GenomeNet

Database: PDB
Entry: 1URM
LinkDB: 1URM
Original site: 1URM 
HEADER    ANTIOXIDANT ENZYME                      31-OCT-03   1URM              
TITLE     HUMAN PEROXIREDOXIN 5, C47S MUTANT                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEROXIREDOXIN 5;                                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 54-214;                                           
COMPND   5 SYNONYM: PRX-V, PEROXISOMAL ANTIOXIDANT ENZYME, PLP, THIOREDOXIN     
COMPND   6 PEROXIDASE PMP20, ANTIOXIDANT ENZYME B166, AOEB166, TPX TYPE VI, ALU 
COMPND   7 CO-REPRESSOR 1;                                                      
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 OTHER_DETAILS: MUTATION CYS 47 SER IN COORDINATES                    
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;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: M15;                                       
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PQE-30                                    
KEYWDS    ANTIOXIDANT ENZYME, PEROXIREDOXIN, THIOREDOXIN PEROXIDASE,            
KEYWDS   2 THIOREDOXIN FOLD                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.P.DECLERCQ,C.EVRARD                                                 
REVDAT   4   24-JUL-19 1URM    1       REMARK                                   
REVDAT   3   13-JUL-11 1URM    1       VERSN                                    
REVDAT   2   24-FEB-09 1URM    1       VERSN                                    
REVDAT   1   29-SEP-04 1URM    0                                                
JRNL        AUTH   C.EVRARD,A.SMEETS,B.KNOOPS,J.P.DECLERCQ                      
JRNL        TITL   CRYSTAL STRUCTURE OF THE C47S MUTANT OF HUMAN PEROXIREDOXIN  
JRNL        TITL 2 5                                                            
JRNL        REF    J. CHEM. CRYST.               V.  34   553 2004              
JRNL        REFN                   ISSN 1074-1542                               
JRNL        DOI    10.1023/B:JOCC.0000042025.08082.6C                           
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.P.DECLERCQ,C.EVRARD,A.CLIPPE,D.VANDERSTRICHT,A.BERNARD,    
REMARK   1  AUTH 2 B.KNOOPS                                                     
REMARK   1  TITL   CRYSTAL STRUCTURE OF HUMAN PEROXIREDOXIN 5, A NOVEL TYPE OF  
REMARK   1  TITL 2 MAMMALIAN PEROXIREDOXIN AT 1.5 A RESOLUTION                  
REMARK   1  REF    J.MOL.BIOL.                   V. 311   751 2001              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   11518528                                                     
REMARK   1  DOI    10.1006/JMBI.2001.4853                                       
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   J.P.DECLERCQ,C.EVRARD                                        
REMARK   1  TITL   A TWINNED MONOCLINIC CRYSTAL FORM OF HUMAN PEROXIREDOXIN 5   
REMARK   1  TITL 2 WITH EIGHT MOLECULES IN THE ASYMMETRIC UNIT                  
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  57  1829 2001              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  PMID   11717495                                                     
REMARK   1  DOI    10.1107/S0907444901015475                                    
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   B.KNOOPS,A.CLIPPE,C.BOGARD,K.ARSALANE,R.WATTIEZ,C.HERMANS,   
REMARK   1  AUTH 2 E.DUCONSEILLE,P.FALMAGNE,A.BERNARD                           
REMARK   1  TITL   CLONING AND CHARACTERIZATION OF AOEB166, A NOVEL MAMMALIAN   
REMARK   1  TITL 2 ANTIOXIDANT ENZYME OF THE PEROXIREDOXIN FAMILY               
REMARK   1  REF    J.BIOL.CHEM.                  V. 274 30451 1999              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  PMID   10521424                                                     
REMARK   1  DOI    10.1074/JBC.274.43.30451                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 28558                          
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) : 0.147                           
REMARK   3   R VALUE            (WORKING SET) : 0.146                           
REMARK   3   FREE R VALUE                     : 0.169                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1527                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2072                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1790                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 120                          
REMARK   3   BIN FREE R VALUE                    : 0.1710                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1196                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 12                                      
REMARK   3   SOLVENT ATOMS            : 285                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.15                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.47000                                              
REMARK   3    B22 (A**2) : 0.47000                                              
REMARK   3    B33 (A**2) : -0.93000                                             
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): 0.067         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.068         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.040         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.189         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.974                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.967                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1278 ; 0.019 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1194 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1729 ; 1.630 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2808 ; 0.842 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   161 ; 5.913 ; 5.000       
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):   202 ; 0.108 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1409 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   226 ; 0.011 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   330 ; 0.219 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1668 ; 0.260 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):   921 ; 0.093 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   235 ; 0.157 ; 0.200       
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):    14 ; 0.143 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    43 ; 0.213 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    29 ; 0.157 ; 0.200       
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):   814 ; 0.822 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1316 ; 1.490 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   464 ; 2.437 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   413 ; 4.045 ; 4.500       
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  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   161                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.7770  41.8070  20.1220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0294 T22:   0.0316                                     
REMARK   3      T33:   0.0130 T12:  -0.0060                                     
REMARK   3      T13:  -0.0071 T23:  -0.0164                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7648 L22:   1.3727                                     
REMARK   3      L33:   1.4383 L12:   0.0261                                     
REMARK   3      L13:   0.0285 L23:   0.6693                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0464 S12:   0.0983 S13:  -0.0215                       
REMARK   3      S21:  -0.1138 S22:  -0.0462 S23:   0.0957                       
REMARK   3      S31:   0.0458 S32:  -0.1566 S33:   0.0926                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1URM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-OCT-03.                  
REMARK 100 THE DEPOSITION ID IS D_1290013842.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-NOV-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.30                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : BW7A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9911                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL FOCUSING            
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : BENT MIRROR                        
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30149                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : 0.05300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 32.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.500                              
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: PDB ENTRY 1HD2                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 1.6 M      
REMARK 280  AMMONIUM SULFATE, 0.1 M SODIUM CITRATE BUFFER PH 5.3, 0.2 M         
REMARK 280  POTASSIUM SODIUM TARTRATE, 1 MM DTT, 0.02 % (W/V) SODIUM AZIDE,     
REMARK 280  PH 5.30                                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.02150            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       32.82300            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       32.82300            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       30.51075            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       32.82300            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       32.82300            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       91.53225            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       32.82300            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       32.82300            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       30.51075            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       32.82300            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       32.82300            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       91.53225            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       61.02150            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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 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 A2073  LIES ON A SPECIAL POSITION.                          
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED MUTATION CYS 100 SER (FOLLOWING NUMBERING                 
REMARK 400  OF THE SWISSPROT DATABASE REFERENCE).                               
REMARK 400                                                                      
REMARK 400  FUNCTION                                                            
REMARK 400   REDUCES HYDROGEN PEROXIDE AND HYDROPEROXIDES WITH                  
REMARK 400   REDUCING EQUIVALENTS USING THE THIOREDOXIN SYSTEM.                 
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ARG A   -10                                                      
REMARK 465     GLY A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 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   OE2  GLU A    18     O    HOH A  2040              2.19            
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      -56.93   -122.78                                   
REMARK 500    LYS A  93      -52.14   -120.91                                   
REMARK 500    ASP A 113     -152.80    -88.60                                   
REMARK 500    THR A 150      -99.75   -136.02                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1162                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1163                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1164                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEZ A 201                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1H4O   RELATED DB: PDB                                   
REMARK 900 MONOCLINIC FORM OF HUMAN PEROXIREDOXIN 5                             
REMARK 900 RELATED ID: 1HD2   RELATED DB: PDB                                   
REMARK 900 HUMAN PEROXIREDOXIN 5                                                
REMARK 900 RELATED ID: 1OC3   RELATED DB: PDB                                   
REMARK 900 HUMAN PEROXIREDOXIN 5                                                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 C47S MUTANT                                                          
DBREF  1URM A  -10     0  PDB    1URM     1URM           -10      0             
DBREF  1URM A    1   161  UNP    P30044   PDX5_HUMAN      54    214             
SEQADV 1URM SER A   47  UNP  P30044    CYS   100 ENGINEERED MUTATION            
SEQRES   1 A  172  ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA PRO          
SEQRES   2 A  172  ILE LYS VAL GLY ASP ALA ILE PRO ALA VAL GLU VAL PHE          
SEQRES   3 A  172  GLU GLY GLU PRO GLY ASN LYS VAL ASN LEU ALA GLU LEU          
SEQRES   4 A  172  PHE LYS GLY LYS LYS GLY VAL LEU PHE GLY VAL PRO GLY          
SEQRES   5 A  172  ALA PHE THR PRO GLY SER SER LYS THR HIS LEU PRO GLY          
SEQRES   6 A  172  PHE VAL GLU GLN ALA GLU ALA LEU LYS ALA LYS GLY VAL          
SEQRES   7 A  172  GLN VAL VAL ALA CYS LEU SER VAL ASN ASP ALA PHE VAL          
SEQRES   8 A  172  THR GLY GLU TRP GLY ARG ALA HIS LYS ALA GLU GLY LYS          
SEQRES   9 A  172  VAL ARG LEU LEU ALA ASP PRO THR GLY ALA PHE GLY LYS          
SEQRES  10 A  172  GLU THR ASP LEU LEU LEU ASP ASP SER LEU VAL SER ILE          
SEQRES  11 A  172  PHE GLY ASN ARG ARG LEU LYS ARG PHE SER MET VAL VAL          
SEQRES  12 A  172  GLN ASP GLY ILE VAL LYS ALA LEU ASN VAL GLU PRO ASP          
SEQRES  13 A  172  GLY THR GLY LEU THR CYS SER LEU ALA PRO ASN ILE ILE          
SEQRES  14 A  172  SER GLN LEU                                                  
HET    BEZ  A 201       9                                                       
HET     CL  A1162       1                                                       
HET     CL  A1163       1                                                       
HET     CL  A1164       1                                                       
HETNAM     BEZ BENZOIC ACID                                                     
HETNAM      CL CHLORIDE ION                                                     
FORMUL   2  BEZ    C7 H6 O2                                                     
FORMUL   3   CL    3(CL 1-)                                                     
FORMUL   6  HOH   *285(H2 O)                                                    
HELIX    1   1 LEU A   25  PHE A   29  1                                   5    
HELIX    2   2 THR A   44  ALA A   64  1                                  21    
HELIX    3   3 ASP A   77  HIS A   88  1                                  12    
HELIX    4   4 GLY A  102  ASP A  109  1                                   8    
HELIX    5   5 LEU A  116  GLY A  121  1                                   6    
HELIX    6   6 LEU A  153  SER A  159  1                                   7    
SHEET    1  AA 2 GLU A  13  PHE A  15  0                                        
SHEET    2  AA 2 LYS A  22  ASN A  24 -1  O  VAL A  23   N  VAL A  14           
SHEET    1  AB 5 ARG A  95  ALA A  98  0                                        
SHEET    2  AB 5 VAL A  67  SER A  74  1  O  VAL A  70   N  ARG A  95           
SHEET    3  AB 5 LYS A  33  GLY A  38  1  O  LYS A  33   N  GLN A  68           
SHEET    4  AB 5 PHE A 128  GLN A 133 -1  O  PHE A 128   N  GLY A  38           
SHEET    5  AB 5 ILE A 136  VAL A 142 -1  O  ILE A 136   N  GLN A 133           
SITE     1 AC1  4 LYS A  63  LYS A  93  SER A 118  HOH A2189                    
SITE     1 AC2  4 ARG A  86  LYS A  89  ALA A  90  GLU A  91                    
SITE     1 AC3  5 GLY A  54  PRO A 155  HOH A2022  HOH A2123                    
SITE     2 AC3  5 HOH A2132                                                     
SITE     1 AC4 11 PRO A  40  THR A  44  PRO A  45  GLY A  46                    
SITE     2 AC4 11 SER A  47  LYS A  63  ALA A  64  PHE A 120                    
SITE     3 AC4 11 ARG A 127  THR A 147  HOH A2145                               
CRYST1   65.646   65.646  122.043  90.00  90.00  90.00 P 41 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015233  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015233  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008194        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system