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Database: PDB
Entry: 1H4O
LinkDB: 1H4O
Original site: 1H4O 
HEADER    OXIDOREDUCTASE                          11-MAY-01   1H4O              
TITLE     MONOCLINIC FORM OF HUMAN PEROXIREDOXIN 5                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEROXIREDOXIN 5;                                           
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 FRAGMENT: RESIDUES 54-214;                                           
COMPND   5 SYNONYM: PRDX5, PRXV, AOEB166, PMP20, ARC1;                          
COMPND   6 EC: 1.11.1.15;                                                       
COMPND   7 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_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PQE-30                                    
KEYWDS    ANTIOXIDANT ENZYME, THIOREDOXIN PEROTHIOREDOXIN, FOLDXIDASE,          
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.P.DECLERCQ,C.EVRARD                                                 
REVDAT   5   05-FEB-14 1H4O    1       HEADER COMPND SOURCE KEYWDS              
REVDAT   5 2                           REMARK                                   
REVDAT   4   13-JUL-11 1H4O    1       VERSN                                    
REVDAT   3   24-FEB-09 1H4O    1       VERSN                                    
REVDAT   2   23-NOV-01 1H4O    1       JRNL                                     
REVDAT   1   23-OCT-01 1H4O    0                                                
JRNL        AUTH   J.P.DECLERCQ,C.EVRARD,A.CLIPPE,D.V.STRICHT,A.BERNARD,        
JRNL        AUTH 2 B.KNOOPS                                                     
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN PEROXIREDOXIN 5, A NOVEL TYPE OF  
JRNL        TITL 2 MAMMALIAN PEROXIREDOXIN AT 1.5 A RESOLUTION                  
JRNL        REF    J.MOL.BIOL.                   V. 311   751 2001              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   11518528                                                     
JRNL        DOI    10.1006/JMBI.2001.4853                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   B.KNOOPS,A.CLIPPE,C.BOGARD,K.ARSALANE,R.WATTIEZ,C.HERMANS,   
REMARK   1  AUTH 2 E.DUCONSEILLE,P.FALMAGNE,A.BERNARD                           
REMARK   1  TITL   CLONING AND CHARACTERIZATION OF AOEB166, A NOVEL MAMMALIAN   
REMARK   1  TITL 2 ANTIOXIDANT ENZYME OF THE PEROXIREDOXIN FAMILY               
REMARK   1  REF    J.BIOL.CHEM.                  V. 274 30451 1999              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  PMID   10521424                                                     
REMARK   1  DOI    10.1074/JBC.274.43.30451                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
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) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 140398                         
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) : 0.166                           
REMARK   3   R VALUE            (WORKING SET) : 0.165                           
REMARK   3   FREE R VALUE                     : 0.190                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7402                            
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) : 1.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.00                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 10293                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2000                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 551                          
REMARK   3   BIN FREE R VALUE                    : 0.2370                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9520                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 72                                      
REMARK   3   SOLVENT ATOMS            : 1213                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.111         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.107         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.106         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.600         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.949                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9760 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  9184 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 13192 ; 1.799 ; 1.987       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES): 21424 ; 1.117 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1520 ; 0.112 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10928 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1800 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2119 ; 0.227 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  8826 ; 0.210 ; 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):  1016 ; 0.157 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     7 ; 0.208 ; 0.000       
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):    32 ; 0.153 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):   153 ; 0.178 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    64 ; 0.125 ; 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):  6384 ; 0.674 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10184 ; 1.284 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3376 ; 2.667 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3008 ; 4.489 ; 4.500       
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 : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D E F G H                 
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A      14      3                      
REMARK   3           1     B      1       B      14      3                      
REMARK   3           1     C      1       C      14      3                      
REMARK   3           1     D      1       D      14      3                      
REMARK   3           1     E      1       E      14      3                      
REMARK   3           1     F      1       F      14      3                      
REMARK   3           1     G      1       G      14      3                      
REMARK   3           1     H      1       H      14      3                      
REMARK   3           2     A     15       A      24      5                      
REMARK   3           2     B     15       B      24      5                      
REMARK   3           2     C     15       C      24      5                      
REMARK   3           2     D     15       D      24      5                      
REMARK   3           2     E     15       E      24      5                      
REMARK   3           2     F     15       F      24      5                      
REMARK   3           2     G     15       G      24      5                      
REMARK   3           2     H     15       H      24      5                      
REMARK   3           3     A     25       A     161      3                      
REMARK   3           3     B     25       B     161      3                      
REMARK   3           3     C     25       C     161      3                      
REMARK   3           3     D     25       D     161      3                      
REMARK   3           3     E     25       E     161      3                      
REMARK   3           3     F     25       F     161      3                      
REMARK   3           3     G     25       G     161      3                      
REMARK   3           3     H     25       H     161      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    880 ;  0.12 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):    880 ;  0.11 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    C    (A):    880 ;  0.07 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    D    (A):    880 ;  0.08 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    E    (A):    880 ;  0.07 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    F    (A):    880 ;  0.07 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    G    (A):    880 ;  0.10 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    H    (A):    880 ;  0.08 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):     57 ;  0.37 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):     57 ;  1.01 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):     57 ;  0.43 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):     57 ;  0.42 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    E    (A):     57 ;  0.42 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    F    (A):     57 ;  0.43 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    G    (A):     57 ;  0.45 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    H    (A):     57 ;  1.40 ;  0.50           
REMARK   3   LOOSE POSITIONAL   1    A    (A):   1396 ;  0.65 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    B    (A):   1396 ;  0.78 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    C    (A):   1396 ;  0.47 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    D    (A):   1396 ;  0.49 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    E    (A):   1396 ;  0.58 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    F    (A):   1396 ;  0.49 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    G    (A):   1396 ;  0.70 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    H    (A):   1396 ;  0.89 ;  5.00           
REMARK   3   TIGHT THERMAL      1    A (A**2):    880 ;  0.21 ;  0.50           
REMARK   3   TIGHT THERMAL      1    B (A**2):    880 ;  0.20 ;  0.50           
REMARK   3   TIGHT THERMAL      1    C (A**2):    880 ;  0.20 ;  0.50           
REMARK   3   TIGHT THERMAL      1    D (A**2):    880 ;  0.20 ;  0.50           
REMARK   3   TIGHT THERMAL      1    E (A**2):    880 ;  0.19 ;  0.50           
REMARK   3   TIGHT THERMAL      1    F (A**2):    880 ;  0.17 ;  0.50           
REMARK   3   TIGHT THERMAL      1    G (A**2):    880 ;  0.18 ;  0.50           
REMARK   3   TIGHT THERMAL      1    H (A**2):    880 ;  0.18 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):     57 ;  1.75 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):     57 ;  4.94 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):     57 ;  0.81 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    D (A**2):     57 ;  2.86 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    E (A**2):     57 ;  1.53 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    F (A**2):     57 ;  2.23 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    G (A**2):     57 ;  1.86 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    H (A**2):     57 ;  4.43 ;  2.00           
REMARK   3   LOOSE THERMAL      1    A (A**2):   1396 ;  1.66 ; 10.00           
REMARK   3   LOOSE THERMAL      1    B (A**2):   1396 ;  2.17 ; 10.00           
REMARK   3   LOOSE THERMAL      1    C (A**2):   1396 ;  1.44 ; 10.00           
REMARK   3   LOOSE THERMAL      1    D (A**2):   1396 ;  1.63 ; 10.00           
REMARK   3   LOOSE THERMAL      1    E (A**2):   1396 ;  1.58 ; 10.00           
REMARK   3   LOOSE THERMAL      1    F (A**2):   1396 ;  1.31 ; 10.00           
REMARK   3   LOOSE THERMAL      1    G (A**2):   1396 ;  1.51 ; 10.00           
REMARK   3   LOOSE THERMAL      1    H (A**2):   1396 ;  1.78 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B C D E F G H                 
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A   1162       A    1162      1                      
REMARK   3           1     B   1162       B    1162      1                      
REMARK   3           1     C   1162       C    1162      1                      
REMARK   3           1     D   1162       D    1162      1                      
REMARK   3           1     E   1162       E    1162      1                      
REMARK   3           1     F   1162       F    1162      1                      
REMARK   3           1     G   1162       G    1162      1                      
REMARK   3           1     H   1162       H    1162      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    A    (A):    894 ;  0.01 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    B    (A):    894 ;  0.01 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    C    (A):    894 ;  0.01 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    D    (A):    894 ;  0.01 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    E    (A):    894 ;  0.01 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    F    (A):    894 ;  0.01 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    G    (A):    894 ;  0.01 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    H    (A):    894 ;  0.01 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  2    A    (A):     57 ;  0.08 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    B    (A):     57 ;  0.13 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    C    (A):     57 ;  0.09 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    D    (A):     57 ;  0.09 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    E    (A):     57 ;  0.09 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    F    (A):     57 ;  0.09 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    G    (A):     57 ;  0.09 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    H    (A):     57 ;  0.16 ;  0.50           
REMARK   3   LOOSE POSITIONAL   2    A    (A):   1396 ;  0.02 ;  5.00           
REMARK   3   LOOSE POSITIONAL   2    B    (A):   1396 ;  0.02 ;  5.00           
REMARK   3   LOOSE POSITIONAL   2    C    (A):   1396 ;  0.02 ;  5.00           
REMARK   3   LOOSE POSITIONAL   2    D    (A):   1396 ;  0.02 ;  5.00           
REMARK   3   LOOSE POSITIONAL   2    E    (A):   1396 ;  0.02 ;  5.00           
REMARK   3   LOOSE POSITIONAL   2    F    (A):   1396 ;  0.02 ;  5.00           
REMARK   3   LOOSE POSITIONAL   2    G    (A):   1396 ;  0.02 ;  5.00           
REMARK   3   LOOSE POSITIONAL   2    H    (A):   1396 ;  0.03 ;  5.00           
REMARK   3   TIGHT THERMAL      2    A (A**2):    894 ;  1.22 ;  0.50           
REMARK   3   TIGHT THERMAL      2    B (A**2):    894 ;  1.18 ;  0.50           
REMARK   3   TIGHT THERMAL      2    C (A**2):    894 ;  1.18 ;  0.50           
REMARK   3   TIGHT THERMAL      2    D (A**2):    894 ;  1.19 ;  0.50           
REMARK   3   TIGHT THERMAL      2    E (A**2):    894 ;  1.15 ;  0.50           
REMARK   3   TIGHT THERMAL      2    F (A**2):    894 ;  1.09 ;  0.50           
REMARK   3   TIGHT THERMAL      2    G (A**2):    894 ;  1.13 ;  0.50           
REMARK   3   TIGHT THERMAL      2    H (A**2):    894 ;  1.11 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    A (A**2):     57 ; 13.84 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    B (A**2):     57 ; 23.25 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    C (A**2):     57 ;  9.43 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    D (A**2):     57 ; 17.67 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    E (A**2):     57 ; 12.95 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    F (A**2):     57 ; 15.62 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    G (A**2):     57 ; 14.27 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    H (A**2):     57 ; 22.01 ;  2.00           
REMARK   3   LOOSE THERMAL      2    A (A**2):   1396 ;  2.73 ; 10.00           
REMARK   3   LOOSE THERMAL      2    B (A**2):   1396 ;  3.11 ; 10.00           
REMARK   3   LOOSE THERMAL      2    C (A**2):   1396 ;  2.53 ; 10.00           
REMARK   3   LOOSE THERMAL      2    D (A**2):   1396 ;  2.70 ; 10.00           
REMARK   3   LOOSE THERMAL      2    E (A**2):   1396 ;  2.66 ; 10.00           
REMARK   3   LOOSE THERMAL      2    F (A**2):   1396 ;  2.42 ; 10.00           
REMARK   3   LOOSE THERMAL      2    G (A**2):   1396 ;  2.60 ; 10.00           
REMARK   3   LOOSE THERMAL      2    H (A**2):   1396 ;  2.82 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
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     1        A   161                          
REMARK   3    RESIDUE RANGE :   A  1162        A  1162                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.3310   6.7580 -26.9610              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0598 T22:   0.1344                                     
REMARK   3      T33:   0.0603 T12:   0.0084                                     
REMARK   3      T13:  -0.0031 T23:  -0.0068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0339 L22:   0.9453                                     
REMARK   3      L33:   2.3691 L12:  -0.0882                                     
REMARK   3      L13:   0.3877 L23:  -0.5139                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0279 S12:   0.1243 S13:   0.1811                       
REMARK   3      S21:  -0.1246 S22:   0.0096 S23:   0.0595                       
REMARK   3      S31:  -0.1723 S32:  -0.3316 S33:   0.0183                       
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  1162        B  1162                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.8550  23.0000   5.7260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0620 T22:   0.1738                                     
REMARK   3      T33:   0.0854 T12:   0.0335                                     
REMARK   3      T13:  -0.0013 T23:  -0.0434                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2985 L22:   2.7278                                     
REMARK   3      L33:   3.4199 L12:  -0.4076                                     
REMARK   3      L13:  -0.3371 L23:   2.1782                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0033 S12:   0.3506 S13:  -0.0708                       
REMARK   3      S21:  -0.2160 S22:  -0.2676 S23:   0.2619                       
REMARK   3      S31:   0.0377 S32:  -0.2567 S33:   0.2709                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C   161                          
REMARK   3    RESIDUE RANGE :   C  1162        C  1162                          
REMARK   3    ORIGIN FOR THE GROUP (A): -24.8250  18.6030  36.7320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0959 T22:   0.0182                                     
REMARK   3      T33:   0.0749 T12:  -0.0254                                     
REMARK   3      T13:   0.0532 T23:  -0.0369                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7155 L22:   1.3897                                     
REMARK   3      L33:   2.1905 L12:   0.0644                                     
REMARK   3      L13:  -0.9259 L23:   0.1812                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1284 S12:   0.2403 S13:  -0.2124                       
REMARK   3      S21:  -0.1820 S22:  -0.0509 S23:   0.0374                       
REMARK   3      S31:   0.2087 S32:  -0.0479 S33:   0.1793                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D   161                          
REMARK   3    RESIDUE RANGE :   D  1162        D  1162                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.6440   1.0870  67.5180              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0653 T22:   0.0382                                     
REMARK   3      T33:   0.0825 T12:   0.0027                                     
REMARK   3      T13:   0.0398 T23:   0.0287                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2767 L22:   2.0637                                     
REMARK   3      L33:   2.0570 L12:   0.2821                                     
REMARK   3      L13:  -0.8021 L23:  -0.9960                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0563 S12:   0.0145 S13:  -0.0538                       
REMARK   3      S21:  -0.1583 S22:  -0.1025 S23:  -0.2789                       
REMARK   3      S31:  -0.0361 S32:   0.2810 S33:   0.1588                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     1        E   161                          
REMARK   3    RESIDUE RANGE :   E  1162        E  1162                          
REMARK   3    ORIGIN FOR THE GROUP (A):  58.4430   2.8990 -26.2660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1602 T22:   0.1167                                     
REMARK   3      T33:   0.1211 T12:   0.0054                                     
REMARK   3      T13:  -0.0492 T23:   0.0517                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8511 L22:   2.4724                                     
REMARK   3      L33:   2.0086 L12:  -1.1434                                     
REMARK   3      L13:   1.2402 L23:  -0.3610                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0337 S12:   0.4936 S13:   0.2936                       
REMARK   3      S21:  -0.4055 S22:  -0.2862 S23:  -0.0965                       
REMARK   3      S31:  -0.1675 S32:   0.0773 S33:   0.2525                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     1        F   161                          
REMARK   3    RESIDUE RANGE :   F  1162        F  1162                          
REMARK   3    ORIGIN FOR THE GROUP (A):  56.2770  20.3120   4.6760              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1002 T22:   0.0461                                     
REMARK   3      T33:   0.1184 T12:   0.0019                                     
REMARK   3      T13:  -0.0624 T23:  -0.0071                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7316 L22:   2.0273                                     
REMARK   3      L33:   1.7197 L12:   0.5100                                     
REMARK   3      L13:   0.5145 L23:   0.7604                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0655 S12:   0.1165 S13:   0.0620                       
REMARK   3      S21:  -0.2067 S22:  -0.0092 S23:   0.2401                       
REMARK   3      S31:   0.0622 S32:  -0.1440 S33:   0.0747                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G     1        G   161                          
REMARK   3    RESIDUE RANGE :   G  1162        G  1162                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.1470  19.9660  35.2670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1519 T22:   0.1392                                     
REMARK   3      T33:   0.0741 T12:  -0.0341                                     
REMARK   3      T13:  -0.0130 T23:  -0.0065                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8236 L22:   1.7206                                     
REMARK   3      L33:   1.8468 L12:  -0.3014                                     
REMARK   3      L13:  -0.7862 L23:   0.3822                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0037 S12:   0.0839 S13:  -0.1418                       
REMARK   3      S21:  -0.2490 S22:   0.0104 S23:  -0.0426                       
REMARK   3      S31:   0.2692 S32:   0.0586 S33:  -0.0067                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H     1        H   161                          
REMARK   3    RESIDUE RANGE :   H  1162        H  1162                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.8240   3.5500  67.9780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0924 T22:   0.2385                                     
REMARK   3      T33:   0.0744 T12:   0.0575                                     
REMARK   3      T13:   0.0099 T23:   0.0063                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5734 L22:   2.4085                                     
REMARK   3      L33:   3.0266 L12:  -0.0821                                     
REMARK   3      L13:  -0.0643 L23:  -1.5129                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0099 S12:   0.3282 S13:   0.0104                       
REMARK   3      S21:  -0.3448 S22:  -0.0952 S23:  -0.1411                       
REMARK   3      S31:   0.0799 S32:   0.2207 S33:   0.0853                       
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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 1H4O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-MAY-01.                  
REMARK 100 THE PDBE ID CODE IS EBI-8028.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-00                          
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               : ESRF                               
REMARK 200  BEAMLINE                       : BM30A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.978766                           
REMARK 200  MONOCHROMATOR                  : FLAT AND N2 COOLED AND             
REMARK 200                                   SAGITTALY BENT MONOCHROMATORS      
REMARK 200  OPTICS                         : TWO MIRRORS                        
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : MAR 345                            
REMARK 200  DETECTOR MANUFACTURER          : X-RAY RESEARCH                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 151926                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 1.830                              
REMARK 200  R MERGE                    (I) : 0.03200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.14200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIR                          
REMARK 200 SOFTWARE USED: MLPHARE, DM                                           
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NCS AVERAGING                                                
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 67                                         
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM            
REMARK 280  1.6 M AMMONIUM SULFATE,  0.1 M SODIUM CITRATE BUFFER                
REMARK 280  PH 5.3, 0.2 M POTASSIUM SODIUM TARTRATE, 1 MM DTT,                  
REMARK 280  0.02 % (W/V) SODIUM AZIDE                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       33.24500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
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: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
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: E                                     
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: 6                                                       
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: F                                     
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: 7                                                       
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: G                                     
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: 8                                                       
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: H                                     
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    LEU C   161     O    HOH C  2187              2.19            
REMARK 500   NZ   LYS D    49     O    HOH D  2067              2.18            
REMARK 500   N    GLY E    31     OD1  ASP E   134              2.17            
REMARK 500   OE2  GLU E    83     NH1  ARG E    86              2.16            
REMARK 500   OXT  LEU E   161     O    HOH E  2127              2.10            
REMARK 500   O    LEU G   161     O    HOH G  2138              2.19            
REMARK 500   O    HOH C  2014     O    HOH C  2045              2.14            
REMARK 500   O    HOH G  2011     O    HOH F  2154              2.17            
REMARK 500   O    HOH G  2035     O    HOH F  2151              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    MET G 130   SD    MET G 130   CE     -0.394                       
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 A 113   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP D 114   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ARG E  95   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG H  86   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  50      -58.15   -122.32                                   
REMARK 500    THR A 150      -93.33   -137.46                                   
REMARK 500    GLU B  18       85.27    -55.28                                   
REMARK 500    PRO B  19       17.51    -44.77                                   
REMARK 500    THR B  50      -56.61   -122.68                                   
REMARK 500    ASP B 113     -156.21    -83.66                                   
REMARK 500    THR B 150      -96.15   -141.05                                   
REMARK 500    THR C  50      -57.11   -125.76                                   
REMARK 500    ASP C 113     -157.73    -82.09                                   
REMARK 500    THR C 150      -95.45   -140.96                                   
REMARK 500    THR D  50      -57.75   -125.38                                   
REMARK 500    ASP D 113     -158.39    -82.78                                   
REMARK 500    THR D 150      -94.99   -140.89                                   
REMARK 500    THR E  50      -58.35   -129.28                                   
REMARK 500    ASP E 113     -159.38    -79.91                                   
REMARK 500    THR E 150      -94.60   -139.19                                   
REMARK 500    THR F  50      -57.11   -121.60                                   
REMARK 500    THR F 150      -94.19   -138.19                                   
REMARK 500    THR G  50      -58.61   -122.21                                   
REMARK 500    ASP G 113     -164.95    -79.36                                   
REMARK 500    THR G 150      -95.59   -137.75                                   
REMARK 500    GLU H  18       97.64    -36.54                                   
REMARK 500    THR H  50      -55.29   -125.78                                   
REMARK 500    ASP H 113     -158.70    -81.45                                   
REMARK 500    THR H 150      -97.93   -139.14                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEZ A1162                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEZ B1162                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEZ C1162                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEZ D1162                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEZ E1162                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEZ F1162                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEZ G1162                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEZ H1162                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1HD2   RELATED DB: PDB                                   
REMARK 900  HUMAN PEROXIREDOXIN 5                                               
DBREF  1H4O A    1   161  UNP    P30044   AOPP_HUMAN      54    214             
DBREF  1H4O B    1   161  UNP    P30044   AOPP_HUMAN      54    214             
DBREF  1H4O C    1   161  UNP    P30044   AOPP_HUMAN      54    214             
DBREF  1H4O D    1   161  UNP    P30044   AOPP_HUMAN      54    214             
DBREF  1H4O E    1   161  UNP    P30044   AOPP_HUMAN      54    214             
DBREF  1H4O F    1   161  UNP    P30044   AOPP_HUMAN      54    214             
DBREF  1H4O G    1   161  UNP    P30044   AOPP_HUMAN      54    214             
DBREF  1H4O H    1   161  UNP    P30044   AOPP_HUMAN      54    214             
SEQADV 1H4O HIS A   88  UNP  P30044    THR    88 VARIANT                        
SEQADV 1H4O HIS B   88  UNP  P30044    THR    88 VARIANT                        
SEQADV 1H4O HIS C   88  UNP  P30044    THR    88 VARIANT                        
SEQADV 1H4O HIS D   88  UNP  P30044    THR    88 VARIANT                        
SEQADV 1H4O HIS E   88  UNP  P30044    THR    88 VARIANT                        
SEQADV 1H4O HIS F   88  UNP  P30044    THR    88 VARIANT                        
SEQADV 1H4O HIS G   88  UNP  P30044    THR    88 VARIANT                        
SEQADV 1H4O HIS H   88  UNP  P30044    THR    88 VARIANT                        
SEQRES   1 A  161  ALA PRO ILE LYS VAL GLY ASP ALA ILE PRO ALA VAL GLU          
SEQRES   2 A  161  VAL PHE GLU GLY GLU PRO GLY ASN LYS VAL ASN LEU ALA          
SEQRES   3 A  161  GLU LEU PHE LYS GLY LYS LYS GLY VAL LEU PHE GLY VAL          
SEQRES   4 A  161  PRO GLY ALA PHE THR PRO GLY CYS SER LYS THR HIS LEU          
SEQRES   5 A  161  PRO GLY PHE VAL GLU GLN ALA GLU ALA LEU LYS ALA LYS          
SEQRES   6 A  161  GLY VAL GLN VAL VAL ALA CYS LEU SER VAL ASN ASP ALA          
SEQRES   7 A  161  PHE VAL THR GLY GLU TRP GLY ARG ALA HIS LYS ALA GLU          
SEQRES   8 A  161  GLY LYS VAL ARG LEU LEU ALA ASP PRO THR GLY ALA PHE          
SEQRES   9 A  161  GLY LYS GLU THR ASP LEU LEU LEU ASP ASP SER LEU VAL          
SEQRES  10 A  161  SER ILE PHE GLY ASN ARG ARG LEU LYS ARG PHE SER MET          
SEQRES  11 A  161  VAL VAL GLN ASP GLY ILE VAL LYS ALA LEU ASN VAL GLU          
SEQRES  12 A  161  PRO ASP GLY THR GLY LEU THR CYS SER LEU ALA PRO ASN          
SEQRES  13 A  161  ILE ILE SER GLN LEU                                          
SEQRES   1 B  161  ALA PRO ILE LYS VAL GLY ASP ALA ILE PRO ALA VAL GLU          
SEQRES   2 B  161  VAL PHE GLU GLY GLU PRO GLY ASN LYS VAL ASN LEU ALA          
SEQRES   3 B  161  GLU LEU PHE LYS GLY LYS LYS GLY VAL LEU PHE GLY VAL          
SEQRES   4 B  161  PRO GLY ALA PHE THR PRO GLY CYS SER LYS THR HIS LEU          
SEQRES   5 B  161  PRO GLY PHE VAL GLU GLN ALA GLU ALA LEU LYS ALA LYS          
SEQRES   6 B  161  GLY VAL GLN VAL VAL ALA CYS LEU SER VAL ASN ASP ALA          
SEQRES   7 B  161  PHE VAL THR GLY GLU TRP GLY ARG ALA HIS LYS ALA GLU          
SEQRES   8 B  161  GLY LYS VAL ARG LEU LEU ALA ASP PRO THR GLY ALA PHE          
SEQRES   9 B  161  GLY LYS GLU THR ASP LEU LEU LEU ASP ASP SER LEU VAL          
SEQRES  10 B  161  SER ILE PHE GLY ASN ARG ARG LEU LYS ARG PHE SER MET          
SEQRES  11 B  161  VAL VAL GLN ASP GLY ILE VAL LYS ALA LEU ASN VAL GLU          
SEQRES  12 B  161  PRO ASP GLY THR GLY LEU THR CYS SER LEU ALA PRO ASN          
SEQRES  13 B  161  ILE ILE SER GLN LEU                                          
SEQRES   1 C  161  ALA PRO ILE LYS VAL GLY ASP ALA ILE PRO ALA VAL GLU          
SEQRES   2 C  161  VAL PHE GLU GLY GLU PRO GLY ASN LYS VAL ASN LEU ALA          
SEQRES   3 C  161  GLU LEU PHE LYS GLY LYS LYS GLY VAL LEU PHE GLY VAL          
SEQRES   4 C  161  PRO GLY ALA PHE THR PRO GLY CYS SER LYS THR HIS LEU          
SEQRES   5 C  161  PRO GLY PHE VAL GLU GLN ALA GLU ALA LEU LYS ALA LYS          
SEQRES   6 C  161  GLY VAL GLN VAL VAL ALA CYS LEU SER VAL ASN ASP ALA          
SEQRES   7 C  161  PHE VAL THR GLY GLU TRP GLY ARG ALA HIS LYS ALA GLU          
SEQRES   8 C  161  GLY LYS VAL ARG LEU LEU ALA ASP PRO THR GLY ALA PHE          
SEQRES   9 C  161  GLY LYS GLU THR ASP LEU LEU LEU ASP ASP SER LEU VAL          
SEQRES  10 C  161  SER ILE PHE GLY ASN ARG ARG LEU LYS ARG PHE SER MET          
SEQRES  11 C  161  VAL VAL GLN ASP GLY ILE VAL LYS ALA LEU ASN VAL GLU          
SEQRES  12 C  161  PRO ASP GLY THR GLY LEU THR CYS SER LEU ALA PRO ASN          
SEQRES  13 C  161  ILE ILE SER GLN LEU                                          
SEQRES   1 D  161  ALA PRO ILE LYS VAL GLY ASP ALA ILE PRO ALA VAL GLU          
SEQRES   2 D  161  VAL PHE GLU GLY GLU PRO GLY ASN LYS VAL ASN LEU ALA          
SEQRES   3 D  161  GLU LEU PHE LYS GLY LYS LYS GLY VAL LEU PHE GLY VAL          
SEQRES   4 D  161  PRO GLY ALA PHE THR PRO GLY CYS SER LYS THR HIS LEU          
SEQRES   5 D  161  PRO GLY PHE VAL GLU GLN ALA GLU ALA LEU LYS ALA LYS          
SEQRES   6 D  161  GLY VAL GLN VAL VAL ALA CYS LEU SER VAL ASN ASP ALA          
SEQRES   7 D  161  PHE VAL THR GLY GLU TRP GLY ARG ALA HIS LYS ALA GLU          
SEQRES   8 D  161  GLY LYS VAL ARG LEU LEU ALA ASP PRO THR GLY ALA PHE          
SEQRES   9 D  161  GLY LYS GLU THR ASP LEU LEU LEU ASP ASP SER LEU VAL          
SEQRES  10 D  161  SER ILE PHE GLY ASN ARG ARG LEU LYS ARG PHE SER MET          
SEQRES  11 D  161  VAL VAL GLN ASP GLY ILE VAL LYS ALA LEU ASN VAL GLU          
SEQRES  12 D  161  PRO ASP GLY THR GLY LEU THR CYS SER LEU ALA PRO ASN          
SEQRES  13 D  161  ILE ILE SER GLN LEU                                          
SEQRES   1 E  161  ALA PRO ILE LYS VAL GLY ASP ALA ILE PRO ALA VAL GLU          
SEQRES   2 E  161  VAL PHE GLU GLY GLU PRO GLY ASN LYS VAL ASN LEU ALA          
SEQRES   3 E  161  GLU LEU PHE LYS GLY LYS LYS GLY VAL LEU PHE GLY VAL          
SEQRES   4 E  161  PRO GLY ALA PHE THR PRO GLY CYS SER LYS THR HIS LEU          
SEQRES   5 E  161  PRO GLY PHE VAL GLU GLN ALA GLU ALA LEU LYS ALA LYS          
SEQRES   6 E  161  GLY VAL GLN VAL VAL ALA CYS LEU SER VAL ASN ASP ALA          
SEQRES   7 E  161  PHE VAL THR GLY GLU TRP GLY ARG ALA HIS LYS ALA GLU          
SEQRES   8 E  161  GLY LYS VAL ARG LEU LEU ALA ASP PRO THR GLY ALA PHE          
SEQRES   9 E  161  GLY LYS GLU THR ASP LEU LEU LEU ASP ASP SER LEU VAL          
SEQRES  10 E  161  SER ILE PHE GLY ASN ARG ARG LEU LYS ARG PHE SER MET          
SEQRES  11 E  161  VAL VAL GLN ASP GLY ILE VAL LYS ALA LEU ASN VAL GLU          
SEQRES  12 E  161  PRO ASP GLY THR GLY LEU THR CYS SER LEU ALA PRO ASN          
SEQRES  13 E  161  ILE ILE SER GLN LEU                                          
SEQRES   1 F  161  ALA PRO ILE LYS VAL GLY ASP ALA ILE PRO ALA VAL GLU          
SEQRES   2 F  161  VAL PHE GLU GLY GLU PRO GLY ASN LYS VAL ASN LEU ALA          
SEQRES   3 F  161  GLU LEU PHE LYS GLY LYS LYS GLY VAL LEU PHE GLY VAL          
SEQRES   4 F  161  PRO GLY ALA PHE THR PRO GLY CYS SER LYS THR HIS LEU          
SEQRES   5 F  161  PRO GLY PHE VAL GLU GLN ALA GLU ALA LEU LYS ALA LYS          
SEQRES   6 F  161  GLY VAL GLN VAL VAL ALA CYS LEU SER VAL ASN ASP ALA          
SEQRES   7 F  161  PHE VAL THR GLY GLU TRP GLY ARG ALA HIS LYS ALA GLU          
SEQRES   8 F  161  GLY LYS VAL ARG LEU LEU ALA ASP PRO THR GLY ALA PHE          
SEQRES   9 F  161  GLY LYS GLU THR ASP LEU LEU LEU ASP ASP SER LEU VAL          
SEQRES  10 F  161  SER ILE PHE GLY ASN ARG ARG LEU LYS ARG PHE SER MET          
SEQRES  11 F  161  VAL VAL GLN ASP GLY ILE VAL LYS ALA LEU ASN VAL GLU          
SEQRES  12 F  161  PRO ASP GLY THR GLY LEU THR CYS SER LEU ALA PRO ASN          
SEQRES  13 F  161  ILE ILE SER GLN LEU                                          
SEQRES   1 G  161  ALA PRO ILE LYS VAL GLY ASP ALA ILE PRO ALA VAL GLU          
SEQRES   2 G  161  VAL PHE GLU GLY GLU PRO GLY ASN LYS VAL ASN LEU ALA          
SEQRES   3 G  161  GLU LEU PHE LYS GLY LYS LYS GLY VAL LEU PHE GLY VAL          
SEQRES   4 G  161  PRO GLY ALA PHE THR PRO GLY CYS SER LYS THR HIS LEU          
SEQRES   5 G  161  PRO GLY PHE VAL GLU GLN ALA GLU ALA LEU LYS ALA LYS          
SEQRES   6 G  161  GLY VAL GLN VAL VAL ALA CYS LEU SER VAL ASN ASP ALA          
SEQRES   7 G  161  PHE VAL THR GLY GLU TRP GLY ARG ALA HIS LYS ALA GLU          
SEQRES   8 G  161  GLY LYS VAL ARG LEU LEU ALA ASP PRO THR GLY ALA PHE          
SEQRES   9 G  161  GLY LYS GLU THR ASP LEU LEU LEU ASP ASP SER LEU VAL          
SEQRES  10 G  161  SER ILE PHE GLY ASN ARG ARG LEU LYS ARG PHE SER MET          
SEQRES  11 G  161  VAL VAL GLN ASP GLY ILE VAL LYS ALA LEU ASN VAL GLU          
SEQRES  12 G  161  PRO ASP GLY THR GLY LEU THR CYS SER LEU ALA PRO ASN          
SEQRES  13 G  161  ILE ILE SER GLN LEU                                          
SEQRES   1 H  161  ALA PRO ILE LYS VAL GLY ASP ALA ILE PRO ALA VAL GLU          
SEQRES   2 H  161  VAL PHE GLU GLY GLU PRO GLY ASN LYS VAL ASN LEU ALA          
SEQRES   3 H  161  GLU LEU PHE LYS GLY LYS LYS GLY VAL LEU PHE GLY VAL          
SEQRES   4 H  161  PRO GLY ALA PHE THR PRO GLY CYS SER LYS THR HIS LEU          
SEQRES   5 H  161  PRO GLY PHE VAL GLU GLN ALA GLU ALA LEU LYS ALA LYS          
SEQRES   6 H  161  GLY VAL GLN VAL VAL ALA CYS LEU SER VAL ASN ASP ALA          
SEQRES   7 H  161  PHE VAL THR GLY GLU TRP GLY ARG ALA HIS LYS ALA GLU          
SEQRES   8 H  161  GLY LYS VAL ARG LEU LEU ALA ASP PRO THR GLY ALA PHE          
SEQRES   9 H  161  GLY LYS GLU THR ASP LEU LEU LEU ASP ASP SER LEU VAL          
SEQRES  10 H  161  SER ILE PHE GLY ASN ARG ARG LEU LYS ARG PHE SER MET          
SEQRES  11 H  161  VAL VAL GLN ASP GLY ILE VAL LYS ALA LEU ASN VAL GLU          
SEQRES  12 H  161  PRO ASP GLY THR GLY LEU THR CYS SER LEU ALA PRO ASN          
SEQRES  13 H  161  ILE ILE SER GLN LEU                                          
HET    BEZ  A1162       9                                                       
HET    BEZ  B1162       9                                                       
HET    BEZ  C1162       9                                                       
HET    BEZ  D1162       9                                                       
HET    BEZ  E1162       9                                                       
HET    BEZ  F1162       9                                                       
HET    BEZ  G1162       9                                                       
HET    BEZ  H1162       9                                                       
HETNAM     BEZ BENZOIC ACID                                                     
FORMUL   9  BEZ    8(C7 H6 O2)                                                  
FORMUL  17  HOH   *1213(H2 O)                                                   
HELIX    1  A1 LEU A   25  PHE A   29  1                                   5    
HELIX    2  A2 THR A   44  ALA A   64  1                                  21    
HELIX    3  A3 ASP A   77  HIS A   88  1                                  12    
HELIX    4  A4 GLY A  102  ASP A  109  1                                   8    
HELIX    5  A5 LEU A  116  GLY A  121  1                                   6    
HELIX    6  A6 LEU A  153  SER A  159  1                                   7    
HELIX    7  B1 LEU B   25  PHE B   29  1                                   5    
HELIX    8  B2 THR B   44  ALA B   64  1                                  21    
HELIX    9  B3 ASP B   77  HIS B   88  1                                  12    
HELIX   10  B4 GLY B  102  ASP B  109  1                                   8    
HELIX   11  B5 LEU B  116  GLY B  121  1                                   6    
HELIX   12  B6 LEU B  153  LEU B  161  1                                   9    
HELIX   13  C1 LEU C   25  PHE C   29  1                                   5    
HELIX   14  C2 THR C   44  ALA C   64  1                                  21    
HELIX   15  C3 ASP C   77  HIS C   88  1                                  12    
HELIX   16  C4 GLY C  102  ASP C  109  1                                   8    
HELIX   17  C5 LEU C  116  GLY C  121  1                                   6    
HELIX   18  C6 LEU C  153  LEU C  161  1                                   9    
HELIX   19  D1 LEU D   25  PHE D   29  1                                   5    
HELIX   20  D2 THR D   44  ALA D   64  1                                  21    
HELIX   21  D3 ASP D   77  HIS D   88  1                                  12    
HELIX   22  D4 GLY D  102  ASP D  109  1                                   8    
HELIX   23  D5 LEU D  116  GLY D  121  1                                   6    
HELIX   24  D6 LEU D  153  LEU D  161  1                                   9    
HELIX   25  E1 LEU E   25  PHE E   29  1                                   5    
HELIX   26  E2 THR E   44  ALA E   64  1                                  21    
HELIX   27  E3 ASP E   77  HIS E   88  1                                  12    
HELIX   28  E4 GLY E  102  ASP E  109  1                                   8    
HELIX   29  E5 LEU E  116  GLY E  121  1                                   6    
HELIX   30  E6 LEU E  153  GLN E  160  1                                   8    
HELIX   31  F1 LEU F   25  PHE F   29  1                                   5    
HELIX   32  F2 THR F   44  ALA F   64  1                                  21    
HELIX   33  F3 ASP F   77  HIS F   88  1                                  12    
HELIX   34  F4 GLY F  102  ASP F  109  1                                   8    
HELIX   35  F5 LEU F  116  GLY F  121  1                                   6    
HELIX   36  F6 LEU F  153  LEU F  161  1                                   9    
HELIX   37  G1 LEU G   25  LYS G   30  1                                   6    
HELIX   38  G2 THR G   44  ALA G   64  1                                  21    
HELIX   39  G3 ASP G   77  HIS G   88  1                                  12    
HELIX   40  G4 GLY G  102  ASP G  109  1                                   8    
HELIX   41  G5 LEU G  116  GLY G  121  1                                   6    
HELIX   42  G6 LEU G  153  LEU G  161  1                                   9    
HELIX   43  H1 LEU H   25  PHE H   29  1                                   5    
HELIX   44  H2 THR H   44  ALA H   64  1                                  21    
HELIX   45  H3 ASP H   77  HIS H   88  1                                  12    
HELIX   46  H4 GLY H  102  ASP H  109  1                                   8    
HELIX   47  H5 LEU H  116  GLY H  121  1                                   6    
HELIX   48  H6 LEU H  153  LEU H  161  1                                   9    
SHEET    1  AA 2 VAL A  12  GLU A  16  0                                        
SHEET    2  AA 2 ASN A  21  ASN A  24 -1  N  VAL A  23   O  VAL A  14           
SHEET    1  AB 5 ARG A  95  ASP A  99  0                                        
SHEET    2  AB 5 VAL A  69  SER A  74  1  O  CYS A  72   N  LEU A  97           
SHEET    3  AB 5 LYS A  32  VAL A  39  1  O  VAL A  35   N  ALA A  71           
SHEET    4  AB 5 ARG A 127  ASP A 134 -1  N  MET A 130   O  LEU A  36           
SHEET    5  AB 5 ILE A 136  GLU A 143 -1  O  ASN A 141   N  SER A 129           
SHEET    1  BA 2 VAL B  12  GLU B  16  0                                        
SHEET    2  BA 2 ASN B  21  ASN B  24 -1  N  VAL B  23   O  VAL B  14           
SHEET    1  BB 5 ARG B  95  ASP B  99  0                                        
SHEET    2  BB 5 VAL B  69  SER B  74  1  O  CYS B  72   N  LEU B  97           
SHEET    3  BB 5 LYS B  32  VAL B  39  1  O  VAL B  35   N  ALA B  71           
SHEET    4  BB 5 ARG B 127  ASP B 134 -1  N  MET B 130   O  LEU B  36           
SHEET    5  BB 5 ILE B 136  GLU B 143 -1  O  ASN B 141   N  SER B 129           
SHEET    1  CA 2 VAL C  12  GLU C  16  0                                        
SHEET    2  CA 2 ASN C  21  ASN C  24 -1  N  VAL C  23   O  VAL C  14           
SHEET    1  CB 5 ARG C  95  ASP C  99  0                                        
SHEET    2  CB 5 VAL C  69  SER C  74  1  O  CYS C  72   N  LEU C  97           
SHEET    3  CB 5 LYS C  32  VAL C  39  1  O  VAL C  35   N  ALA C  71           
SHEET    4  CB 5 ARG C 127  ASP C 134 -1  N  MET C 130   O  LEU C  36           
SHEET    5  CB 5 ILE C 136  GLU C 143 -1  O  ASN C 141   N  SER C 129           
SHEET    1  DA 2 VAL D  12  GLU D  16  0                                        
SHEET    2  DA 2 ASN D  21  ASN D  24 -1  N  VAL D  23   O  VAL D  14           
SHEET    1  DB 5 ARG D  95  ASP D  99  0                                        
SHEET    2  DB 5 VAL D  69  SER D  74  1  O  CYS D  72   N  LEU D  97           
SHEET    3  DB 5 LYS D  32  VAL D  39  1  O  VAL D  35   N  ALA D  71           
SHEET    4  DB 5 ARG D 127  ASP D 134 -1  N  MET D 130   O  LEU D  36           
SHEET    5  DB 5 ILE D 136  GLU D 143 -1  O  ASN D 141   N  SER D 129           
SHEET    1  EA 2 VAL E  12  GLU E  16  0                                        
SHEET    2  EA 2 ASN E  21  ASN E  24 -1  N  VAL E  23   O  VAL E  14           
SHEET    1  EB 5 ARG E  95  ASP E  99  0                                        
SHEET    2  EB 5 VAL E  69  SER E  74  1  O  CYS E  72   N  LEU E  97           
SHEET    3  EB 5 LYS E  32  VAL E  39  1  O  VAL E  35   N  ALA E  71           
SHEET    4  EB 5 ARG E 127  ASP E 134 -1  N  MET E 130   O  LEU E  36           
SHEET    5  EB 5 ILE E 136  GLU E 143 -1  O  ASN E 141   N  SER E 129           
SHEET    1  FA 2 VAL F  12  GLU F  16  0                                        
SHEET    2  FA 2 ASN F  21  ASN F  24 -1  N  VAL F  23   O  VAL F  14           
SHEET    1  FB 5 ARG F  95  ASP F  99  0                                        
SHEET    2  FB 5 VAL F  69  SER F  74  1  O  CYS F  72   N  LEU F  97           
SHEET    3  FB 5 LYS F  32  VAL F  39  1  O  VAL F  35   N  ALA F  71           
SHEET    4  FB 5 ARG F 127  ASP F 134 -1  N  MET F 130   O  LEU F  36           
SHEET    5  FB 5 ILE F 136  GLU F 143 -1  O  ASN F 141   N  SER F 129           
SHEET    1  GA 2 VAL G  12  GLU G  16  0                                        
SHEET    2  GA 2 ASN G  21  ASN G  24 -1  N  VAL G  23   O  VAL G  14           
SHEET    1  GB 5 ARG G  95  ASP G  99  0                                        
SHEET    2  GB 5 VAL G  69  SER G  74  1  O  CYS G  72   N  LEU G  97           
SHEET    3  GB 5 LYS G  32  VAL G  39  1  O  VAL G  35   N  ALA G  71           
SHEET    4  GB 5 ARG G 127  ASP G 134 -1  N  MET G 130   O  LEU G  36           
SHEET    5  GB 5 ILE G 136  GLU G 143 -1  O  ASN G 141   N  SER G 129           
SHEET    1  HA 2 VAL H  12  GLU H  16  0                                        
SHEET    2  HA 2 ASN H  21  ASN H  24 -1  N  VAL H  23   O  VAL H  14           
SHEET    1  HB 5 ARG H  95  ASP H  99  0                                        
SHEET    2  HB 5 VAL H  69  SER H  74  1  O  CYS H  72   N  LEU H  97           
SHEET    3  HB 5 LYS H  32  VAL H  39  1  O  VAL H  35   N  ALA H  71           
SHEET    4  HB 5 ARG H 127  ASP H 134 -1  N  MET H 130   O  LEU H  36           
SHEET    5  HB 5 ILE H 136  GLU H 143 -1  O  ASN H 141   N  SER H 129           
SITE     1 AC1  7 PRO A  40  THR A  44  PRO A  45  GLY A  46                    
SITE     2 AC1  7 CYS A  47  ARG A 127  ALA B  64                               
SITE     1 AC2  8 PRO B  40  THR B  44  PRO B  45  GLY B  46                    
SITE     2 AC2  8 CYS B  47  ARG B 127  ALA C  64  HOH C2092                    
SITE     1 AC3  9 THR C  44  PRO C  45  GLY C  46  CYS C  47                    
SITE     2 AC3  9 ARG C 127  HOH C2188  LYS D  63  ALA D  64                    
SITE     3 AC3  9 GLY D  66                                                     
SITE     1 AC4  9 PRO D  40  THR D  44  PRO D  45  GLY D  46                    
SITE     2 AC4  9 CYS D  47  ARG D 127  HOH D2184  ALA E  64                    
SITE     3 AC4  9 GLY E  66                                                     
SITE     1 AC5  9 THR E  44  PRO E  45  GLY E  46  CYS E  47                    
SITE     2 AC5  9 ARG E 127  HOH E2128  LYS F  63  ALA F  64                    
SITE     3 AC5  9 GLY F  66                                                     
SITE     1 AC6  9 THR F  44  PRO F  45  GLY F  46  CYS F  47                    
SITE     2 AC6  9 ARG F 127  HOH F2160  LYS G  63  ALA G  64                    
SITE     3 AC6  9 GLY G  66                                                     
SITE     1 AC7  8 THR G  44  PRO G  45  GLY G  46  CYS G  47                    
SITE     2 AC7  8 PHE G 120  ARG G 127  HOH G2139  ALA H  64                    
SITE     1 AC8  8 ALA A  64  HOH A2090  PRO H  40  THR H  44                    
SITE     2 AC8  8 PRO H  45  GLY H  46  CYS H  47  ARG H 127                    
CRYST1  130.790   66.490  141.240  90.00 117.54  90.00 P 1 21 1     16          
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      0.007646  0.000000  0.003987        0.00000                         
SCALE2      0.000000  0.015040  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007985        0.00000                         
MTRIX1   1 -0.270446 -0.953291  0.134518      -31.45600    1                    
MTRIX2   1  0.950263 -0.286741 -0.121570        4.38000    1                    
MTRIX3   1  0.154464  0.094949  0.983425      -28.61000    1                    
MTRIX1   2 -0.985374  0.163467  0.048136      -29.80000    1                    
MTRIX2   2 -0.161289 -0.985829  0.046121       27.76400    1                    
MTRIX3   2  0.054993  0.037683  0.997775      -63.28900    1                    
MTRIX1   3  0.100545  0.992969 -0.062480       -6.78300    1                    
MTRIX2   3 -0.993238  0.103839  0.051920       26.29100    1                    
MTRIX3   3  0.058042  0.056838  0.996695      -95.79400    1                    
MTRIX1   4  0.986253 -0.142584 -0.083513      -62.01200    1                    
MTRIX2   4  0.138721  0.989048 -0.050397       13.21300    1                    
MTRIX3   4  0.089784  0.038120  0.995232        4.17800    1                    
MTRIX1   5 -0.097589 -0.994769  0.030188      -21.28400    1                    
MTRIX2   5  0.993386 -0.099208 -0.057815       64.63500    1                    
MTRIX3   5  0.060508  0.024346  0.997871      -32.17800    1                    
MTRIX1   6 -0.999018 -0.010470  0.043054       30.05000    1                    
MTRIX2   6  0.010323 -0.999940 -0.003643       27.22600    1                    
MTRIX3   6  0.043089 -0.003195  0.999066      -63.80200    1                    
MTRIX1   7  0.256840  0.961914 -0.093568      -23.77700    1                    
MTRIX2   7 -0.954999  0.267466  0.128215      -38.25700    1                    
MTRIX3   7  0.148358  0.056427  0.987323      -90.62500    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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