GenomeNet

Database: PDB
Entry: 4K7I
LinkDB: 4K7I
Original site: 4K7I 
HEADER    OXIDOREDUCTASE                          17-APR-13   4K7I              
TITLE     HUMAN PEROXIREDOXIN 5 WITH A FRAGMENT                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEROXIREDOXIN-5, MITOCHONDRIAL;                            
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 54-214;                     
COMPND   5 SYNONYM: ALU COREPRESSOR 1, ANTIOXIDANT ENZYME B166, AOEB166, LIVER  
COMPND   6 TISSUE 2D-PAGE SPOT 71B, PLP, PEROXIREDOXIN V, PRX-V, PEROXISOMAL    
COMPND   7 ANTIOXIDANT ENZYME, TPX TYPE VI, THIOREDOXIN PEROXIDASE PMP20,       
COMPND   8 THIOREDOXIN REDUCTASE;                                               
COMPND   9 EC: 1.11.1.15;                                                       
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PRDX5, ACR1, SBBI10;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ENZYME, CYTOSOL, OXIDOREDUCTASE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.F.GUICHOU                                                           
REVDAT   2   30-JUL-14 4K7I    1       JRNL                                     
REVDAT   1   23-APR-14 4K7I    0                                                
JRNL        AUTH   C.AGUIRRE,T.T.BRINK,J.F.GUICHOU,O.CALA,I.KRIMM               
JRNL        TITL   COMPARING BINDING MODES OF ANALOGOUS FRAGMENTS USING NMR IN  
JRNL        TITL 2 FRAGMENT-BASED DRUG DESIGN: APPLICATION TO PRDX5             
JRNL        REF    PLOS ONE                      V.   9 02300 2014              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   25025339                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0102300                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1                                           
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.60                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.100                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 27007                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1442                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE SET COUNT          : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3568                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 382                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.99                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.73000                                              
REMARK   3    B22 (A**2) : 0.16000                                              
REMARK   3    B33 (A**2) : -0.90000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL                          
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : NULL                                          
REMARK   3   ION PROBE RADIUS   : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4K7I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-APR-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB078988.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-OCT-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.977                              
REMARK 200  MONOCHROMATOR                  : YALE MIRRORS                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28855                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.100                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 47.60                    
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 1HD2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG3350, 0.1M SODIUM CITRATE         
REMARK 280  BUFFER, 0.2M POTASSIUM SODIUM TARTRATE, 5MM 1,4-DITHIO-DL-          
REMARK 280  THREITOL, 0.02%(W/V) SODIUM AZIDE, PH 5.3, VAPOR DIFFUSION,         
REMARK 280  HANGING DROP, TEMPERATURE 291K                                      
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       72.46750            
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       72.46750            
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       39.79950            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       51.88100            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       39.79950            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       51.88100            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       72.46750            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       39.79950            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       51.88100            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       72.46750            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       39.79950            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       51.88100            
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, 3, 4, 5                                           
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: MONOMERIC                         
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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       72.46750            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1530 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 A2139  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C 319  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     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     HIS A    -1                                                      
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     HIS B    -1                                                      
REMARK 465     SER B     0                                                      
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     HIS C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 465     ASP C   145                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  2115     O    HOH A  2138              1.97            
REMARK 500   O    HOH B  2087     O    HOH B  2091              2.00            
REMARK 500   O    HOH A  2098     O    HOH A  2134              2.02            
REMARK 500   O    HOH A  2105     O    HOH C   205              2.03            
REMARK 500   O    HOH B  2084     O    HOH B  2112              2.08            
REMARK 500   NE2  GLN C    68     O    HOH C   304              2.17            
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      -59.52   -126.57                                   
REMARK 500    LYS A  93      -50.32   -131.48                                   
REMARK 500    ASP A 113     -158.03    -77.63                                   
REMARK 500    THR A 150     -100.09   -134.18                                   
REMARK 500    PHE B  43       11.58     59.47                                   
REMARK 500    THR B  50      -58.27   -126.36                                   
REMARK 500    ASP B 113     -153.40    -75.45                                   
REMARK 500    ASN B 122     -179.70   -171.80                                   
REMARK 500    THR B 150     -100.01   -134.92                                   
REMARK 500    SER C  48      -45.68    -28.33                                   
REMARK 500    HIS C  51     -162.48   -105.17                                   
REMARK 500    ASP C 113     -161.84    -75.57                                   
REMARK 500    THR C 147      -42.85     52.77                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR C 147        23.1      L          L   OUTSIDE RANGE           
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 A2110        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH A2131        DISTANCE =  6.24 ANGSTROMS                       
REMARK 525    HOH A2136        DISTANCE =  6.83 ANGSTROMS                       
REMARK 525    HOH B2100        DISTANCE =  6.60 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAQ A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAQ B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 202                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4K7N   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4K7O   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4MMM   RELATED DB: PDB                                   
DBREF  4K7I A    1   161  UNP    P30044   PRDX5_HUMAN     54    214             
DBREF  4K7I B    1   161  UNP    P30044   PRDX5_HUMAN     54    214             
DBREF  4K7I C    1   161  UNP    P30044   PRDX5_HUMAN     54    214             
SEQADV 4K7I HIS A   -6  UNP  P30044              EXPRESSION TAG                 
SEQADV 4K7I HIS A   -5  UNP  P30044              EXPRESSION TAG                 
SEQADV 4K7I HIS A   -4  UNP  P30044              EXPRESSION TAG                 
SEQADV 4K7I HIS A   -3  UNP  P30044              EXPRESSION TAG                 
SEQADV 4K7I HIS A   -2  UNP  P30044              EXPRESSION TAG                 
SEQADV 4K7I HIS A   -1  UNP  P30044              EXPRESSION TAG                 
SEQADV 4K7I SER A    0  UNP  P30044              EXPRESSION TAG                 
SEQADV 4K7I HIS B   -6  UNP  P30044              EXPRESSION TAG                 
SEQADV 4K7I HIS B   -5  UNP  P30044              EXPRESSION TAG                 
SEQADV 4K7I HIS B   -4  UNP  P30044              EXPRESSION TAG                 
SEQADV 4K7I HIS B   -3  UNP  P30044              EXPRESSION TAG                 
SEQADV 4K7I HIS B   -2  UNP  P30044              EXPRESSION TAG                 
SEQADV 4K7I HIS B   -1  UNP  P30044              EXPRESSION TAG                 
SEQADV 4K7I SER B    0  UNP  P30044              EXPRESSION TAG                 
SEQADV 4K7I HIS C   -6  UNP  P30044              EXPRESSION TAG                 
SEQADV 4K7I HIS C   -5  UNP  P30044              EXPRESSION TAG                 
SEQADV 4K7I HIS C   -4  UNP  P30044              EXPRESSION TAG                 
SEQADV 4K7I HIS C   -3  UNP  P30044              EXPRESSION TAG                 
SEQADV 4K7I HIS C   -2  UNP  P30044              EXPRESSION TAG                 
SEQADV 4K7I HIS C   -1  UNP  P30044              EXPRESSION TAG                 
SEQADV 4K7I SER C    0  UNP  P30044              EXPRESSION TAG                 
SEQRES   1 A  168  HIS HIS HIS HIS HIS HIS SER ALA PRO ILE LYS VAL GLY          
SEQRES   2 A  168  ASP ALA ILE PRO ALA VAL GLU VAL PHE GLU GLY GLU PRO          
SEQRES   3 A  168  GLY ASN LYS VAL ASN LEU ALA GLU LEU PHE LYS GLY LYS          
SEQRES   4 A  168  LYS GLY VAL LEU PHE GLY VAL PRO GLY ALA PHE THR PRO          
SEQRES   5 A  168  GLY CYS SER LYS THR HIS LEU PRO GLY PHE VAL GLU GLN          
SEQRES   6 A  168  ALA GLU ALA LEU LYS ALA LYS GLY VAL GLN VAL VAL ALA          
SEQRES   7 A  168  CYS LEU SER VAL ASN ASP ALA PHE VAL THR GLY GLU TRP          
SEQRES   8 A  168  GLY ARG ALA HIS LYS ALA GLU GLY LYS VAL ARG LEU LEU          
SEQRES   9 A  168  ALA ASP PRO THR GLY ALA PHE GLY LYS GLU THR ASP LEU          
SEQRES  10 A  168  LEU LEU ASP ASP SER LEU VAL SER ILE PHE GLY ASN ARG          
SEQRES  11 A  168  ARG LEU LYS ARG PHE SER MET VAL VAL GLN ASP GLY ILE          
SEQRES  12 A  168  VAL LYS ALA LEU ASN VAL GLU PRO ASP GLY THR GLY LEU          
SEQRES  13 A  168  THR CYS SER LEU ALA PRO ASN ILE ILE SER GLN LEU              
SEQRES   1 B  168  HIS HIS HIS HIS HIS HIS SER ALA PRO ILE LYS VAL GLY          
SEQRES   2 B  168  ASP ALA ILE PRO ALA VAL GLU VAL PHE GLU GLY GLU PRO          
SEQRES   3 B  168  GLY ASN LYS VAL ASN LEU ALA GLU LEU PHE LYS GLY LYS          
SEQRES   4 B  168  LYS GLY VAL LEU PHE GLY VAL PRO GLY ALA PHE THR PRO          
SEQRES   5 B  168  GLY CYS SER LYS THR HIS LEU PRO GLY PHE VAL GLU GLN          
SEQRES   6 B  168  ALA GLU ALA LEU LYS ALA LYS GLY VAL GLN VAL VAL ALA          
SEQRES   7 B  168  CYS LEU SER VAL ASN ASP ALA PHE VAL THR GLY GLU TRP          
SEQRES   8 B  168  GLY ARG ALA HIS LYS ALA GLU GLY LYS VAL ARG LEU LEU          
SEQRES   9 B  168  ALA ASP PRO THR GLY ALA PHE GLY LYS GLU THR ASP LEU          
SEQRES  10 B  168  LEU LEU ASP ASP SER LEU VAL SER ILE PHE GLY ASN ARG          
SEQRES  11 B  168  ARG LEU LYS ARG PHE SER MET VAL VAL GLN ASP GLY ILE          
SEQRES  12 B  168  VAL LYS ALA LEU ASN VAL GLU PRO ASP GLY THR GLY LEU          
SEQRES  13 B  168  THR CYS SER LEU ALA PRO ASN ILE ILE SER GLN LEU              
SEQRES   1 C  168  HIS HIS HIS HIS HIS HIS SER ALA PRO ILE LYS VAL GLY          
SEQRES   2 C  168  ASP ALA ILE PRO ALA VAL GLU VAL PHE GLU GLY GLU PRO          
SEQRES   3 C  168  GLY ASN LYS VAL ASN LEU ALA GLU LEU PHE LYS GLY LYS          
SEQRES   4 C  168  LYS GLY VAL LEU PHE GLY VAL PRO GLY ALA PHE THR PRO          
SEQRES   5 C  168  GLY CYS SER LYS THR HIS LEU PRO GLY PHE VAL GLU GLN          
SEQRES   6 C  168  ALA GLU ALA LEU LYS ALA LYS GLY VAL GLN VAL VAL ALA          
SEQRES   7 C  168  CYS LEU SER VAL ASN ASP ALA PHE VAL THR GLY GLU TRP          
SEQRES   8 C  168  GLY ARG ALA HIS LYS ALA GLU GLY LYS VAL ARG LEU LEU          
SEQRES   9 C  168  ALA ASP PRO THR GLY ALA PHE GLY LYS GLU THR ASP LEU          
SEQRES  10 C  168  LEU LEU ASP ASP SER LEU VAL SER ILE PHE GLY ASN ARG          
SEQRES  11 C  168  ARG LEU LYS ARG PHE SER MET VAL VAL GLN ASP GLY ILE          
SEQRES  12 C  168  VAL LYS ALA LEU ASN VAL GLU PRO ASP GLY THR GLY LEU          
SEQRES  13 C  168  THR CYS SER LEU ALA PRO ASN ILE ILE SER GLN LEU              
HET    CAQ  A 201       8                                                       
HET    DMS  A 202       4                                                       
HET    CAQ  B 201       8                                                       
HET    DMS  B 202       4                                                       
HETNAM     CAQ CATECHOL                                                         
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETSYN     CAQ 1,2-DIHYDROXYBENZENE                                             
FORMUL   4  CAQ    2(C6 H6 O2)                                                  
FORMUL   5  DMS    2(C2 H6 O S)                                                 
FORMUL   8  HOH   *382(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  LEU A  161  1                                   9    
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 LEU B  116  GLY B  121  1                                   6    
HELIX   17  17 LEU B  153  GLN B  160  1                                   8    
HELIX   18  18 LEU C   25  PHE C   29  1                                   5    
HELIX   19  19 CYS C   47  THR C   50  5                                   4    
HELIX   20  20 HIS C   51  GLN C   58  1                                   8    
HELIX   21  21 GLN C   58  ALA C   64  1                                   7    
HELIX   22  22 ASP C   77  HIS C   88  1                                  12    
HELIX   23  23 GLY C  102  ASP C  109  1                                   8    
HELIX   24  24 LEU C  116  GLY C  121  1                                   6    
HELIX   25  25 ILE C  157  LEU C  161  5                                   5    
SHEET    1   A 2 GLU A  13  PHE A  15  0                                        
SHEET    2   A 2 LYS A  22  ASN A  24 -1  O  VAL A  23   N  VAL A  14           
SHEET    1   B 5 ARG A  95  ALA A  98  0                                        
SHEET    2   B 5 VAL A  67  SER A  74  1  N  CYS A  72   O  LEU A  97           
SHEET    3   B 5 LYS A  33  GLY A  38  1  N  VAL A  35   O  VAL A  69           
SHEET    4   B 5 PHE A 128  GLN A 133 -1  O  VAL A 132   N  GLY A  34           
SHEET    5   B 5 ILE A 136  VAL A 142 -1  O  ASN A 141   N  SER A 129           
SHEET    1   C 2 GLU B  13  PHE B  15  0                                        
SHEET    2   C 2 LYS B  22  ASN B  24 -1  O  VAL B  23   N  VAL B  14           
SHEET    1   D 5 ARG B  95  ALA B  98  0                                        
SHEET    2   D 5 VAL B  69  SER B  74  1  N  CYS B  72   O  LEU B  97           
SHEET    3   D 5 LYS B  33  GLY B  38  1  N  VAL B  35   O  VAL B  69           
SHEET    4   D 5 PHE B 128  GLN B 133 -1  O  VAL B 132   N  GLY B  34           
SHEET    5   D 5 ILE B 136  VAL B 142 -1  O  LYS B 138   N  VAL B 131           
SHEET    1   E 7 LYS C  22  ASN C  24  0                                        
SHEET    2   E 7 GLU C  13  GLU C  16 -1  N  VAL C  14   O  VAL C  23           
SHEET    3   E 7 ARG C  95  ALA C  98 -1  O  ALA C  98   N  PHE C  15           
SHEET    4   E 7 VAL C  69  SER C  74  1  N  CYS C  72   O  ARG C  95           
SHEET    5   E 7 LYS C  33  GLY C  38  1  N  PHE C  37   O  LEU C  73           
SHEET    6   E 7 PHE C 128  GLN C 133 -1  O  VAL C 132   N  GLY C  34           
SHEET    7   E 7 ILE C 136  VAL C 142 -1  O  ASN C 141   N  SER C 129           
SSBOND   1 CYS C   47    CYS C  151                          1555   1555  2.04  
SITE     1 AC1  8 PRO A  40  THR A  44  PRO A  45  GLY A  46                    
SITE     2 AC1  8 CYS A  47  ARG A 127  HOH A2106  ALA C  64                    
SITE     1 AC2  5 PHE A  43  SER A  48  GLU A  83  TRP A  84                    
SITE     2 AC2  5 HIS A  88                                                     
SITE     1 AC3  7 ALA A  64  PRO B  40  THR B  44  PRO B  45                    
SITE     2 AC3  7 GLY B  46  CYS B  47  ARG B 127                               
SITE     1 AC4  4 VAL B  70  GLY B  92  LYS B  93  ARG B  95                    
CRYST1   79.599  103.762  144.935  90.00  90.00  90.00 C 2 2 21     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      0.012563  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009637  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006900        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system