GenomeNet

Database: PDB
Entry: 3MNG
LinkDB: 3MNG
Original site: 3MNG 
HEADER    OXIDOREDUCTASE                          21-APR-10   3MNG              
TITLE     WILD TYPE HUMAN PRXV WITH DTT BOUND AS A COMPETITIVE INHIBITOR        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEROXIREDOXIN-5, MITOCHONDRIAL;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PEROXIREDOXIN V, PRX-V, PEROXISOMAL ANTIOXIDANT ENZYME, PLP,
COMPND   5 THIOREDOXIN REDUCTASE, THIOREDOXIN PEROXIDASE PMP20, ANTIOXIDANT     
COMPND   6 ENZYME B166, AOEB166, TPX TYPE VI, LIVER TISSUE 2D-PAGE SPOT 71B, ALU
COMPND   7 COREPRESSOR 1;                                                       
COMPND   8 EC: 1.11.1.15;                                                       
COMPND   9 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: ACR1, AOEB166, ARC1, PMP20, PRDX5, SBBI10;                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: B834/PREP4;                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PQE30-PRX5                                
KEYWDS    PEROXIREDOXIN, PEROXIDASE, PRXV, SUBSTRATE ANALOG, DTT,               
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.HALL,P.A.KARPLUS                                                    
REVDAT   2   15-SEP-10 3MNG    1       JRNL                                     
REVDAT   1   04-AUG-10 3MNG    0                                                
JRNL        AUTH   A.HALL,D.PARSONAGE,L.B.POOLE,P.A.KARPLUS                     
JRNL        TITL   STRUCTURAL EVIDENCE THAT PEROXIREDOXIN CATALYTIC POWER IS    
JRNL        TITL 2 BASED ON TRANSITION-STATE STABILIZATION.                     
JRNL        REF    J.MOL.BIOL.                   V. 402   194 2010              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   20643143                                                     
JRNL        DOI    10.1016/J.JMB.2010.07.022                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 59.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 48609                          
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) : 0.114                           
REMARK   3   R VALUE            (WORKING SET) : 0.113                           
REMARK   3   FREE R VALUE                     : 0.136                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2633                            
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) : 1.45                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.49                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3564                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.84                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1660                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 184                          
REMARK   3   BIN FREE R VALUE                    : 0.1890                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1190                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 288                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 11.05                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.29000                                             
REMARK   3    B22 (A**2) : -0.29000                                             
REMARK   3    B33 (A**2) : 0.58000                                              
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): 0.035         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.036         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.016         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.923         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.978                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.969                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1251 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):   861 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1692 ; 2.726 ; 1.997       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2118 ; 2.413 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   166 ; 6.104 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    47 ;37.523 ;25.319       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   214 ;10.911 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     5 ;11.064 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   195 ; 0.161 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1384 ; 0.013 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   228 ; 0.001 ; 0.020       
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):   804 ; 3.104 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   334 ; 1.081 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1291 ; 4.357 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   447 ; 6.900 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   398 ; 9.969 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2112 ; 2.816 ; 3.000       
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 : 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 3MNG COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-APR-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB058764.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-DEC-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.978                              
REMARK 200  MONOCHROMATOR                  : SINGLE CRYSTAL, CYLINDRICALLY      
REMARK 200                                   BENT SI(220)                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48609                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 59.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 36.700                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 30.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.00                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.39300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: RIGID BODY REFINEMENT OF     
REMARK 200  STARTING MODEL                                                      
REMARK 200 SOFTWARE USED: REFMAC 5.5.0109                                       
REMARK 200 STARTING MODEL: PDB CODE 1HD2 WITH BENZOATE REMOVED                  
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR CONTAINED 1.6 M AMMONIUM       
REMARK 280  SULFATE, 0.1 M SODIUM CITRATE, 0.2 M SODIUM/POTASSIUM TARTRATE.     
REMARK 280  PROTEIN WAS STORED AT 0.8 MM WITH 10 MM DTT., PH 5.6, VAPOR         
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
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       61.93350            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       33.65650            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       33.65650            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       30.96675            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       33.65650            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       33.65650            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       92.90025            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       33.65650            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       33.65650            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       30.96675            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       33.65650            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       33.65650            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       92.90025            
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       61.93350            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000 -1.000000  0.000000       67.31300            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000       67.31300            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       61.93350            
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 A1016  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     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 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    GLU A  57   OE1 -  CD  -  OE2 ANGL. DEV. = -11.3 DEGREES          
REMARK 500    LYS A  89   CD  -  CE  -  NZ  ANGL. DEV. =  15.3 DEGREES          
REMARK 500    MET A 130   CG  -  SD  -  CE  ANGL. DEV. =  13.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  50      -61.99   -126.14                                   
REMARK 500    ASP A 113     -149.00    -86.26                                   
REMARK 500    ASP A 134       60.15     39.18                                   
REMARK 500    THR A 150     -100.32   -135.70                                   
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 A1200        DISTANCE =  9.64 ANGSTROMS                       
REMARK 525    HOH A1279        DISTANCE =  5.79 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D1D A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 306                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 307                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 308                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 402                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1HD2   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN BOUND TO BENZOATE AT 1.5 A RESOLUTION.              
REMARK 900 RELATED ID: 1H4O   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN BOUND TO BENZOATE AT 2.0 A RESOLUTION.              
REMARK 900 RELATED ID: 1OC3   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN BOUND TO BENZOATE AT 2.0 A RESOLUTION.              
REMARK 900 RELATED ID: 1URM   RELATED DB: PDB                                   
REMARK 900 THE C47S MUTANT OF THE SAME PROTEIN BOUND TO BENZOATE AT             
REMARK 900 1.7 A RESOLUTION.                                                    
REMARK 900 RELATED ID: 2VL2   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN BOUND TO BENZOATE AT 1.9 A RESOLUTION.              
REMARK 900 RELATED ID: 2VL3   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN AT 1.8 A RESOLUTION.                                
DBREF  3MNG A    1   161  UNP    P30044   PRDX5_HUMAN     54    214             
SEQADV 3MNG MET A  -11  UNP  P30044              EXPRESSION TAG                 
SEQADV 3MNG ARG A  -10  UNP  P30044              EXPRESSION TAG                 
SEQADV 3MNG GLY A   -9  UNP  P30044              EXPRESSION TAG                 
SEQADV 3MNG SER A   -8  UNP  P30044              EXPRESSION TAG                 
SEQADV 3MNG HIS A   -7  UNP  P30044              EXPRESSION TAG                 
SEQADV 3MNG HIS A   -6  UNP  P30044              EXPRESSION TAG                 
SEQADV 3MNG HIS A   -5  UNP  P30044              EXPRESSION TAG                 
SEQADV 3MNG HIS A   -4  UNP  P30044              EXPRESSION TAG                 
SEQADV 3MNG HIS A   -3  UNP  P30044              EXPRESSION TAG                 
SEQADV 3MNG HIS A   -2  UNP  P30044              EXPRESSION TAG                 
SEQADV 3MNG GLY A   -1  UNP  P30044              EXPRESSION TAG                 
SEQADV 3MNG SER A    0  UNP  P30044              EXPRESSION TAG                 
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 CYS 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                                              
HET    D1D  A 201       8                                                       
HET     BR  A 301       1                                                       
HET     BR  A 302       1                                                       
HET     BR  A 303       1                                                       
HET     BR  A 304       1                                                       
HET     BR  A 305       1                                                       
HET     BR  A 306       1                                                       
HET     BR  A 307       1                                                       
HET     BR  A 308       1                                                       
HET    GOL  A 401       6                                                       
HET    GOL  A 402       6                                                       
HETNAM     D1D (4S,5S)-1,2-DITHIANE-4,5-DIOL                                    
HETNAM      BR BROMIDE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  D1D    C4 H8 O2 S2                                                  
FORMUL   3   BR    8(BR 1-)                                                     
FORMUL  11  GOL    2(C3 H8 O3)                                                  
FORMUL  13  HOH   *288(H2 O)                                                    
HELIX    1   1 LEU A   25  PHE A   29  1                                   5    
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 LEU A  116  GLY A  121  1                                   6    
HELIX    8   8 LEU A  153  LEU A  161  1                                   9    
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  69  SER A  74  1  N  CYS A  72   O  LEU A  97           
SHEET    3   B 5 LYS A  33  GLY A  38  1  N  PHE A  37   O  LEU A  73           
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  LYS A 138   N  VAL A 131           
SITE     1 AC1  7 PRO A  40  THR A  44  GLY A  46  CYS A  47                    
SITE     2 AC1  7 ALA A  64  GLY A  66  ARG A 127                               
SITE     1 AC2  3 LYS A  63  LYS A  93  SER A 118                               
SITE     1 AC3  1 PRO A 155                                                     
SITE     1 AC4  2 GLN A 133  LEU A 149                                          
SITE     1 AC5  2 ALA A  90  GLU A  91                                          
SITE     1 AC6  3 GLN A  68  ASP A 113  SER A 115                               
SITE     1 AC7  1 HIS A  88                                                     
SITE     1 AC8  1 VAL A   5                                                     
SITE     1 AC9  2 HOH A1053  HOH A1122                                          
SITE     1 BC1  4 THR A 150  CYS A 151  HOH A1154  HOH A1195                    
SITE     1 BC2  5 HOH A1142  HOH A1211  HOH A1241  HOH A1250                    
SITE     2 BC2  5 HOH A1256                                                     
CRYST1   67.313   67.313  123.867  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      0.014856  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014856  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008073        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system