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Database: PDB
Entry: 2FIY
LinkDB: 2FIY
Original site: 2FIY 
HEADER    STRUCTURAL GENOMICS, UNKNOWN FUNCTION   30-DEC-05   2FIY              
TITLE     THE CRYSTAL STRUCTURE OF THE FDHE PROTEIN FROM PSEUDOMONAS AERUGINOSA 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN FDHE HOMOLOG;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 208964;                                              
SOURCE   4 STRAIN: PAO1;                                                        
SOURCE   5 GENE: FDHE GI:9951077;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    FDHE PROTEIN, PSEUDOMONAS AERUGINOSA, STRUCTURAL GENOMICS, PSI,       
KEYWDS   2 PROTEIN STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL          
KEYWDS   3 GENOMICS, MCSG, UNKNOWN FUNCTION                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.ZHANG,E.EVDOKIMOVA,A.SAVCHENKO,A.EDWARDS,A.JOACHIMIAK,MIDWEST       
AUTHOR   2 CENTER FOR STRUCTURAL GENOMICS (MCSG)                                
REVDAT   3   13-JUL-11 2FIY    1       VERSN                                    
REVDAT   2   24-FEB-09 2FIY    1       VERSN                                    
REVDAT   1   14-FEB-06 2FIY    0                                                
JRNL        AUTH   R.ZHANG,E.EVDOKIMOVA,A.SAVCHENKO,A.EDWARDS,A.JOACHIMIAK      
JRNL        TITL   THE CRYSTAL STRUCTURE OF THE FDHE PROTEIN FROM PSEUDOMONAS   
JRNL        TITL 2 AERUGINOSA PAO1                                              
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 96.67                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 35601                          
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) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1890                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.16                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2497                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.72                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2080                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 128                          
REMARK   3   BIN FREE R VALUE                    : 0.2830                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4364                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 369                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 35.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.99                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.45000                                             
REMARK   3    B22 (A**2) : -0.32000                                             
REMARK   3    B33 (A**2) : 0.77000                                              
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): 0.225         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.189         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.140         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.745         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4470 ; 0.010 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  4170 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6072 ; 1.407 ; 1.988       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9643 ; 0.880 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   558 ; 6.604 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   195 ;36.561 ;22.667       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   710 ;16.758 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    42 ;16.219 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   660 ; 0.083 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4977 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   905 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1025 ; 0.200 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4176 ; 0.189 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2073 ; 0.171 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2634 ; 0.086 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   306 ; 0.188 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    36 ; 0.235 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):   118 ; 0.240 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    27 ; 0.183 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3620 ; 0.931 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1135 ; 0.125 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4452 ; 1.051 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1912 ; 1.467 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1620 ; 2.128 ; 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 : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    19        A    78                          
REMARK   3    RESIDUE RANGE :   A    79        A   180                          
REMARK   3    RESIDUE RANGE :   A   181        A   250                          
REMARK   3    RESIDUE RANGE :   A   251        A   307                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.2050  96.4260  51.6310              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0624 T22:  -0.1297                                     
REMARK   3      T33:  -0.1193 T12:   0.0152                                     
REMARK   3      T13:   0.0489 T23:   0.0306                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5549 L22:   2.4971                                     
REMARK   3      L33:   1.7231 L12:  -0.0422                                     
REMARK   3      L13:  -0.1417 L23:   0.1655                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0961 S12:   0.0538 S13:   0.1357                       
REMARK   3      S21:  -0.0150 S22:  -0.0233 S23:  -0.2280                       
REMARK   3      S31:  -0.2212 S32:  -0.0217 S33:  -0.0728                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    18        B    78                          
REMARK   3    RESIDUE RANGE :   B    79        B   182                          
REMARK   3    RESIDUE RANGE :   B   183        B   250                          
REMARK   3    RESIDUE RANGE :   B   251        B   308                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.6720  47.4860  52.9300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0785 T22:  -0.1808                                     
REMARK   3      T33:  -0.1913 T12:   0.0408                                     
REMARK   3      T13:  -0.0357 T23:   0.0047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3079 L22:   3.1053                                     
REMARK   3      L33:   2.8972 L12:   0.4225                                     
REMARK   3      L13:  -0.2393 L23:   0.4154                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0353 S12:   0.0295 S13:  -0.2351                       
REMARK   3      S21:   0.1703 S22:   0.0320 S23:   0.1140                       
REMARK   3      S31:   0.0657 S32:   0.0681 S33:   0.0033                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 2FIY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB035930.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUL-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9798                             
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SBCCOLLECT                         
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35601                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 97.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 8.700                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 33.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M (NH4)2SO4, 0.1M TRIS PH8.5, 25%    
REMARK 280  P 5K MME, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 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                                                                      
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       70.31000            
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       70.31000            
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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     ILE A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     GLN A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     GLN A    10                                                      
REMARK 465     ILE A    11                                                      
REMARK 465     GLU A    12                                                      
REMARK 465     ALA A    13                                                      
REMARK 465     ALA A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     ASN A    16                                                      
REMARK 465     ILE A    17                                                      
REMARK 465     PRO A    18                                                      
REMARK 465     GLY A   200                                                      
REMARK 465     GLY A   201                                                      
REMARK 465     LYS A   202                                                      
REMARK 465     GLU A   203                                                      
REMARK 465     ASP A   242                                                      
REMARK 465     GLU A   309                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     THR B     4                                                      
REMARK 465     ILE B     5                                                      
REMARK 465     LEU B     6                                                      
REMARK 465     GLN B     7                                                      
REMARK 465     PRO B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     GLN B    10                                                      
REMARK 465     ILE B    11                                                      
REMARK 465     GLU B    12                                                      
REMARK 465     ALA B    13                                                      
REMARK 465     ALA B    14                                                      
REMARK 465     ALA B    15                                                      
REMARK 465     ASN B    16                                                      
REMARK 465     ILE B    17                                                      
REMARK 465     GLU B   172                                                      
REMARK 465     GLU B   180                                                      
REMARK 465     SER B   181                                                      
REMARK 465     GLY B   200                                                      
REMARK 465     GLY B   201                                                      
REMARK 465     LYS B   202                                                      
REMARK 465     GLU B   203                                                      
REMARK 465     GLU B   240                                                      
REMARK 465     HIS B   241                                                      
REMARK 465     ASP B   242                                                      
REMARK 465     GLU B   309                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER A 231    OG                                                  
REMARK 470     GLU B 230    CG   CD   OE1  OE2                                  
REMARK 470     SER B 231    OG                                                  
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    GLU A   180     O    HOH A   422              1.93            
REMARK 500   O    HIS A   233     O    HOH A   602              2.09            
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    THR A 255   C     THR A 255   O      -0.140                       
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    ARG A 133   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    LEU A 148   CA  -  CB  -  CG  ANGL. DEV. =  15.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  89      114.06    -37.84                                   
REMARK 500    GLU A 172       52.62     70.36                                   
REMARK 500    SER A 181       59.44   -142.10                                   
REMARK 500    ILE A 223       47.80   -108.99                                   
REMARK 500    HIS A 227      -77.69   -108.69                                   
REMARK 500    HIS A 233       97.80    -41.74                                   
REMARK 500    ASP A 271      105.16   -161.17                                   
REMARK 500    ALA B  89      112.09    -35.69                                   
REMARK 500    ALA B 114      -87.53    -72.84                                   
REMARK 500    ILE B 223       57.10   -109.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU A  171     GLU A  172                   48.14                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    THR A 255         10.02                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE A 401  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 185   SG                                                     
REMARK 620 2 CYS A 211   SG  109.1                                              
REMARK 620 3 CYS A 214   SG  104.5 111.7                                        
REMARK 620 4 CYS A 188   SG  114.1  94.9 122.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B 402  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 185   SG                                                     
REMARK 620 2 CYS B 188   SG  115.7                                              
REMARK 620 3 CYS B 211   SG  107.8  93.6                                        
REMARK 620 4 CYS B 214   SG  106.5 121.8 110.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE A 403  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 259   SG                                                     
REMARK 620 2 CYS A 225   SG  102.7                                              
REMARK 620 3 CYS A 256   SG  112.2 104.8                                        
REMARK 620 4 CYS A 228   SG  123.9 104.2 107.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B 404  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 228   SG                                                     
REMARK 620 2 CYS B 259   SG   64.1                                              
REMARK 620 3 CYS B 256   SG  118.2 116.9                                        
REMARK 620 4 CYS B 225   SG  127.8 100.9 113.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B 405  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  20   NE2                                                    
REMARK 620 2 HIS B  22   NE2 105.6                                              
REMARK 620 3 HIS B 219   NE2 118.1 113.0                                        
REMARK 620 4 GLU B 173   OE1 100.1 130.9  89.4                                  
REMARK 620 5 GLU B 173   OE2 129.8  82.1 102.6  49.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 405                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: APC5764   RELATED DB: TARGETDB                           
DBREF  2FIY A    1   309  UNP    Q9HV00   FDHE_PSEAE       1    309             
DBREF  2FIY B    1   309  UNP    Q9HV00   FDHE_PSEAE       1    309             
SEQRES   1 A  309  MET SER ARG THR ILE LEU GLN PRO GLY GLN ILE GLU ALA          
SEQRES   2 A  309  ALA ALA ASN ILE PRO PRO HIS LEU HIS GLN PRO SER ARG          
SEQRES   3 A  309  ASP LEU PHE ALA ARG ARG GLY GLU ARG LEU LEU GLN LEU          
SEQRES   4 A  309  ALA GLU GLY HIS PRO MET GLY ASP TYR LEU ARG LEU VAL          
SEQRES   5 A  309  ALA GLY LEU CYS ARG LEU GLN GLN ALA LEU LEU ASP ASN          
SEQRES   6 A  309  PRO PRO ALA LEU ALA PRO LEU ASP PRO GLU ARG LEU ARG          
SEQRES   7 A  309  LYS SER ARG GLU HIS GLY MET PRO PRO LEU ALA TYR ASP          
SEQRES   8 A  309  LEU LEU VAL ARG GLU GLY ALA TRP LEU PRO TRP LEU ASP          
SEQRES   9 A  309  ALA LEU LEU ALA GLY TYR PRO ALA PRO ALA ASN ALA ALA          
SEQRES  10 A  309  VAL GLY ALA ALA LEU GLU GLN LEU ARG GLU ALA GLU GLU          
SEQRES  11 A  309  GLY GLN ARG LYS ALA TRP ALA ILE ALA LEU LEU SER GLY          
SEQRES  12 A  309  GLN PHE ASP LEU LEU PRO ALA ALA LEU VAL PRO PHE LEU          
SEQRES  13 A  309  GLY ALA ALA LEU GLN VAL ALA TRP SER HIS TRP LEU LEU          
SEQRES  14 A  309  GLY LEU GLU GLU GLY ALA VAL VAL GLU THR GLU SER ARG          
SEQRES  15 A  309  THR LEU CYS PRO ALA CYS GLY SER PRO PRO MET ALA GLY          
SEQRES  16 A  309  MET ILE ARG GLN GLY GLY LYS GLU THR GLY LEU ARG TYR          
SEQRES  17 A  309  LEU SER CYS SER LEU CYS ALA CYS GLU TRP HIS TYR VAL          
SEQRES  18 A  309  ARG ILE LYS CYS SER HIS CYS GLU GLU SER LYS HIS LEU          
SEQRES  19 A  309  ALA TYR LEU SER LEU GLU HIS ASP GLY GLN PRO ALA GLU          
SEQRES  20 A  309  LYS ALA VAL LEU ARG ALA GLU THR CYS PRO SER CYS GLN          
SEQRES  21 A  309  GLY TYR LEU LYS GLN PHE TYR LEU GLU PHE ASP ARG HIS          
SEQRES  22 A  309  ALA ASP ALA LEU ALA ASP ASP LEU ALA SER LEU ALA LEU          
SEQRES  23 A  309  ASP MET ARG LEU ALA GLU ASP GLY TYR LEU ARG ARG SER          
SEQRES  24 A  309  PRO ASN LEU LEU LEU ALA PRO GLY GLY GLU                      
SEQRES   1 B  309  MET SER ARG THR ILE LEU GLN PRO GLY GLN ILE GLU ALA          
SEQRES   2 B  309  ALA ALA ASN ILE PRO PRO HIS LEU HIS GLN PRO SER ARG          
SEQRES   3 B  309  ASP LEU PHE ALA ARG ARG GLY GLU ARG LEU LEU GLN LEU          
SEQRES   4 B  309  ALA GLU GLY HIS PRO MET GLY ASP TYR LEU ARG LEU VAL          
SEQRES   5 B  309  ALA GLY LEU CYS ARG LEU GLN GLN ALA LEU LEU ASP ASN          
SEQRES   6 B  309  PRO PRO ALA LEU ALA PRO LEU ASP PRO GLU ARG LEU ARG          
SEQRES   7 B  309  LYS SER ARG GLU HIS GLY MET PRO PRO LEU ALA TYR ASP          
SEQRES   8 B  309  LEU LEU VAL ARG GLU GLY ALA TRP LEU PRO TRP LEU ASP          
SEQRES   9 B  309  ALA LEU LEU ALA GLY TYR PRO ALA PRO ALA ASN ALA ALA          
SEQRES  10 B  309  VAL GLY ALA ALA LEU GLU GLN LEU ARG GLU ALA GLU GLU          
SEQRES  11 B  309  GLY GLN ARG LYS ALA TRP ALA ILE ALA LEU LEU SER GLY          
SEQRES  12 B  309  GLN PHE ASP LEU LEU PRO ALA ALA LEU VAL PRO PHE LEU          
SEQRES  13 B  309  GLY ALA ALA LEU GLN VAL ALA TRP SER HIS TRP LEU LEU          
SEQRES  14 B  309  GLY LEU GLU GLU GLY ALA VAL VAL GLU THR GLU SER ARG          
SEQRES  15 B  309  THR LEU CYS PRO ALA CYS GLY SER PRO PRO MET ALA GLY          
SEQRES  16 B  309  MET ILE ARG GLN GLY GLY LYS GLU THR GLY LEU ARG TYR          
SEQRES  17 B  309  LEU SER CYS SER LEU CYS ALA CYS GLU TRP HIS TYR VAL          
SEQRES  18 B  309  ARG ILE LYS CYS SER HIS CYS GLU GLU SER LYS HIS LEU          
SEQRES  19 B  309  ALA TYR LEU SER LEU GLU HIS ASP GLY GLN PRO ALA GLU          
SEQRES  20 B  309  LYS ALA VAL LEU ARG ALA GLU THR CYS PRO SER CYS GLN          
SEQRES  21 B  309  GLY TYR LEU LYS GLN PHE TYR LEU GLU PHE ASP ARG HIS          
SEQRES  22 B  309  ALA ASP ALA LEU ALA ASP ASP LEU ALA SER LEU ALA LEU          
SEQRES  23 B  309  ASP MET ARG LEU ALA GLU ASP GLY TYR LEU ARG ARG SER          
SEQRES  24 B  309  PRO ASN LEU LEU LEU ALA PRO GLY GLY GLU                      
HET     FE  A 401       1                                                       
HET     FE  B 402       1                                                       
HET     FE  A 403       1                                                       
HET     FE  B 404       1                                                       
HET     FE  B 405       1                                                       
HETNAM      FE FE (III) ION                                                     
FORMUL   3   FE    5(FE 3+)                                                     
FORMUL   8  HOH   *369(H2 O)                                                    
HELIX    1   1 ASP A   27  GLU A   41  1                                  15    
HELIX    2   2 MET A   45  ASP A   64  1                                  20    
HELIX    3   3 ASP A   73  HIS A   83  1                                  11    
HELIX    4   4 ALA A   89  GLY A   97  1                                   9    
HELIX    5   5 TRP A   99  GLY A  109  1                                  11    
HELIX    6   6 ASN A  115  ALA A  128  1                                  14    
HELIX    7   7 GLU A  129  SER A  142  1                                  14    
HELIX    8   8 GLN A  144  LEU A  148  5                                   5    
HELIX    9   9 PRO A  149  ALA A  151  5                                   3    
HELIX   10  10 LEU A  152  GLY A  170  1                                  19    
HELIX   11  11 ASP A  275  ALA A  282  1                                   8    
HELIX   12  12 SER A  283  ASP A  293  1                                  11    
HELIX   13  13 ASP B   27  GLU B   41  1                                  15    
HELIX   14  14 MET B   45  ASN B   65  1                                  21    
HELIX   15  15 ASP B   73  HIS B   83  1                                  11    
HELIX   16  16 ALA B   89  GLY B   97  1                                   9    
HELIX   17  17 TRP B   99  GLY B  109  1                                  11    
HELIX   18  18 ASN B  115  ALA B  128  1                                  14    
HELIX   19  19 GLU B  129  SER B  142  1                                  14    
HELIX   20  20 GLY B  143  LEU B  148  5                                   6    
HELIX   21  21 PRO B  149  ALA B  151  5                                   3    
HELIX   22  22 LEU B  152  GLY B  170  1                                  19    
HELIX   23  23 PRO B  245  ALA B  249  5                                   5    
HELIX   24  24 ASP B  275  ALA B  282  1                                   8    
HELIX   25  25 SER B  283  ASP B  293  1                                  11    
SHEET    1   A 7 LEU A  21  HIS A  22  0                                        
SHEET    2   A 7 GLU A 217  HIS A 219 -1  O  GLU A 217   N  HIS A  22           
SHEET    3   A 7 LEU A 206  CYS A 211 -1  N  LEU A 209   O  TRP A 218           
SHEET    4   A 7 PRO A 192  ARG A 198 -1  N  MET A 193   O  SER A 210           
SHEET    5   A 7 GLY A 261  TYR A 267  1  O  PHE A 266   N  ILE A 197           
SHEET    6   A 7 LEU A 251  GLU A 254 -1  N  GLU A 254   O  LEU A 263           
SHEET    7   A 7 TYR A 236  LEU A 237 -1  N  LEU A 237   O  ALA A 253           
SHEET    1   B 6 LEU A  21  HIS A  22  0                                        
SHEET    2   B 6 GLU A 217  HIS A 219 -1  O  GLU A 217   N  HIS A  22           
SHEET    3   B 6 LEU A 206  CYS A 211 -1  N  LEU A 209   O  TRP A 218           
SHEET    4   B 6 PRO A 192  ARG A 198 -1  N  MET A 193   O  SER A 210           
SHEET    5   B 6 GLY A 261  TYR A 267  1  O  PHE A 266   N  ILE A 197           
SHEET    6   B 6 LEU A 296  ARG A 297  1  O  LEU A 296   N  TYR A 262           
SHEET    1   C 6 GLU B 217  HIS B 219  0                                        
SHEET    2   C 6 LEU B 206  CYS B 211 -1  N  LEU B 209   O  TRP B 218           
SHEET    3   C 6 PRO B 192  ARG B 198 -1  N  MET B 196   O  TYR B 208           
SHEET    4   C 6 GLY B 261  TYR B 267  1  O  PHE B 266   N  ILE B 197           
SHEET    5   C 6 LEU B 251  CYS B 256 -1  N  GLU B 254   O  LEU B 263           
SHEET    6   C 6 ALA B 235  LEU B 237 -1  N  LEU B 237   O  ALA B 253           
SHEET    1   D 5 GLU B 217  HIS B 219  0                                        
SHEET    2   D 5 LEU B 206  CYS B 211 -1  N  LEU B 209   O  TRP B 218           
SHEET    3   D 5 PRO B 192  ARG B 198 -1  N  MET B 196   O  TYR B 208           
SHEET    4   D 5 GLY B 261  TYR B 267  1  O  PHE B 266   N  ILE B 197           
SHEET    5   D 5 LEU B 296  ARG B 297  1  O  LEU B 296   N  TYR B 262           
SSBOND   1 CYS B  228    CYS B  259                          1555   1555  2.08  
LINK        FE    FE A 401                 SG  CYS A 185     1555   1555  2.28  
LINK        FE    FE B 402                 SG  CYS B 185     1555   1555  2.30  
LINK        FE    FE A 403                 SG  CYS A 259     1555   1555  1.89  
LINK        FE    FE B 404                 SG  CYS B 228     1555   1555  2.13  
LINK        FE    FE B 404                 SG  CYS B 259     1555   1555  1.74  
LINK        FE    FE B 405                 NE2 HIS B  20     1555   1555  2.10  
LINK        FE    FE B 405                 NE2 HIS B  22     1555   1555  2.06  
LINK        FE    FE B 405                 NE2 HIS B 219     1555   1555  2.09  
LINK        FE    FE A 401                 SG  CYS A 211     1555   1555  2.38  
LINK        FE    FE A 401                 SG  CYS A 214     1555   1555  2.32  
LINK        FE    FE A 401                 SG  CYS A 188     1555   1555  2.35  
LINK        FE    FE A 403                 SG  CYS A 225     1555   1555  2.63  
LINK        FE    FE A 403                 SG  CYS A 256     1555   1555  2.41  
LINK        FE    FE A 403                 SG  CYS A 228     1555   1555  2.45  
LINK        FE    FE B 402                 SG  CYS B 188     1555   1555  2.39  
LINK        FE    FE B 402                 SG  CYS B 211     1555   1555  2.40  
LINK        FE    FE B 402                 SG  CYS B 214     1555   1555  2.35  
LINK        FE    FE B 404                 SG  CYS B 256     1555   1555  2.41  
LINK        FE    FE B 404                 SG  CYS B 225     1555   1555  2.41  
LINK        FE    FE B 405                 OE1 GLU B 173     1555   4566  2.73  
LINK        FE    FE B 405                 OE2 GLU B 173     1555   4566  2.40  
CISPEP   1 PRO A  306    GLY A  307          0         9.66                     
CISPEP   2 GLY A  307    GLY A  308          0        -1.04                     
CISPEP   3 PRO B  306    GLY B  307          0        -4.08                     
CISPEP   4 GLY B  307    GLY B  308          0        19.03                     
SITE     1 AC1  4 CYS A 185  CYS A 188  CYS A 211  CYS A 214                    
SITE     1 AC2  4 CYS B 185  CYS B 188  CYS B 211  CYS B 214                    
SITE     1 AC3  4 CYS A 225  CYS A 228  CYS A 256  CYS A 259                    
SITE     1 AC4  4 CYS B 225  CYS B 228  CYS B 256  CYS B 259                    
SITE     1 AC5  4 HIS B  20  HIS B  22  GLU B 173  HIS B 219                    
CRYST1   46.261   96.617  140.620  90.00  90.00  90.00 P 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.021616  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010350  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007111        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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