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Database: PDB
Entry: 1OC3
LinkDB: 1OC3
Original site: 1OC3 
HEADER    OXIDOREDUCTASE                          05-FEB-03   1OC3              
TITLE     HUMAN PEROXIREDOXIN 5                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEROXIREDOXIN 5;                                           
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: PEROXIREDOXIN 5, RESIDUES 54-214;                          
COMPND   5 SYNONYM: MITOCHONDRIAL PRECURSOR, PRX-V, PEROXISOMAL ANTIOXIDANT     
COMPND   6 ENZYME, PLP, THIOREDOXIN PEROXIDASE PMP20, ANTIOXIDANT ENZYME B166,  
COMPND   7 AOEB166, TPX TYPE VI, LIVER TISSUE 2D-PAGE SPOT 71B, ALU CO-REPRESSOR
COMPND   8 1, SBBI10;                                                           
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 ORGAN: LUNG;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI M15;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 1007065;                                    
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PQE-30                                    
KEYWDS    OXIDOREDUCTASE, ANTIOXIDANT ENZYME, PEROXIREDOXIN, THIOREDOXIN        
KEYWDS   2 PEROXIDASE, THIOREDOXIN FOLD, PEROXISOME, MITOCHONDRION, TRANSIT     
KEYWDS   3 PEPTIDE                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.EVRARD,J.-P.DECLERCQ                                                
REVDAT   7   24-JUL-19 1OC3    1       REMARK                                   
REVDAT   6   10-JUL-19 1OC3    1       REMARK                                   
REVDAT   5   24-OCT-18 1OC3    1       SOURCE REMARK                            
REVDAT   4   14-DEC-16 1OC3    1       COMPND KEYWDS JRNL   REMARK              
REVDAT   4 2                   1       VERSN  FORMUL HELIX  SHEET               
REVDAT   4 3                   1       MASTER                                   
REVDAT   3   24-FEB-09 1OC3    1       VERSN                                    
REVDAT   2   26-MAY-05 1OC3    1       JRNL                                     
REVDAT   1   10-FEB-04 1OC3    0                                                
JRNL        AUTH   C.EVRARD,A.CAPRON,C.MARCHAND,A.CLIPPE,R.WATTIEZ,             
JRNL        AUTH 2 P.SOUMILLION,B.KNOOPS,J.-P.DECLERCQ                          
JRNL        TITL   CRYSTAL STRUCTURE OF A DIMERIC OXIDIZED FORM OF HUMAN        
JRNL        TITL 2 PEROXIREDOXIN 5                                              
JRNL        REF    J.MOL.BIOL.                   V. 337  1079 2004              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   15046979                                                     
JRNL        DOI    10.1016/J.JMB.2004.02.017                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.P.DECLERCQ,C.EVRARD,A.CLIPPE,D.V.STRICHT,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. D57  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.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 72.55                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 36850                          
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) : 0.223                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1933                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2654                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2860                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 127                          
REMARK   3   BIN FREE R VALUE                    : 0.3550                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3576                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 18                                      
REMARK   3   SOLVENT ATOMS            : 62                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.93                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.80000                                              
REMARK   3    B22 (A**2) : -1.21000                                             
REMARK   3    B33 (A**2) : -3.59000                                             
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): 0.184         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.168         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.175         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.139         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.931                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3657 ; 0.021 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3443 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4944 ; 1.945 ; 1.985       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8034 ; 0.901 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   481 ; 4.963 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   655 ;18.816 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   571 ; 0.118 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4094 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   676 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   766 ; 0.235 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3341 ; 0.216 ; 0.300       
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):   218 ; 0.133 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     3 ; 0.096 ; 0.500       
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):    23 ; 0.397 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    80 ; 0.245 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.227 ; 0.500       
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):  2396 ; 0.913 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3825 ; 1.554 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1261 ; 2.739 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1119 ; 4.504 ; 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  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     0        A   161                          
REMARK   3    RESIDUE RANGE :   A   201        A   201                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.1250   7.5750  26.5190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1510 T22:   0.1153                                     
REMARK   3      T33:   0.1213 T12:  -0.0045                                     
REMARK   3      T13:   0.0269 T23:  -0.0184                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1411 L22:   1.4356                                     
REMARK   3      L33:   1.8217 L12:   0.1133                                     
REMARK   3      L13:  -0.9742 L23:  -0.4160                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1489 S12:   0.2075 S13:  -0.0332                       
REMARK   3      S21:  -0.0785 S22:  -0.0863 S23:  -0.1409                       
REMARK   3      S31:  -0.1796 S32:   0.1513 S33:  -0.0626                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   161                          
REMARK   3    RESIDUE RANGE :   B   201        B   201                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.7580  29.8860  68.4880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0456 T22:   0.2116                                     
REMARK   3      T33:   0.2017 T12:  -0.0557                                     
REMARK   3      T13:  -0.0389 T23:   0.0468                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1930 L22:   2.8155                                     
REMARK   3      L33:   2.7399 L12:  -0.2895                                     
REMARK   3      L13:   0.4779 L23:  -1.4381                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0458 S12:   0.1212 S13:   0.1268                       
REMARK   3      S21:  -0.3370 S22:   0.0092 S23:   0.0165                       
REMARK   3      S31:   0.0806 S32:  -0.0607 S33:   0.0366                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C   161                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.4240  -6.2980  57.0430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0931 T22:   0.2347                                     
REMARK   3      T33:   0.1951 T12:  -0.0300                                     
REMARK   3      T13:  -0.0200 T23:   0.0075                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0896 L22:   3.4240                                     
REMARK   3      L33:   2.8394 L12:  -0.9457                                     
REMARK   3      L13:   0.5710 L23:  -2.5917                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1356 S12:   0.0504 S13:   0.3052                       
REMARK   3      S21:   0.2800 S22:  -0.0715 S23:  -0.2475                       
REMARK   3      S31:  -0.5355 S32:   0.1706 S33:   0.2071                       
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 1OC3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-FEB-03.                  
REMARK 100 THE DEPOSITION ID IS D_1290012060.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JUL-02                          
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                       : BW7B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8441                             
REMARK 200  MONOCHROMATOR                  : TRIANGULAR MONOCHROMATOR           
REMARK 200  OPTICS                         : PREMIRROR, BENT MIRROR             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
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   : 38821                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.33200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1HD2                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 20% PEG    
REMARK 280  3350, 0.1 M SODIUM CITRATE BUFFER, PH 5.3, 1 MM DTT, 0.02 % (W/V)   
REMARK 280  SODIUM AZIDE, PH 5.30                                               
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       72.53000            
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       72.53000            
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       39.59750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       51.02650            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       39.59750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       51.02650            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       72.53000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       39.59750            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       51.02650            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       72.53000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       39.59750            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       51.02650            
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                                                 
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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 400                                                                      
REMARK 400 COMPOUND                                                             
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 465     ARG B   -10                                                      
REMARK 465     GLY B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     HIS B    -7                                                      
REMARK 465     HIS B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     ARG C   -10                                                      
REMARK 465     GLY C    -9                                                      
REMARK 465     SER C    -8                                                      
REMARK 465     HIS C    -7                                                      
REMARK 465     HIS C    -6                                                      
REMARK 465     HIS C    -5                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     HIS C    -3                                                      
REMARK 465     HIS C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  83   CD    GLU A  83   OE1    -0.074                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP B 114   CB  -  CG  -  OD2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ASP B 134   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP C  77   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 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      -54.84   -123.18                                   
REMARK 500    ASP A 113     -157.18    -83.30                                   
REMARK 500    THR A 150      -94.90   -132.82                                   
REMARK 500    LYS B  93      -46.53   -132.60                                   
REMARK 500    ASP B 113     -156.62    -88.65                                   
REMARK 500    THR B 150      -99.77   -135.05                                   
REMARK 500    PHE C  43       10.23     56.69                                   
REMARK 500    GLU C  91      120.08    -34.64                                   
REMARK 500    ASP C 145       -2.80     60.11                                   
REMARK 500    THR C 147       47.59    -73.51                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 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 BEZ A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEZ B 201                 
DBREF  1OC3 A  -10     0  PDB    1OC3     1OC3           -10      0             
DBREF  1OC3 A    1   161  UNP    P30044   PDX5_HUMAN      54    214             
DBREF  1OC3 B  -10     0  PDB    1OC3     1OC3           -10      0             
DBREF  1OC3 B    1   161  UNP    P30044   PDX5_HUMAN      54    214             
DBREF  1OC3 C  -10     0  PDB    1OC3     1OC3           -10      0             
DBREF  1OC3 C    1   161  UNP    P30044   PDX5_HUMAN      54    214             
SEQRES   1 A  172  ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA PRO          
SEQRES   2 A  172  ILE LYS VAL GLY ASP ALA ILE PRO ALA VAL GLU VAL PHE          
SEQRES   3 A  172  GLU GLY GLU PRO GLY ASN LYS VAL ASN LEU ALA GLU LEU          
SEQRES   4 A  172  PHE LYS GLY LYS LYS GLY VAL LEU PHE GLY VAL PRO GLY          
SEQRES   5 A  172  ALA PHE THR PRO GLY CYS SER LYS THR HIS LEU PRO GLY          
SEQRES   6 A  172  PHE VAL GLU GLN ALA GLU ALA LEU LYS ALA LYS GLY VAL          
SEQRES   7 A  172  GLN VAL VAL ALA CYS LEU SER VAL ASN ASP ALA PHE VAL          
SEQRES   8 A  172  THR GLY GLU TRP GLY ARG ALA HIS LYS ALA GLU GLY LYS          
SEQRES   9 A  172  VAL ARG LEU LEU ALA ASP PRO THR GLY ALA PHE GLY LYS          
SEQRES  10 A  172  GLU THR ASP LEU LEU LEU ASP ASP SER LEU VAL SER ILE          
SEQRES  11 A  172  PHE GLY ASN ARG ARG LEU LYS ARG PHE SER MET VAL VAL          
SEQRES  12 A  172  GLN ASP GLY ILE VAL LYS ALA LEU ASN VAL GLU PRO ASP          
SEQRES  13 A  172  GLY THR GLY LEU THR CYS SER LEU ALA PRO ASN ILE ILE          
SEQRES  14 A  172  SER GLN LEU                                                  
SEQRES   1 B  172  ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA PRO          
SEQRES   2 B  172  ILE LYS VAL GLY ASP ALA ILE PRO ALA VAL GLU VAL PHE          
SEQRES   3 B  172  GLU GLY GLU PRO GLY ASN LYS VAL ASN LEU ALA GLU LEU          
SEQRES   4 B  172  PHE LYS GLY LYS LYS GLY VAL LEU PHE GLY VAL PRO GLY          
SEQRES   5 B  172  ALA PHE THR PRO GLY CYS SER LYS THR HIS LEU PRO GLY          
SEQRES   6 B  172  PHE VAL GLU GLN ALA GLU ALA LEU LYS ALA LYS GLY VAL          
SEQRES   7 B  172  GLN VAL VAL ALA CYS LEU SER VAL ASN ASP ALA PHE VAL          
SEQRES   8 B  172  THR GLY GLU TRP GLY ARG ALA HIS LYS ALA GLU GLY LYS          
SEQRES   9 B  172  VAL ARG LEU LEU ALA ASP PRO THR GLY ALA PHE GLY LYS          
SEQRES  10 B  172  GLU THR ASP LEU LEU LEU ASP ASP SER LEU VAL SER ILE          
SEQRES  11 B  172  PHE GLY ASN ARG ARG LEU LYS ARG PHE SER MET VAL VAL          
SEQRES  12 B  172  GLN ASP GLY ILE VAL LYS ALA LEU ASN VAL GLU PRO ASP          
SEQRES  13 B  172  GLY THR GLY LEU THR CYS SER LEU ALA PRO ASN ILE ILE          
SEQRES  14 B  172  SER GLN LEU                                                  
SEQRES   1 C  172  ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA PRO          
SEQRES   2 C  172  ILE LYS VAL GLY ASP ALA ILE PRO ALA VAL GLU VAL PHE          
SEQRES   3 C  172  GLU GLY GLU PRO GLY ASN LYS VAL ASN LEU ALA GLU LEU          
SEQRES   4 C  172  PHE LYS GLY LYS LYS GLY VAL LEU PHE GLY VAL PRO GLY          
SEQRES   5 C  172  ALA PHE THR PRO GLY CYS SER LYS THR HIS LEU PRO GLY          
SEQRES   6 C  172  PHE VAL GLU GLN ALA GLU ALA LEU LYS ALA LYS GLY VAL          
SEQRES   7 C  172  GLN VAL VAL ALA CYS LEU SER VAL ASN ASP ALA PHE VAL          
SEQRES   8 C  172  THR GLY GLU TRP GLY ARG ALA HIS LYS ALA GLU GLY LYS          
SEQRES   9 C  172  VAL ARG LEU LEU ALA ASP PRO THR GLY ALA PHE GLY LYS          
SEQRES  10 C  172  GLU THR ASP LEU LEU LEU ASP ASP SER LEU VAL SER ILE          
SEQRES  11 C  172  PHE GLY ASN ARG ARG LEU LYS ARG PHE SER MET VAL VAL          
SEQRES  12 C  172  GLN ASP GLY ILE VAL LYS ALA LEU ASN VAL GLU PRO ASP          
SEQRES  13 C  172  GLY THR GLY LEU THR CYS SER LEU ALA PRO ASN ILE ILE          
SEQRES  14 C  172  SER GLN LEU                                                  
HET    BEZ  A 201       9                                                       
HET    BEZ  B 201       9                                                       
HETNAM     BEZ BENZOIC ACID                                                     
FORMUL   4  BEZ    2(C7 H6 O2)                                                  
FORMUL   6  HOH   *62(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  LYS A   65  1                                   8    
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  SER A  159  1                                   7    
HELIX    9   9 LEU B   25  LYS B   30  1                                   6    
HELIX   10  10 THR B   44  THR B   50  1                                   7    
HELIX   11  11 THR B   50  GLN B   58  1                                   9    
HELIX   12  12 GLN B   58  LYS B   65  1                                   8    
HELIX   13  13 ASP B   77  HIS B   88  1                                  12    
HELIX   14  14 GLY B  102  ASP B  109  1                                   8    
HELIX   15  15 LEU B  116  GLY B  121  1                                   6    
HELIX   16  16 LEU B  153  GLN B  160  1                                   8    
HELIX   17  17 LEU C   25  PHE C   29  1                                   5    
HELIX   18  18 CYS C   47  THR C   50  5                                   4    
HELIX   19  19 HIS C   51  GLN C   58  1                                   8    
HELIX   20  20 GLN C   58  LYS C   65  1                                   8    
HELIX   21  21 ASP C   77  HIS C   88  1                                  12    
HELIX   22  22 GLY C  102  ASP C  109  1                                   8    
HELIX   23  23 ASP C  113  SER C  115  5                                   3    
HELIX   24  24 LEU C  116  GLY C  121  1                                   6    
HELIX   25  25 ILE C  157  LEU C  161  5                                   5    
SHEET    1  AA 2 GLU A  13  PHE A  15  0                                        
SHEET    2  AA 2 LYS A  22  ASN A  24 -1  O  VAL A  23   N  VAL A  14           
SHEET    1  AB 5 ARG A  95  ALA A  98  0                                        
SHEET    2  AB 5 VAL A  67  SER A  74  1  O  VAL A  70   N  ARG A  95           
SHEET    3  AB 5 LYS A  33  GLY A  38  1  O  LYS A  33   N  GLN A  68           
SHEET    4  AB 5 PHE A 128  GLN A 133 -1  O  PHE A 128   N  GLY A  38           
SHEET    5  AB 5 ILE A 136  VAL A 142 -1  O  ILE A 136   N  GLN A 133           
SHEET    1  BA 7 LYS B  22  ASN B  24  0                                        
SHEET    2  BA 7 GLU B  13  GLU B  16 -1  O  VAL B  14   N  VAL B  23           
SHEET    3  BA 7 ARG B  95  ALA B  98 -1  O  ALA B  98   N  PHE B  15           
SHEET    4  BA 7 VAL B  69  SER B  74  1  O  VAL B  70   N  ARG B  95           
SHEET    5  BA 7 LYS B  33  VAL B  39  1  O  VAL B  35   N  ALA B  71           
SHEET    6  BA 7 PHE B 128  GLN B 133 -1  O  PHE B 128   N  GLY B  38           
SHEET    7  BA 7 ILE B 136  VAL B 142 -1  O  ILE B 136   N  GLN B 133           
SHEET    1  CA 2 GLU C  13  PHE C  15  0                                        
SHEET    2  CA 2 LYS C  22  ASN C  24 -1  O  VAL C  23   N  VAL C  14           
SHEET    1  CB 5 ARG C  95  ALA C  98  0                                        
SHEET    2  CB 5 VAL C  69  SER C  74  1  O  VAL C  70   N  ARG C  95           
SHEET    3  CB 5 LYS C  33  GLY C  38  1  O  VAL C  35   N  ALA C  71           
SHEET    4  CB 5 PHE C 128  GLN C 133 -1  O  PHE C 128   N  GLY C  38           
SHEET    5  CB 5 ILE C 136  VAL C 142 -1  O  ILE C 136   N  GLN C 133           
SSBOND   1 CYS C   47    CYS C  151                          1555   4556  2.43  
SITE     1 AC1  6 PRO A  40  THR A  44  GLY A  46  CYS A  47                    
SITE     2 AC1  6 ARG A 127  ALA C  64                                          
SITE     1 AC2  8 LYS A  63  ALA A  64  GLY A  66  PRO B  40                    
SITE     2 AC2  8 THR B  44  GLY B  46  CYS B  47  ARG B 127                    
CRYST1   79.195  102.053  145.060  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      0.012627  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009799  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006894        0.00000                         
MTRIX1   1 -0.217500 -0.975800 -0.024300       27.50350    1                    
MTRIX2   1  0.975600 -0.218100  0.024300       19.09820    1                    
MTRIX3   1 -0.029000 -0.018400  0.999400       42.49590    1                    
MTRIX1   2  0.243600 -0.969900  0.005300       26.58770    1                    
MTRIX2   2  0.969900  0.243600  0.000400      -20.18920    1                    
MTRIX3   2 -0.001600  0.005100  1.000000       30.41330    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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