DEGREES          
REMARK 500    GLY B  46   N   -  CA  -  C   ANGL. DEV. =  29.7 DEGREES          
REMARK 500    GLY B  46   CA  -  C   -  O   ANGL. DEV. =  16.6 DEGREES          
REMARK 500    CYS B  47   N   -  CA  -  CB  ANGL. DEV. = -18.3 DEGREES          
REMARK 500    CYS B  47   N   -  CA  -  C   ANGL. DEV. =  33.4 DEGREES          
REMARK 500    SER C  48   CB  -  CA  -  C   ANGL. DEV. = -18.1 DEGREES          
REMARK 500    SER C  48   N   -  CA  -  C   ANGL. DEV. =  30.1 DEGREES          
REMARK 500    PRO D   2   C   -  N   -  CA  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    PHE D  15   CB  -  CA  -  C   ANGL. DEV. = -15.1 DEGREES          
REMARK 500    LYS D  89   N   -  CA  -  C   ANGL. DEV. =  16.6 DEGREES          
REMARK 500    PRO D 155   C   -  N   -  CD  ANGL. DEV. = -16.1 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    LYS A   4     -158.10   -128.40                                   
REMARK 500    ILE A   9      137.76    -39.57                                   
REMARK 500    VAL A  14     -156.71   -110.52                                   
REMARK 500    LYS A  32      123.34   -171.08                                   
REMARK 500    LYS A  49       -6.41    -54.45                                   
REMARK 500    HIS A  51     -160.72   -109.47                                   
REMARK 500    GLU A  57      -19.73    -48.59                                   
REMARK 500    LYS A  65       29.41   -140.67                                   
REMARK 500    GLN A  68      -71.50    -76.52                                   
REMARK 500    ALA A  90       34.26    -92.23                                   
REMARK 500    GLU A 107       22.71    -76.87                                   
REMARK 500    ASP A 109       11.26     57.58                                   
REMARK 500    ASP A 114       11.16    -67.05                                   
REMARK 500    SER A 118        0.70    -59.45                                   
REMARK 500    PHE A 128     -167.68   -175.64                                   
REMARK 500    ASP A 134       -3.04     63.03                                   
REMARK 500    LEU A 140       65.77   -157.24                                   
REMARK 500    ASN A 141       82.94    -67.93                                   
REMARK 500    LEU A 149       52.41     38.14                                   
REMARK 500    ALA A 154      176.95    179.72                                   
REMARK 500    SER A 159        2.26    -69.78                                   
REMARK 500    GLN A 160      126.88   -172.74                                   
REMARK 500    PRO B   2      154.39    -44.13                                   
REMARK 500    PHE B  29        1.60   -150.05                                   
REMARK 500    LYS B  65       15.11    -67.00                                   
REMARK 500    VAL B  67      141.19    -37.12                                   
REMARK 500    LYS B  89       76.70     55.78                                   
REMARK 500    ALA B  90       66.26   -119.71                                   
REMARK 500    PRO B 100       28.51    -78.27                                   
REMARK 500    THR B 101       16.60   -144.34                                   
REMARK 500    GLU B 107       13.74    -65.43                                   
REMARK 500    ASP B 109       -1.61     65.91                                   
REMARK 500    ASP B 113      154.80    -44.79                                   
REMARK 500    ASP B 114       28.32    -75.45                                   
REMARK 500    ARG B 124      157.30    -49.26                                   
REMARK 500    PHE B 128     -153.18   -111.34                                   
REMARK 500    SER B 129      147.37   -177.72                                   
REMARK 500    MET B 130      119.77   -162.25                                   
REMARK 500    ASP B 134       12.34     53.77                                   
REMARK 500    VAL B 137      152.51    -46.95                                   
REMARK 500    LYS B 138      -46.53   -136.04                                   
REMARK 500    LEU B 149       34.98     36.09                                   
REMARK 500    PRO C   2     -168.51    -76.63                                   
REMARK 500    ASP C   7      114.07   -166.84                                   
REMARK 500    ALA C   8      108.60    -56.50                                   
REMARK 500    ILE C   9      126.67    -38.02                                   
REMARK 500    VAL C  14     -155.18   -139.36                                   
REMARK 500    GLU C  16       43.18   -151.06                                   
REMARK 500    GLU C  27       -7.34    -55.54                                   
REMARK 500    LEU C  28      -78.16    -93.67                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      91 RAMACHANDRAN OUTLIERS.                        
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 B2002        DISTANCE =  8.71 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1URM   RELATED DB: PDB                                   
REMARK 900 HUMAN PEROXIREDOXIN 5, C47S MUTANT                                   
REMARK 900 RELATED ID: 1HD2   RELATED DB: PDB                                   
REMARK 900 HUMAN PEROXIREDOXIN 5                                                
REMARK 900 RELATED ID: 1OC3   RELATED DB: PDB                                   
REMARK 900 HUMAN PEROXIREDOXIN 5                                                
REMARK 900 RELATED ID: 2VL3   RELATED DB: PDB                                   
REMARK 900 OXIDIZED AND REDUCED FORMS OF HUMAN PEROXIREDOXIN 5                  
REMARK 900 RELATED ID: 2VL2   RELATED DB: PDB                                   
REMARK 900 OXIDIZED AND REDUCED FORMS OF HUMAN PEROXIREDOXIN 5                  
REMARK 900 RELATED ID: 1H4O   RELATED DB: PDB                                   
REMARK 900 MONOCLINIC FORM OF HUMAN PEROXIREDOXIN 5                             
DBREF  2VL9 A  -11     0  PDB    2VL9     2VL9           -11      0             
DBREF  2VL9 A    1   161  UNP    P30044   PRDX5_HUMAN      2    162             
DBREF  2VL9 B  -11     0  PDB    2VL9     2VL9           -11      0             
DBREF  2VL9 B    1   161  UNP    P30044   PRDX5_HUMAN      2    162             
DBREF  2VL9 C  -11     0  PDB    2VL9     2VL9           -11      0             
DBREF  2VL9 C    1   161  UNP    P30044   PRDX5_HUMAN      2    162             
DBREF  2VL9 D  -11     0  PDB    2VL9     2VL9           -11      0             
DBREF  2VL9 D    1   161  UNP    P30044   PRDX5_HUMAN      2    162             
SEQADV 2VL9 SER A   72  UNP  P30044    CYS    73 ENGINEERED MUTATION            
SEQADV 2VL9 SER B   72  UNP  P30044    CYS    73 ENGINEERED MUTATION            
SEQADV 2VL9 SER C   72  UNP  P30044    CYS    73 ENGINEERED MUTATION            
SEQADV 2VL9 SER D   72  UNP  P30044    CYS    73 ENGINEERED MUTATION            
SEQRES   1 A  173  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA          
SEQRES   2 A  173  PRO ILE LYS VAL GLY ASP ALA ILE PRO ALA VAL GLU VAL          
SEQRES   3 A  173  PHE GLU GLY GLU PRO GLY ASN LYS VAL ASN LEU ALA GLU          
SEQRES   4 A  173  LEU PHE LYS GLY LYS LYS GLY VAL LEU PHE GLY VAL PRO          
SEQRES   5 A  173  GLY ALA PHE THR PRO GLY CYS SER LYS THR HIS LEU PRO          
SEQRES   6 A  173  GLY PHE VAL GLU GLN ALA GLU ALA LEU LYS ALA LYS GLY          
SEQRES   7 A  173  VAL GLN VAL VAL ALA SER LEU SER VAL ASN ASP ALA PHE          
SEQRES   8 A  173  VAL THR GLY GLU TRP GLY ARG ALA HIS LYS ALA GLU GLY          
SEQRES   9 A  173  LYS VAL ARG LEU LEU ALA ASP PRO THR GLY ALA PHE GLY          
SEQRES  10 A  173  LYS GLU THR ASP LEU LEU LEU ASP ASP SER LEU VAL SER          
SEQRES  11 A  173  ILE PHE GLY ASN ARG ARG LEU LYS ARG PHE SER MET VAL          
SEQRES  12 A  173  VAL GLN ASP GLY ILE VAL LYS ALA LEU ASN VAL GLU PRO          
SEQRES  13 A  173  ASP GLY THR GLY LEU THR CYS SER LEU ALA PRO ASN ILE          
SEQRES  14 A  173  ILE SER GLN LEU                                              
SEQRES   1 B  173  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA          
SEQRES   2 B  173  PRO ILE LYS VAL GLY ASP ALA ILE PRO ALA VAL GLU VAL          
SEQRES   3 B  173  PHE GLU GLY GLU PRO GLY ASN LYS VAL ASN LEU ALA GLU          
SEQRES   4 B  173  LEU PHE LYS GLY LYS LYS GLY VAL LEU PHE GLY VAL PRO          
SEQRES   5 B  173  GLY ALA PHE THR PRO GLY CYS SER LYS THR HIS LEU PRO          
SEQRES   6 B  173  GLY PHE VAL GLU GLN ALA GLU ALA LEU LYS ALA LYS GLY          
SEQRES   7 B  173  VAL GLN VAL VAL ALA SER LEU SER VAL ASN ASP ALA PHE          
SEQRES   8 B  173  VAL THR GLY GLU TRP GLY ARG ALA HIS LYS ALA GLU GLY          
SEQRES   9 B  173  LYS VAL ARG LEU LEU ALA ASP PRO THR GLY ALA PHE GLY          
SEQRES  10 B  173  LYS GLU THR ASP LEU LEU LEU ASP ASP SER LEU VAL SER          
SEQRES  11 B  173  ILE PHE GLY ASN ARG ARG LEU LYS ARG PHE SER MET VAL          
SEQRES  12 B  173  VAL GLN ASP GLY ILE VAL LYS ALA LEU ASN VAL GLU PRO          
SEQRES  13 B  173  ASP GLY THR GLY LEU THR CYS SER LEU ALA PRO ASN ILE          
SEQRES  14 B  173  ILE SER GLN LEU                                              
SEQRES   1 C  173  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA          
SEQRES   2 C  173  PRO ILE LYS VAL GLY ASP ALA ILE PRO ALA VAL GLU VAL          
SEQRES   3 C  173  PHE GLU GLY GLU PRO GLY ASN LYS VAL ASN LEU ALA GLU          
SEQRES   4 C  173  LEU PHE LYS GLY LYS LYS GLY VAL LEU PHE GLY VAL PRO          
SEQRES   5 C  173  GLY ALA PHE THR PRO GLY CYS SER LYS THR HIS LEU PRO          
SEQRES   6 C  173  GLY PHE VAL GLU GLN ALA GLU ALA LEU LYS ALA LYS GLY          
SEQRES   7 C  173  VAL GLN VAL VAL ALA SER LEU SER VAL ASN ASP ALA PHE          
SEQRES   8 C  173  VAL THR GLY GLU TRP GLY ARG ALA HIS LYS ALA GLU GLY          
SEQRES   9 C  173  LYS VAL ARG LEU LEU ALA ASP PRO THR GLY ALA PHE GLY          
SEQRES  10 C  173  LYS GLU THR ASP LEU LEU LEU ASP ASP SER LEU VAL SER          
SEQRES  11 C  173  ILE PHE GLY ASN ARG ARG LEU LYS ARG PHE SER MET VAL          
SEQRES  12 C  173  VAL GLN ASP GLY ILE VAL LYS ALA LEU ASN VAL GLU PRO          
SEQRES  13 C  173  ASP GLY THR GLY LEU THR CYS SER LEU ALA PRO ASN ILE          
SEQRES  14 C  173  ILE SER GLN LEU                                              
SEQRES   1 D  173  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA          
SEQRES   2 D  173  PRO ILE LYS VAL GLY ASP ALA ILE PRO ALA VAL GLU VAL          
SEQRES   3 D  173  PHE GLU GLY GLU PRO GLY ASN LYS VAL ASN LEU ALA GLU          
SEQRES   4 D  173  LEU PHE LYS GLY LYS LYS GLY VAL LEU PHE GLY VAL PRO          
SEQRES   5 D  173  GLY ALA PHE THR PRO GLY CYS SER LYS THR HIS LEU PRO          
SEQRES   6 D  173  GLY PHE VAL GLU GLN ALA GLU ALA LEU LYS ALA LYS GLY          
SEQRES   7 D  173  VAL GLN VAL VAL ALA SER LEU SER VAL ASN ASP ALA PHE          
SEQRES   8 D  173  VAL THR GLY GLU TRP GLY ARG ALA HIS LYS ALA GLU GLY          
SEQRES   9 D  173  LYS VAL ARG LEU LEU ALA ASP PRO THR GLY ALA PHE GLY          
SEQRES  10 D  173  LYS GLU THR ASP LEU LEU LEU ASP ASP SER LEU VAL SER          
SEQRES  11 D  173  ILE PHE GLY ASN ARG ARG LEU LYS ARG PHE SER MET VAL          
SEQRES  12 D  173  VAL GLN ASP GLY ILE VAL LYS ALA LEU ASN VAL GLU PRO          
SEQRES  13 D  173  ASP GLY THR GLY LEU THR CYS SER LEU ALA PRO ASN ILE          
SEQRES  14 D  173  ILE SER GLN LEU                                              
FORMUL   5  HOH   *57(H2 O)                                                     
HELIX    1   1 GLU A   18  LYS A   22  5                                   5    
HELIX    2   2 LEU A   25  LYS A   30  1                                   6    
HELIX    3   3 CYS A   47  HIS A   51  5                                   5    
HELIX    4   4 GLY A   82  HIS A   88  1                                   7    
HELIX    5   5 GLY A  102  GLU A  107  1                                   6    
HELIX    6   6 LEU A  116  GLY A  121  1                                   6    
HELIX    7   7 ASN A  156  GLN A  160  5                                   5    
HELIX    8   8 CYS B   47  HIS B   51  5                                   5    
HELIX    9   9 LEU B   52  VAL B   56  5                                   5    
HELIX   10  10 GLN B   58  LYS B   63  1                                   6    
HELIX   11  11 ASP B   77  HIS B   88  1                                  12    
HELIX   12  12 GLY B  102  GLU B  107  1                                   6    
HELIX   13  13 LEU B  116  GLY B  121  1                                   6    
HELIX   14  14 ASN B  156  GLN B  160  5                                   5    
HELIX   15  15 LEU C   25  LYS C   30  1                                   6    
HELIX   16  16 LEU C   52  GLU C   57  1                                   6    
HELIX   17  17 GLN C   58  LYS C   63  1                                   6    
HELIX   18  18 ASP C   77  HIS C   88  1                                  12    
HELIX   19  19 GLY C  102  ASP C  109  1                                   8    
HELIX   20  20 SER C  115  PHE C  120  5                                   6    
HELIX   21  21 ASN C  156  GLN C  160  5                                   5    
HELIX   22  22 LEU D   25  LYS D   30  1                                   6    
HELIX   23  23 LEU D   52  GLU D   57  1                                   6    
HELIX   24  24 GLU D   57  LYS D   63  1                                   7    
HELIX   25  25 ALA D   64  GLY D   66  5                                   3    
HELIX   26  26 ASP D   77  GLY D   82  1                                   6    
HELIX   27  27 GLY D   82  ALA D   87  1                                   6    
HELIX   28  28 GLY D  102  GLU D  107  1                                   6    
HELIX   29  29 LEU D  116  GLY D  121  1                                   6    
SHEET    1  AA 2 GLU A  13  VAL A  14  0                                        
SHEET    2  AA 2 VAL A  23  ASN A  24 -1  O  VAL A  23   N  VAL A  14           
SHEET    1  AB 2 ALA A  71  SER A  72  0                                        
SHEET    2  AB 2 ARG A  95  LEU A  96  1  O  ARG A  95   N  SER A  72           
SHEET    1  AC 2 VAL A 132  GLN A 133  0                                        
SHEET    2  AC 2 ILE A 136  VAL A 137 -1  O  ILE A 136   N  GLN A 133           
SHEET    1  BA 2 GLU B  13  VAL B  14  0                                        
SHEET    2  BA 2 VAL B  23  ASN B  24 -1  O  VAL B  23   N  VAL B  14           
SHEET    1  BB 4 VAL B  69  LEU B  73  0                                        
SHEET    2  BB 4 GLY B  34  GLY B  38  1  O  VAL B  35   N  ALA B  71           
SHEET    3  BB 4 PHE B 128  GLN B 133 -1  O  PHE B 128   N  GLY B  38           
SHEET    4  BB 4 ILE B 136  LEU B 140 -1  O  ILE B 136   N  GLN B 133           
SHEET    1  CA 2 GLU C  13  VAL C  14  0                                        
SHEET    2  CA 2 VAL C  23  ASN C  24 -1  O  VAL C  23   N  VAL C  14           
SHEET    1  CB 2 GLY C  34  GLY C  38  0                                        
SHEET    2  CB 2 VAL C  69  LEU C  73  1  O  VAL C  69   N  VAL C  35           
SHEET    1  CC 2 PHE C 128  SER C 129  0                                        
SHEET    2  CC 2 ASN C 141  VAL C 142 -1  O  ASN C 141   N  SER C 129           
SHEET    1  DA 3 VAL D  23  ASN D  24  0                                        
SHEET    2  DA 3 GLU D  13  GLU D  16 -1  O  VAL D  14   N  VAL D  23           
SHEET    3  DA 3 LEU D  97  ALA D  98 -1  O  ALA D  98   N  PHE D  15           
SHEET    1  DB 2 GLY D  34  GLY D  38  0                                        
SHEET    2  DB 2 VAL D  69  LEU D  73  1  O  VAL D  69   N  VAL D  35           
SHEET    1  DC 2 VAL D 132  GLN D 133  0                                        
SHEET    2  DC 2 ILE D 136  VAL D 137 -1  O  ILE D 136   N  GLN D 133           
SSBOND   1 CYS A   47    CYS A  151                          1555   1555  2.04  
SSBOND   2 CYS B   47    CYS B  151                          1555   1555  2.04  
SSBOND   3 CYS C   47    CYS C  151                          1555   1555  2.04  
SSBOND   4 CYS D   47    CYS D  151                          1555   1555  2.04  
CRYST1   75.870   75.870  193.254  90.00  90.00 120.00 P 31 2 1     24          
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      0.013180  0.007610  0.000000        0.00000                         
SCALE2      0.000000  0.015219  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005175        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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