GenomeNet

Database: PDB
Entry: 1GN2
LinkDB: 1GN2
Original site: 1GN2 
HEADER    OXIDOREDUCTASE                          02-OCT-01   1GN2              
TITLE     S123C MUTANT OF THE IRON-SUPEROXIDE DISMUTASE FROM                    
TITLE    2 MYCOBACTERIUM TUBERCULOSIS.                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE;                                      
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 1773;                                                
SOURCE   4 EXPRESSION_SYSTEM: MYCOBACTERIUM VACCAE;                             
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 1810                                        
KEYWDS    OXIDOREDUCTASE, IRON                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.A.BUNTING,J.B.COOPER,I.J.TICKLE,D.B.YOUNG                           
REVDAT   4   24-FEB-09 1GN2    1       VERSN                                    
REVDAT   3   28-FEB-03 1GN2    1       REMARK COMPND SSBOND                     
REVDAT   2   02-JAN-02 1GN2    1       JRNL   REMARK                            
REVDAT   1   05-OCT-01 1GN2    0                                                
JRNL        AUTH   K.A.BUNTING,J.B.COOPER,I.J.TICKLE,D.B.YOUNG                  
JRNL        TITL   ENGINEERING OF AN INTERSUBUNIT DISULFIDE BRIDGE IN           
JRNL        TITL 2 THE IRON-SUPEROXIDE DISMUTASE OF MYCOBACTERIUM               
JRNL        TITL 3 TUBERCULOSIS.                                                
JRNL        REF    ARCH.BIOCHEM.BIOPHYS.         V. 397    69 2002              
JRNL        REFN                   ISSN 0003-9861                               
JRNL        PMID   11747311                                                     
JRNL        DOI    10.1006/ABBI.2001.2635                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   K.BUNTING,J.B.COOPER,M.O.BADASSO,I.J.TICKLE,                 
REMARK   1  AUTH 2 M.NEWTON,S.P.WOOD,Y.ZHANG,D.YOUNG                            
REMARK   1  TITL   ENGINEERING A CHANGE IN METAL-ION SPECIFICITY OF             
REMARK   1  TITL 2 THE IRON-DEPENDENT SUPEROXIDE DISMUTASE FROM                 
REMARK   1  TITL 3 MYCOBACTERIUM TUBERCULOSIS-- X-RAY STRUCTURE                 
REMARK   1  TITL 4 ANALYSIS OF SITE-DIRECTED MUTANTS                            
REMARK   1  REF    EUR.J.BIOCHEM.                V. 251   795 1998              
REMARK   1  REFN                   ISSN 0014-2956                               
REMARK   1  PMID   9490054                                                      
REMARK   1  DOI    10.1046/J.1432-1327.1998.2510795.X                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CCP4                                                 
REMARK   3   AUTHORS     : NULL                                                 
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21                             
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   COMPLETENESS FOR RANGE        (%) : 67.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 15192                          
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) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.249                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 750                             
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12544                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.011 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : 0.027 ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.009 ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.015 ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: INDIVIDUAL B-FACTORS NO REFINED.          
REMARK   4                                                                      
REMARK   4 1GN2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  04-OCT-01.                 
REMARK 100 THE PDBE ID CODE IS EBI-8651.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 293.0                              
REMARK 200  PH                             : 7.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : ENRAF-NONIUS FR591                 
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15208                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.400                              
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     (%) : 67.5                               
REMARK 200  DATA REDUNDANCY                : 1.700                              
REMARK 200  R MERGE                    (I) : 0.19700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 3.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 67.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CCP4                                                  
REMARK 200 STARTING MODEL: 1IDS                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 39.7                                       
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS-HCL PH 7.0,                   
REMARK 280  25% PEG 6000, PROTEIN CONCENTRATION = 3 MG/ML.                      
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       53.16500            
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                                                    
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 GENERATING THE BIOMOLECULE                                           
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 14740 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 34310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -103.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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:  2                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 14600 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 34480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -101.3 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  ENGINEERED MUTATION:                                                
REMARK 400  OTHER_DETAILS: DISULPHIDE BRIDGE BETWEEN CYS 123 OF NCS             
REMARK 400  RELATED SUBUNITS.                                                   
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     GLN A   200                                                      
REMARK 465     THR A   201                                                      
REMARK 465     LYS A   202                                                      
REMARK 465     GLY A   203                                                      
REMARK 465     LEU A   204                                                      
REMARK 465     ILE A   205                                                      
REMARK 465     PHE A   206                                                      
REMARK 465     GLY A   207                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLN B   200                                                      
REMARK 465     THR B   201                                                      
REMARK 465     LYS B   202                                                      
REMARK 465     GLY B   203                                                      
REMARK 465     LEU B   204                                                      
REMARK 465     ILE B   205                                                      
REMARK 465     PHE B   206                                                      
REMARK 465     GLY B   207                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLN C   200                                                      
REMARK 465     THR C   201                                                      
REMARK 465     LYS C   202                                                      
REMARK 465     GLY C   203                                                      
REMARK 465     LEU C   204                                                      
REMARK 465     ILE C   205                                                      
REMARK 465     PHE C   206                                                      
REMARK 465     GLY C   207                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLN D   200                                                      
REMARK 465     THR D   201                                                      
REMARK 465     LYS D   202                                                      
REMARK 465     GLY D   203                                                      
REMARK 465     LEU D   204                                                      
REMARK 465     ILE D   205                                                      
REMARK 465     PHE D   206                                                      
REMARK 465     GLY D   207                                                      
REMARK 465     MET E     1                                                      
REMARK 465     GLN E   200                                                      
REMARK 465     THR E   201                                                      
REMARK 465     LYS E   202                                                      
REMARK 465     GLY E   203                                                      
REMARK 465     LEU E   204                                                      
REMARK 465     ILE E   205                                                      
REMARK 465     PHE E   206                                                      
REMARK 465     GLY E   207                                                      
REMARK 465     MET F     1                                                      
REMARK 465     GLN F   200                                                      
REMARK 465     THR F   201                                                      
REMARK 465     LYS F   202                                                      
REMARK 465     GLY F   203                                                      
REMARK 465     LEU F   204                                                      
REMARK 465     ILE F   205                                                      
REMARK 465     PHE F   206                                                      
REMARK 465     GLY F   207                                                      
REMARK 465     MET G     1                                                      
REMARK 465     GLN G   200                                                      
REMARK 465     THR G   201                                                      
REMARK 465     LYS G   202                                                      
REMARK 465     GLY G   203                                                      
REMARK 465     LEU G   204                                                      
REMARK 465     ILE G   205                                                      
REMARK 465     PHE G   206                                                      
REMARK 465     GLY G   207                                                      
REMARK 465     MET H     1                                                      
REMARK 465     GLN H   200                                                      
REMARK 465     THR H   201                                                      
REMARK 465     LYS H   202                                                      
REMARK 465     GLY H   203                                                      
REMARK 465     LEU H   204                                                      
REMARK 465     ILE H   205                                                      
REMARK 465     PHE H   206                                                      
REMARK 465     GLY H   207                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU A    94  -  CG   GLN G    23              1.99            
REMARK 500   OE2  GLU A    94  -  NE2  GLN G    23              1.85            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500                                                                      
REMARK 500   CE   LYS A    38     OE2  GLU F    94     1455      2.16           
REMARK 500   NZ   LYS A    38     OE2  GLU F    94     1455      1.98           
REMARK 500   CA   ALA B     2     CG   ASP C   176     1545      1.96           
REMARK 500   CA   ALA B     2     OD2  ASP C   176     1545      1.72           
REMARK 500   CA   ALA B     2     OD1  ASP C   176     1545      1.89           
REMARK 500   CB   ALA B     2     CG   ASP C   176     1545      0.75           
REMARK 500   CB   ALA B     2     CB   ASP C   176     1545      2.02           
REMARK 500   CB   ALA B     2     OD2  ASP C   176     1545      0.65           
REMARK 500   CB   ALA B     2     OD1  ASP C   176     1545      1.69           
REMARK 500   CG   ASN B    86     O    ALA G    52     1544      2.11           
REMARK 500   OD1  ASN B    86     O    ALA G    52     1544      2.10           
REMARK 500   ND2  ASN B    86     O    ALA G    52     1544      1.83           
REMARK 500   C    SER C    30     OE2  GLU E    94     1556      1.69           
REMARK 500   O    SER C    30     OE2  GLU E    94     1556      0.95           
REMARK 500   O    SER C    30     CD   GLU E    94     1556      1.67           
REMARK 500   O    ALA C    52     OD2  ASP F    12     1644      2.04           
REMARK 500   CD   GLU C    54     CB   ASP F    12     1644      2.13           
REMARK 500   OE2  GLU C    54     CB   ASP F    12     1644      1.60           
REMARK 500   CB   ASP C   176     CB   ALA B     2     1555      2.02           
REMARK 500   CG   ASP C   176     CA   ALA B     2     1555      1.96           
REMARK 500   CG   ASP C   176     CB   ALA B     2     1555      0.75           
REMARK 500   OD1  ASP C   176     CA   ALA B     2     1555      1.89           
REMARK 500   OD1  ASP C   176     CB   ALA B     2     1555      1.69           
REMARK 500   OD2  ASP C   176     CA   ALA B     2     1555      1.72           
REMARK 500   OD2  ASP C   176     CB   ALA B     2     1555      0.65           
REMARK 500   CD   GLU E    94     O    SER C    30     1554      1.67           
REMARK 500   OE2  GLU E    94     C    SER C    30     1554      1.69           
REMARK 500   OE2  GLU E    94     O    SER C    30     1554      0.95           
REMARK 500   CB   ASP F    12     CD   GLU C    54     1654      2.13           
REMARK 500   CB   ASP F    12     OE2  GLU C    54     1654      1.60           
REMARK 500   OD2  ASP F    12     O    ALA C    52     1654      2.04           
REMARK 500   OE2  GLU F    94     CE   LYS A    38     1655      2.16           
REMARK 500   OE2  GLU F    94     NZ   LYS A    38     1655      1.98           
REMARK 500   O    ALA G    52     CG   ASN B    86     1554      2.11           
REMARK 500   O    ALA G    52     ND2  ASN B    86     1554      1.83           
REMARK 500   O    ALA G    52     OD1  ASN B    86     1554      2.10           
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    GLU A  54   CA  -  CB  -  CG  ANGL. DEV. =  15.8 DEGREES          
REMARK 500    CYS A 123   CA  -  CB  -  SG  ANGL. DEV. = -10.3 DEGREES          
REMARK 500    ARG A 193   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    GLU B  54   CA  -  CB  -  CG  ANGL. DEV. =  15.8 DEGREES          
REMARK 500    CYS B 123   CA  -  CB  -  SG  ANGL. DEV. = -10.3 DEGREES          
REMARK 500    ARG B 193   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    GLU C  54   CA  -  CB  -  CG  ANGL. DEV. =  15.8 DEGREES          
REMARK 500    CYS C 123   CA  -  CB  -  SG  ANGL. DEV. = -10.2 DEGREES          
REMARK 500    ARG C 193   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    GLU D  54   CA  -  CB  -  CG  ANGL. DEV. =  15.8 DEGREES          
REMARK 500    CYS D 123   CA  -  CB  -  SG  ANGL. DEV. = -10.3 DEGREES          
REMARK 500    ARG D 193   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    GLU E  54   CA  -  CB  -  CG  ANGL. DEV. =  15.8 DEGREES          
REMARK 500    CYS E 123   CA  -  CB  -  SG  ANGL. DEV. = -10.3 DEGREES          
REMARK 500    ARG E 193   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    GLU F  54   CA  -  CB  -  CG  ANGL. DEV. =  15.8 DEGREES          
REMARK 500    CYS F 123   CA  -  CB  -  SG  ANGL. DEV. = -10.3 DEGREES          
REMARK 500    ARG F 193   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    GLU G  54   CA  -  CB  -  CG  ANGL. DEV. =  15.8 DEGREES          
REMARK 500    CYS G 123   CA  -  CB  -  SG  ANGL. DEV. = -10.3 DEGREES          
REMARK 500    ARG G 193   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    GLU H  54   CA  -  CB  -  CG  ANGL. DEV. =  15.8 DEGREES          
REMARK 500    CYS H 123   CA  -  CB  -  SG  ANGL. DEV. = -10.3 DEGREES          
REMARK 500    ARG H 193   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 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 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    GLU A   3      170.28    -55.84                                   
REMARK 500    ALA A  15      -18.56    -47.54                                   
REMARK 500    HIS A  56       36.51    -96.56                                   
REMARK 500    ASP A  89     -148.14     80.46                                   
REMARK 500    ASP A 144     -111.24     62.74                                   
REMARK 500    ASN A 148       36.56     90.16                                   
REMARK 500    PHE A 166       -5.61   -161.56                                   
REMARK 500    LYS A 171     -130.69     57.80                                   
REMARK 500    GLU B   3      170.27    -55.80                                   
REMARK 500    ALA B  15      -18.51    -47.55                                   
REMARK 500    HIS B  56       36.54    -96.49                                   
REMARK 500    ASP B  89     -148.09     80.47                                   
REMARK 500    ASP B 144     -111.22     62.71                                   
REMARK 500    ASN B 148       36.49     90.14                                   
REMARK 500    PHE B 166       -5.64   -161.59                                   
REMARK 500    LYS B 171     -130.68     57.86                                   
REMARK 500    GLU C   3      170.26    -55.79                                   
REMARK 500    ALA C  15      -18.59    -47.51                                   
REMARK 500    HIS C  56       36.52    -96.55                                   
REMARK 500    ASP C  89     -148.15     80.49                                   
REMARK 500    ASP C 144     -111.23     62.74                                   
REMARK 500    ASN C 148       36.55     90.12                                   
REMARK 500    PHE C 166       -5.60   -161.57                                   
REMARK 500    LYS C 171     -130.65     57.80                                   
REMARK 500    GLU D   3      170.24    -55.79                                   
REMARK 500    ALA D  15      -18.62    -47.48                                   
REMARK 500    HIS D  56       36.52    -96.56                                   
REMARK 500    ASP D  89     -148.16     80.46                                   
REMARK 500    ASP D 144     -111.26     62.69                                   
REMARK 500    ASN D 148       36.49     90.14                                   
REMARK 500    PHE D 166       -5.63   -161.52                                   
REMARK 500    LYS D 171     -130.64     57.86                                   
REMARK 500    GLU E   3      170.27    -55.80                                   
REMARK 500    ALA E  15      -18.55    -47.53                                   
REMARK 500    HIS E  56       36.52    -96.55                                   
REMARK 500    ASP E  89     -148.16     80.51                                   
REMARK 500    ASP E 144     -111.26     62.78                                   
REMARK 500    ASN E 148       36.62     90.14                                   
REMARK 500    PHE E 166       -5.60   -161.58                                   
REMARK 500    LYS E 171     -130.64     57.79                                   
REMARK 500    GLU F   3      170.31    -55.88                                   
REMARK 500    ALA F  15      -18.57    -47.55                                   
REMARK 500    HIS F  56       36.55    -96.52                                   
REMARK 500    ASP F  89     -148.17     80.48                                   
REMARK 500    ASP F 144     -111.23     62.74                                   
REMARK 500    ASN F 148       36.60     90.09                                   
REMARK 500    PHE F 166       -5.62   -161.52                                   
REMARK 500    LYS F 171     -130.64     57.80                                   
REMARK 500    GLU G   3      170.29    -55.90                                   
REMARK 500    ALA G  15      -18.53    -47.57                                   
REMARK 500    HIS G  56       36.54    -96.57                                   
REMARK 500    ASP G  89     -148.11     80.45                                   
REMARK 500    ASP G 144     -111.26     62.77                                   
REMARK 500    ASN G 148       36.55     90.12                                   
REMARK 500    PHE G 166       -5.65   -161.59                                   
REMARK 500    LYS G 171     -130.69     57.80                                   
REMARK 500    GLU H   3      170.29    -55.88                                   
REMARK 500    ALA H  15      -18.54    -47.54                                   
REMARK 500    HIS H  56       36.44    -96.53                                   
REMARK 500    ASP H  89     -148.12     80.53                                   
REMARK 500    ASP H 144     -111.32     62.76                                   
REMARK 500    ASN H 148       36.63     90.10                                   
REMARK 500    PHE H 166       -5.59   -161.58                                   
REMARK 500    LYS H 171     -130.63     57.76                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    GLU A  94        19.1      L          L   OUTSIDE RANGE           
REMARK 500    ASN A 148        22.6      L          L   OUTSIDE RANGE           
REMARK 500    MET A 161        22.8      L          L   OUTSIDE RANGE           
REMARK 500    GLU B  94        19.1      L          L   OUTSIDE RANGE           
REMARK 500    ASN B 148        22.6      L          L   OUTSIDE RANGE           
REMARK 500    MET B 161        22.8      L          L   OUTSIDE RANGE           
REMARK 500    GLU C  94        19.1      L          L   OUTSIDE RANGE           
REMARK 500    ASN C 148        22.6      L          L   OUTSIDE RANGE           
REMARK 500    MET C 161        22.8      L          L   OUTSIDE RANGE           
REMARK 500    GLU D  94        19.1      L          L   OUTSIDE RANGE           
REMARK 500    ASN D 148        22.6      L          L   OUTSIDE RANGE           
REMARK 500    MET D 161        22.7      L          L   OUTSIDE RANGE           
REMARK 500    GLU E  94        19.2      L          L   OUTSIDE RANGE           
REMARK 500    ASN E 148        22.7      L          L   OUTSIDE RANGE           
REMARK 500    MET E 161        22.8      L          L   OUTSIDE RANGE           
REMARK 500    GLU F  94        19.1      L          L   OUTSIDE RANGE           
REMARK 500    ASN F 148        22.7      L          L   OUTSIDE RANGE           
REMARK 500    MET F 161        22.8      L          L   OUTSIDE RANGE           
REMARK 500    GLU G  94        19.1      L          L   OUTSIDE RANGE           
REMARK 500    ASN G 148        22.6      L          L   OUTSIDE RANGE           
REMARK 500    MET G 161        22.8      L          L   OUTSIDE RANGE           
REMARK 500    GLU H  94        19.1      L          L   OUTSIDE RANGE           
REMARK 500    ASN H 148        22.7      L          L   OUTSIDE RANGE           
REMARK 500    MET H 161        22.8      L          L   OUTSIDE RANGE           
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 999  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 164   NE2                                                    
REMARK 620 2 HIS A  28   NE2  85.3                                              
REMARK 620 3 HIS A  76   NE2 127.6  81.6                                        
REMARK 620 4 ASP A 160   OD2 114.0  82.8 114.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B 999  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  28   NE2                                                    
REMARK 620 2 HIS B  76   NE2  81.6                                              
REMARK 620 3 ASP B 160   OD2  82.8 114.2                                        
REMARK 620 4 HIS B 164   NE2  85.3 127.6 114.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE C 999  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 164   NE2                                                    
REMARK 620 2 ASP C 160   OD2 114.0                                              
REMARK 620 3 HIS C  76   NE2 127.6 114.2                                        
REMARK 620 4 HIS C  28   NE2  85.3  82.8  81.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE D 999  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  28   NE2                                                    
REMARK 620 2 HIS D  76   NE2  81.6                                              
REMARK 620 3 ASP D 160   OD2  82.8 114.2                                        
REMARK 620 4 HIS D 164   NE2  85.3 127.6 114.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE E 999  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  76   NE2                                                    
REMARK 620 2 HIS E  28   NE2  81.6                                              
REMARK 620 3 ASP E 160   OD2 114.2  82.8                                        
REMARK 620 4 HIS E 164   NE2 127.6  85.3 114.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE F 999  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F 164   NE2                                                    
REMARK 620 2 HIS F  76   NE2 127.6                                              
REMARK 620 3 HIS F  28   NE2  85.3  81.6                                        
REMARK 620 4 ASP F 160   OD2 114.0 114.2  82.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE G 999  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G  28   NE2                                                    
REMARK 620 2 HIS G  76   NE2  81.6                                              
REMARK 620 3 HIS G 164   NE2  85.3 127.6                                        
REMARK 620 4 ASP G 160   OD2  82.8 114.2 114.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE H 999  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP H 160   OD2                                                    
REMARK 620 2 HIS H 164   NE2 114.0                                              
REMARK 620 3 HIS H  28   NE2  82.8  85.3                                        
REMARK 620 4 HIS H  76   NE2 114.3 127.6  81.6                                  
REMARK 620 N                    1     2     3                                   
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 999                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE B 999                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE C 999                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE D 999                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE E 999                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE F 999                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE G 999                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE H 999                 
DBREF  1GN2 A    1   207  UNP    P17670   SODF_MYCTU       1    207             
DBREF  1GN2 B    1   207  UNP    P17670   SODF_MYCTU       1    207             
DBREF  1GN2 C    1   207  UNP    P17670   SODF_MYCTU       1    207             
DBREF  1GN2 D    1   207  UNP    P17670   SODF_MYCTU       1    207             
DBREF  1GN2 E    1   207  UNP    P17670   SODF_MYCTU       1    207             
DBREF  1GN2 F    1   207  UNP    P17670   SODF_MYCTU       1    207             
DBREF  1GN2 G    1   207  UNP    P17670   SODF_MYCTU       1    207             
DBREF  1GN2 H    1   207  UNP    P17670   SODF_MYCTU       1    207             
SEQRES   1 A  207  MET ALA GLU TYR THR LEU PRO ASP LEU ASP TRP ASP TYR          
SEQRES   2 A  207  GLY ALA LEU GLU PRO HIS ILE SER GLY GLN ILE ASN GLU          
SEQRES   3 A  207  LEU HIS HIS SER LYS HIS HIS ALA THR TYR VAL LYS GLY          
SEQRES   4 A  207  ALA ASN ASP ALA VAL ALA LYS LEU GLU GLU ALA ARG ALA          
SEQRES   5 A  207  LYS GLU ASP HIS SER ALA ILE LEU LEU ASN GLU LYS ASN          
SEQRES   6 A  207  LEU ALA PHE ASN LEU ALA GLY HIS VAL ASN HIS THR ILE          
SEQRES   7 A  207  TRP TRP LYS ASN LEU SER PRO ASN GLY GLY ASP LYS PRO          
SEQRES   8 A  207  THR GLY GLU LEU ALA ALA ALA ILE ALA ASP ALA PHE GLY          
SEQRES   9 A  207  SER PHE ASP LYS PHE ARG ALA GLN PHE HIS ALA ALA ALA          
SEQRES  10 A  207  THR THR VAL GLN GLY CYS GLY TRP ALA ALA LEU GLY TRP          
SEQRES  11 A  207  ASP THR LEU GLY ASN LYS LEU LEU ILE PHE GLN VAL TYR          
SEQRES  12 A  207  ASP HIS GLN THR ASN PHE PRO LEU GLY ILE VAL PRO LEU          
SEQRES  13 A  207  LEU LEU LEU ASP MET TRP GLU HIS ALA PHE TYR LEU GLN          
SEQRES  14 A  207  TYR LYS ASN VAL LYS VAL ASP PHE ALA LYS ALA PHE TRP          
SEQRES  15 A  207  ASN VAL VAL ASN TRP ALA ASP VAL GLN SER ARG TYR ALA          
SEQRES  16 A  207  ALA ALA THR SER GLN THR LYS GLY LEU ILE PHE GLY              
SEQRES   1 B  207  MET ALA GLU TYR THR LEU PRO ASP LEU ASP TRP ASP TYR          
SEQRES   2 B  207  GLY ALA LEU GLU PRO HIS ILE SER GLY GLN ILE ASN GLU          
SEQRES   3 B  207  LEU HIS HIS SER LYS HIS HIS ALA THR TYR VAL LYS GLY          
SEQRES   4 B  207  ALA ASN ASP ALA VAL ALA LYS LEU GLU GLU ALA ARG ALA          
SEQRES   5 B  207  LYS GLU ASP HIS SER ALA ILE LEU LEU ASN GLU LYS ASN          
SEQRES   6 B  207  LEU ALA PHE ASN LEU ALA GLY HIS VAL ASN HIS THR ILE          
SEQRES   7 B  207  TRP TRP LYS ASN LEU SER PRO ASN GLY GLY ASP LYS PRO          
SEQRES   8 B  207  THR GLY GLU LEU ALA ALA ALA ILE ALA ASP ALA PHE GLY          
SEQRES   9 B  207  SER PHE ASP LYS PHE ARG ALA GLN PHE HIS ALA ALA ALA          
SEQRES  10 B  207  THR THR VAL GLN GLY CYS GLY TRP ALA ALA LEU GLY TRP          
SEQRES  11 B  207  ASP THR LEU GLY ASN LYS LEU LEU ILE PHE GLN VAL TYR          
SEQRES  12 B  207  ASP HIS GLN THR ASN PHE PRO LEU GLY ILE VAL PRO LEU          
SEQRES  13 B  207  LEU LEU LEU ASP MET TRP GLU HIS ALA PHE TYR LEU GLN          
SEQRES  14 B  207  TYR LYS ASN VAL LYS VAL ASP PHE ALA LYS ALA PHE TRP          
SEQRES  15 B  207  ASN VAL VAL ASN TRP ALA ASP VAL GLN SER ARG TYR ALA          
SEQRES  16 B  207  ALA ALA THR SER GLN THR LYS GLY LEU ILE PHE GLY              
SEQRES   1 C  207  MET ALA GLU TYR THR LEU PRO ASP LEU ASP TRP ASP TYR          
SEQRES   2 C  207  GLY ALA LEU GLU PRO HIS ILE SER GLY GLN ILE ASN GLU          
SEQRES   3 C  207  LEU HIS HIS SER LYS HIS HIS ALA THR TYR VAL LYS GLY          
SEQRES   4 C  207  ALA ASN ASP ALA VAL ALA LYS LEU GLU GLU ALA ARG ALA          
SEQRES   5 C  207  LYS GLU ASP HIS SER ALA ILE LEU LEU ASN GLU LYS ASN          
SEQRES   6 C  207  LEU ALA PHE ASN LEU ALA GLY HIS VAL ASN HIS THR ILE          
SEQRES   7 C  207  TRP TRP LYS ASN LEU SER PRO ASN GLY GLY ASP LYS PRO          
SEQRES   8 C  207  THR GLY GLU LEU ALA ALA ALA ILE ALA ASP ALA PHE GLY          
SEQRES   9 C  207  SER PHE ASP LYS PHE ARG ALA GLN PHE HIS ALA ALA ALA          
SEQRES  10 C  207  THR THR VAL GLN GLY CYS GLY TRP ALA ALA LEU GLY TRP          
SEQRES  11 C  207  ASP THR LEU GLY ASN LYS LEU LEU ILE PHE GLN VAL TYR          
SEQRES  12 C  207  ASP HIS GLN THR ASN PHE PRO LEU GLY ILE VAL PRO LEU          
SEQRES  13 C  207  LEU LEU LEU ASP MET TRP GLU HIS ALA PHE TYR LEU GLN          
SEQRES  14 C  207  TYR LYS ASN VAL LYS VAL ASP PHE ALA LYS ALA PHE TRP          
SEQRES  15 C  207  ASN VAL VAL ASN TRP ALA ASP VAL GLN SER ARG TYR ALA          
SEQRES  16 C  207  ALA ALA THR SER GLN THR LYS GLY LEU ILE PHE GLY              
SEQRES   1 D  207  MET ALA GLU TYR THR LEU PRO ASP LEU ASP TRP ASP TYR          
SEQRES   2 D  207  GLY ALA LEU GLU PRO HIS ILE SER GLY GLN ILE ASN GLU          
SEQRES   3 D  207  LEU HIS HIS SER LYS HIS HIS ALA THR TYR VAL LYS GLY          
SEQRES   4 D  207  ALA ASN ASP ALA VAL ALA LYS LEU GLU GLU ALA ARG ALA          
SEQRES   5 D  207  LYS GLU ASP HIS SER ALA ILE LEU LEU ASN GLU LYS ASN          
SEQRES   6 D  207  LEU ALA PHE ASN LEU ALA GLY HIS VAL ASN HIS THR ILE          
SEQRES   7 D  207  TRP TRP LYS ASN LEU SER PRO ASN GLY GLY ASP LYS PRO          
SEQRES   8 D  207  THR GLY GLU LEU ALA ALA ALA ILE ALA ASP ALA PHE GLY          
SEQRES   9 D  207  SER PHE ASP LYS PHE ARG ALA GLN PHE HIS ALA ALA ALA          
SEQRES  10 D  207  THR THR VAL GLN GLY CYS GLY TRP ALA ALA LEU GLY TRP          
SEQRES  11 D  207  ASP THR LEU GLY ASN LYS LEU LEU ILE PHE GLN VAL TYR          
SEQRES  12 D  207  ASP HIS GLN THR ASN PHE PRO LEU GLY ILE VAL PRO LEU          
SEQRES  13 D  207  LEU LEU LEU ASP MET TRP GLU HIS ALA PHE TYR LEU GLN          
SEQRES  14 D  207  TYR LYS ASN VAL LYS VAL ASP PHE ALA LYS ALA PHE TRP          
SEQRES  15 D  207  ASN VAL VAL ASN TRP ALA ASP VAL GLN SER ARG TYR ALA          
SEQRES  16 D  207  ALA ALA THR SER GLN THR LYS GLY LEU ILE PHE GLY              
SEQRES   1 E  207  MET ALA GLU TYR THR LEU PRO ASP LEU ASP TRP ASP TYR          
SEQRES   2 E  207  GLY ALA LEU GLU PRO HIS ILE SER GLY GLN ILE ASN GLU          
SEQRES   3 E  207  LEU HIS HIS SER LYS HIS HIS ALA THR TYR VAL LYS GLY          
SEQRES   4 E  207  ALA ASN ASP ALA VAL ALA LYS LEU GLU GLU ALA ARG ALA          
SEQRES   5 E  207  LYS GLU ASP HIS SER ALA ILE LEU LEU ASN GLU LYS ASN          
SEQRES   6 E  207  LEU ALA PHE ASN LEU ALA GLY HIS VAL ASN HIS THR ILE          
SEQRES   7 E  207  TRP TRP LYS ASN LEU SER PRO ASN GLY GLY ASP LYS PRO          
SEQRES   8 E  207  THR GLY GLU LEU ALA ALA ALA ILE ALA ASP ALA PHE GLY          
SEQRES   9 E  207  SER PHE ASP LYS PHE ARG ALA GLN PHE HIS ALA ALA ALA          
SEQRES  10 E  207  THR THR VAL GLN GLY CYS GLY TRP ALA ALA LEU GLY TRP          
SEQRES  11 E  207  ASP THR LEU GLY ASN LYS LEU LEU ILE PHE GLN VAL TYR          
SEQRES  12 E  207  ASP HIS GLN THR ASN PHE PRO LEU GLY ILE VAL PRO LEU          
SEQRES  13 E  207  LEU LEU LEU ASP MET TRP GLU HIS ALA PHE TYR LEU GLN          
SEQRES  14 E  207  TYR LYS ASN VAL LYS VAL ASP PHE ALA LYS ALA PHE TRP          
SEQRES  15 E  207  ASN VAL VAL ASN TRP ALA ASP VAL GLN SER ARG TYR ALA          
SEQRES  16 E  207  ALA ALA THR SER GLN THR LYS GLY LEU ILE PHE GLY              
SEQRES   1 F  207  MET ALA GLU TYR THR LEU PRO ASP LEU ASP TRP ASP TYR          
SEQRES   2 F  207  GLY ALA LEU GLU PRO HIS ILE SER GLY GLN ILE ASN GLU          
SEQRES   3 F  207  LEU HIS HIS SER LYS HIS HIS ALA THR TYR VAL LYS GLY          
SEQRES   4 F  207  ALA ASN ASP ALA VAL ALA LYS LEU GLU GLU ALA ARG ALA          
SEQRES   5 F  207  LYS GLU ASP HIS SER ALA ILE LEU LEU ASN GLU LYS ASN          
SEQRES   6 F  207  LEU ALA PHE ASN LEU ALA GLY HIS VAL ASN HIS THR ILE          
SEQRES   7 F  207  TRP TRP LYS ASN LEU SER PRO ASN GLY GLY ASP LYS PRO          
SEQRES   8 F  207  THR GLY GLU LEU ALA ALA ALA ILE ALA ASP ALA PHE GLY          
SEQRES   9 F  207  SER PHE ASP LYS PHE ARG ALA GLN PHE HIS ALA ALA ALA          
SEQRES  10 F  207  THR THR VAL GLN GLY CYS GLY TRP ALA ALA LEU GLY TRP          
SEQRES  11 F  207  ASP THR LEU GLY ASN LYS LEU LEU ILE PHE GLN VAL TYR          
SEQRES  12 F  207  ASP HIS GLN THR ASN PHE PRO LEU GLY ILE VAL PRO LEU          
SEQRES  13 F  207  LEU LEU LEU ASP MET TRP GLU HIS ALA PHE TYR LEU GLN          
SEQRES  14 F  207  TYR LYS ASN VAL LYS VAL ASP PHE ALA LYS ALA PHE TRP          
SEQRES  15 F  207  ASN VAL VAL ASN TRP ALA ASP VAL GLN SER ARG TYR ALA          
SEQRES  16 F  207  ALA ALA THR SER GLN THR LYS GLY LEU ILE PHE GLY              
SEQRES   1 G  207  MET ALA GLU TYR THR LEU PRO ASP LEU ASP TRP ASP TYR          
SEQRES   2 G  207  GLY ALA LEU GLU PRO HIS ILE SER GLY GLN ILE ASN GLU          
SEQRES   3 G  207  LEU HIS HIS SER LYS HIS HIS ALA THR TYR VAL LYS GLY          
SEQRES   4 G  207  ALA ASN ASP ALA VAL ALA LYS LEU GLU GLU ALA ARG ALA          
SEQRES   5 G  207  LYS GLU ASP HIS SER ALA ILE LEU LEU ASN GLU LYS ASN          
SEQRES   6 G  207  LEU ALA PHE ASN LEU ALA GLY HIS VAL ASN HIS THR ILE          
SEQRES   7 G  207  TRP TRP LYS ASN LEU SER PRO ASN GLY GLY ASP LYS PRO          
SEQRES   8 G  207  THR GLY GLU LEU ALA ALA ALA ILE ALA ASP ALA PHE GLY          
SEQRES   9 G  207  SER PHE ASP LYS PHE ARG ALA GLN PHE HIS ALA ALA ALA          
SEQRES  10 G  207  THR THR VAL GLN GLY CYS GLY TRP ALA ALA LEU GLY TRP          
SEQRES  11 G  207  ASP THR LEU GLY ASN LYS LEU LEU ILE PHE GLN VAL TYR          
SEQRES  12 G  207  ASP HIS GLN THR ASN PHE PRO LEU GLY ILE VAL PRO LEU          
SEQRES  13 G  207  LEU LEU LEU ASP MET TRP GLU HIS ALA PHE TYR LEU GLN          
SEQRES  14 G  207  TYR LYS ASN VAL LYS VAL ASP PHE ALA LYS ALA PHE TRP          
SEQRES  15 G  207  ASN VAL VAL ASN TRP ALA ASP VAL GLN SER ARG TYR ALA          
SEQRES  16 G  207  ALA ALA THR SER GLN THR LYS GLY LEU ILE PHE GLY              
SEQRES   1 H  207  MET ALA GLU TYR THR LEU PRO ASP LEU ASP TRP ASP TYR          
SEQRES   2 H  207  GLY ALA LEU GLU PRO HIS ILE SER GLY GLN ILE ASN GLU          
SEQRES   3 H  207  LEU HIS HIS SER LYS HIS HIS ALA THR TYR VAL LYS GLY          
SEQRES   4 H  207  ALA ASN ASP ALA VAL ALA LYS LEU GLU GLU ALA ARG ALA          
SEQRES   5 H  207  LYS GLU ASP HIS SER ALA ILE LEU LEU ASN GLU LYS ASN          
SEQRES   6 H  207  LEU ALA PHE ASN LEU ALA GLY HIS VAL ASN HIS THR ILE          
SEQRES   7 H  207  TRP TRP LYS ASN LEU SER PRO ASN GLY GLY ASP LYS PRO          
SEQRES   8 H  207  THR GLY GLU LEU ALA ALA ALA ILE ALA ASP ALA PHE GLY          
SEQRES   9 H  207  SER PHE ASP LYS PHE ARG ALA GLN PHE HIS ALA ALA ALA          
SEQRES  10 H  207  THR THR VAL GLN GLY CYS GLY TRP ALA ALA LEU GLY TRP          
SEQRES  11 H  207  ASP THR LEU GLY ASN LYS LEU LEU ILE PHE GLN VAL TYR          
SEQRES  12 H  207  ASP HIS GLN THR ASN PHE PRO LEU GLY ILE VAL PRO LEU          
SEQRES  13 H  207  LEU LEU LEU ASP MET TRP GLU HIS ALA PHE TYR LEU GLN          
SEQRES  14 H  207  TYR LYS ASN VAL LYS VAL ASP PHE ALA LYS ALA PHE TRP          
SEQRES  15 H  207  ASN VAL VAL ASN TRP ALA ASP VAL GLN SER ARG TYR ALA          
SEQRES  16 H  207  ALA ALA THR SER GLN THR LYS GLY LEU ILE PHE GLY              
HET     FE  A 999       1                                                       
HET     FE  B 999       1                                                       
HET     FE  C 999       1                                                       
HET     FE  D 999       1                                                       
HET     FE  E 999       1                                                       
HET     FE  F 999       1                                                       
HET     FE  G 999       1                                                       
HET     FE  H 999       1                                                       
HETNAM      FE FE (III) ION                                                     
FORMUL   9   FE    8(FE 3+)                                                     
HELIX    1   1 ASP A   12  GLU A   17  5                                   6    
HELIX    2   2 SER A   21  LYS A   31  1                                  11    
HELIX    3   3 LYS A   31  GLU A   54  1                                  24    
HELIX    4   4 ALA A   58  LEU A   83  1                                  26    
HELIX    5   5 GLY A   93  GLY A  104  1                                  12    
HELIX    6   6 SER A  105  THR A  119  1                                  15    
HELIX    7   7 TRP A  162  ALA A  165  5                                   4    
HELIX    8   8 PHE A  166  LYS A  171  1                                   6    
HELIX    9   9 VAL A  173  PHE A  181  1                                   9    
HELIX   10  10 TRP A  182  VAL A  184  5                                   3    
HELIX   11  11 ASN A  186  THR A  198  1                                  13    
HELIX   12  12 ASP B   12  GLU B   17  5                                   6    
HELIX   13  13 SER B   21  LYS B   31  1                                  11    
HELIX   14  14 LYS B   31  GLU B   54  1                                  24    
HELIX   15  15 ALA B   58  LEU B   83  1                                  26    
HELIX   16  16 GLY B   93  GLY B  104  1                                  12    
HELIX   17  17 SER B  105  THR B  119  1                                  15    
HELIX   18  18 TRP B  162  ALA B  165  5                                   4    
HELIX   19  19 PHE B  166  LYS B  171  1                                   6    
HELIX   20  20 VAL B  173  PHE B  181  1                                   9    
HELIX   21  21 TRP B  182  VAL B  184  5                                   3    
HELIX   22  22 ASN B  186  THR B  198  1                                  13    
HELIX   23  23 ASP C   12  GLU C   17  5                                   6    
HELIX   24  24 SER C   21  LYS C   31  1                                  11    
HELIX   25  25 LYS C   31  GLU C   54  1                                  24    
HELIX   26  26 ALA C   58  LEU C   83  1                                  26    
HELIX   27  27 GLY C   93  GLY C  104  1                                  12    
HELIX   28  28 SER C  105  THR C  119  1                                  15    
HELIX   29  29 TRP C  162  ALA C  165  5                                   4    
HELIX   30  30 PHE C  166  LYS C  171  1                                   6    
HELIX   31  31 VAL C  173  PHE C  181  1                                   9    
HELIX   32  32 TRP C  182  VAL C  184  5                                   3    
HELIX   33  33 ASN C  186  THR C  198  1                                  13    
HELIX   34  34 ASP D   12  GLU D   17  5                                   6    
HELIX   35  35 SER D   21  LYS D   31  1                                  11    
HELIX   36  36 LYS D   31  GLU D   54  1                                  24    
HELIX   37  37 ALA D   58  LEU D   83  1                                  26    
HELIX   38  38 GLY D   93  GLY D  104  1                                  12    
HELIX   39  39 SER D  105  THR D  119  1                                  15    
HELIX   40  40 TRP D  162  ALA D  165  5                                   4    
HELIX   41  41 PHE D  166  LYS D  171  1                                   6    
HELIX   42  42 VAL D  173  PHE D  181  1                                   9    
HELIX   43  43 TRP D  182  VAL D  184  5                                   3    
HELIX   44  44 ASN D  186  THR D  198  1                                  13    
HELIX   45  45 ASP E   12  GLU E   17  5                                   6    
HELIX   46  46 SER E   21  LYS E   31  1                                  11    
HELIX   47  47 LYS E   31  GLU E   54  1                                  24    
HELIX   48  48 ALA E   58  LEU E   83  1                                  26    
HELIX   49  49 GLY E   93  GLY E  104  1                                  12    
HELIX   50  50 SER E  105  THR E  119  1                                  15    
HELIX   51  51 TRP E  162  ALA E  165  5                                   4    
HELIX   52  52 PHE E  166  LYS E  171  1                                   6    
HELIX   53  53 VAL E  173  PHE E  181  1                                   9    
HELIX   54  54 TRP E  182  VAL E  184  5                                   3    
HELIX   55  55 ASN E  186  THR E  198  1                                  13    
HELIX   56  56 ASP F   12  GLU F   17  5                                   6    
HELIX   57  57 SER F   21  LYS F   31  1                                  11    
HELIX   58  58 LYS F   31  GLU F   54  1                                  24    
HELIX   59  59 ALA F   58  LEU F   83  1                                  26    
HELIX   60  60 GLY F   93  GLY F  104  1                                  12    
HELIX   61  61 SER F  105  THR F  119  1                                  15    
HELIX   62  62 TRP F  162  ALA F  165  5                                   4    
HELIX   63  63 PHE F  166  LYS F  171  1                                   6    
HELIX   64  64 VAL F  173  PHE F  181  1                                   9    
HELIX   65  65 TRP F  182  VAL F  184  5                                   3    
HELIX   66  66 ASN F  186  THR F  198  1                                  13    
HELIX   67  67 ASP G   12  GLU G   17  5                                   6    
HELIX   68  68 SER G   21  LYS G   31  1                                  11    
HELIX   69  69 LYS G   31  GLU G   54  1                                  24    
HELIX   70  70 ALA G   58  LEU G   83  1                                  26    
HELIX   71  71 GLY G   93  GLY G  104  1                                  12    
HELIX   72  72 SER G  105  THR G  119  1                                  15    
HELIX   73  73 TRP G  162  ALA G  165  5                                   4    
HELIX   74  74 PHE G  166  LYS G  171  1                                   6    
HELIX   75  75 VAL G  173  PHE G  181  1                                   9    
HELIX   76  76 TRP G  182  VAL G  184  5                                   3    
HELIX   77  77 ASN G  186  THR G  198  1                                  13    
HELIX   78  78 ASP H   12  GLU H   17  5                                   6    
HELIX   79  79 SER H   21  LYS H   31  1                                  11    
HELIX   80  80 LYS H   31  GLU H   54  1                                  24    
HELIX   81  81 ALA H   58  LEU H   83  1                                  26    
HELIX   82  82 GLY H   93  GLY H  104  1                                  12    
HELIX   83  83 SER H  105  THR H  119  1                                  15    
HELIX   84  84 TRP H  162  ALA H  165  5                                   4    
HELIX   85  85 PHE H  166  LYS H  171  1                                   6    
HELIX   86  86 VAL H  173  PHE H  181  1                                   9    
HELIX   87  87 TRP H  182  VAL H  184  5                                   3    
HELIX   88  88 ASN H  186  THR H  198  1                                  13    
SHEET    1  AA 3 LYS A 136  TYR A 143  0                                        
SHEET    2  AA 3 GLY A 124  ASP A 131 -1  O  TRP A 125   N  VAL A 142           
SHEET    3  AA 3 ILE A 153  ASP A 160 -1  O  VAL A 154   N  TRP A 130           
SHEET    1  BA 3 LYS B 136  TYR B 143  0                                        
SHEET    2  BA 3 GLY B 124  ASP B 131 -1  O  TRP B 125   N  VAL B 142           
SHEET    3  BA 3 ILE B 153  ASP B 160 -1  O  VAL B 154   N  TRP B 130           
SHEET    1  CA 3 LYS C 136  TYR C 143  0                                        
SHEET    2  CA 3 GLY C 124  ASP C 131 -1  O  TRP C 125   N  VAL C 142           
SHEET    3  CA 3 ILE C 153  ASP C 160 -1  O  VAL C 154   N  TRP C 130           
SHEET    1  DA 3 LYS D 136  TYR D 143  0                                        
SHEET    2  DA 3 GLY D 124  ASP D 131 -1  O  TRP D 125   N  VAL D 142           
SHEET    3  DA 3 ILE D 153  ASP D 160 -1  O  VAL D 154   N  TRP D 130           
SHEET    1  EA 3 LYS E 136  TYR E 143  0                                        
SHEET    2  EA 3 GLY E 124  ASP E 131 -1  O  TRP E 125   N  VAL E 142           
SHEET    3  EA 3 ILE E 153  ASP E 160 -1  O  VAL E 154   N  TRP E 130           
SHEET    1  FA 3 LYS F 136  TYR F 143  0                                        
SHEET    2  FA 3 GLY F 124  ASP F 131 -1  O  TRP F 125   N  VAL F 142           
SHEET    3  FA 3 ILE F 153  ASP F 160 -1  O  VAL F 154   N  TRP F 130           
SHEET    1  GA 3 LYS G 136  TYR G 143  0                                        
SHEET    2  GA 3 GLY G 124  ASP G 131 -1  O  TRP G 125   N  VAL G 142           
SHEET    3  GA 3 ILE G 153  ASP G 160 -1  O  VAL G 154   N  TRP G 130           
SHEET    1  HA 3 LYS H 136  TYR H 143  0                                        
SHEET    2  HA 3 GLY H 124  ASP H 131 -1  O  TRP H 125   N  VAL H 142           
SHEET    3  HA 3 ILE H 153  ASP H 160 -1  O  VAL H 154   N  TRP H 130           
SSBOND   1 CYS A  123    CYS B  123                          1555   1555  2.05  
SSBOND   2 CYS C  123    CYS D  123                          1555   1555  1.76  
SSBOND   3 CYS E  123    CYS F  123                          1555   1555  2.25  
SSBOND   4 CYS G  123    CYS H  123                          1555   1555  1.92  
LINK        FE    FE A 999                 NE2 HIS A 164     1555   1555  2.12  
LINK        FE    FE A 999                 NE2 HIS A  28     1555   1555  2.36  
LINK        FE    FE A 999                 NE2 HIS A  76     1555   1555  2.28  
LINK        FE    FE A 999                 OD2 ASP A 160     1555   1555  1.97  
LINK        FE    FE B 999                 NE2 HIS B  28     1555   1555  2.36  
LINK        FE    FE B 999                 NE2 HIS B  76     1555   1555  2.28  
LINK        FE    FE B 999                 OD2 ASP B 160     1555   1555  1.97  
LINK        FE    FE B 999                 NE2 HIS B 164     1555   1555  2.12  
LINK        FE    FE C 999                 NE2 HIS C 164     1555   1555  2.12  
LINK        FE    FE C 999                 OD2 ASP C 160     1555   1555  1.96  
LINK        FE    FE C 999                 NE2 HIS C  76     1555   1555  2.28  
LINK        FE    FE C 999                 NE2 HIS C  28     1555   1555  2.36  
LINK        FE    FE D 999                 NE2 HIS D  28     1555   1555  2.36  
LINK        FE    FE D 999                 NE2 HIS D  76     1555   1555  2.28  
LINK        FE    FE D 999                 OD2 ASP D 160     1555   1555  1.97  
LINK        FE    FE D 999                 NE2 HIS D 164     1555   1555  2.12  
LINK        FE    FE E 999                 NE2 HIS E  28     1555   1555  2.36  
LINK        FE    FE E 999                 OD2 ASP E 160     1555   1555  1.97  
LINK        FE    FE E 999                 NE2 HIS E 164     1555   1555  2.12  
LINK        FE    FE E 999                 NE2 HIS E  76     1555   1555  2.28  
LINK        FE    FE F 999                 NE2 HIS F  76     1555   1555  2.28  
LINK        FE    FE F 999                 NE2 HIS F  28     1555   1555  2.36  
LINK        FE    FE F 999                 OD2 ASP F 160     1555   1555  1.96  
LINK        FE    FE F 999                 NE2 HIS F 164     1555   1555  2.12  
LINK        FE    FE G 999                 NE2 HIS G  76     1555   1555  2.28  
LINK        FE    FE G 999                 NE2 HIS G 164     1555   1555  2.12  
LINK        FE    FE G 999                 OD2 ASP G 160     1555   1555  1.97  
LINK        FE    FE G 999                 NE2 HIS G  28     1555   1555  2.36  
LINK        FE    FE H 999                 NE2 HIS H 164     1555   1555  2.12  
LINK        FE    FE H 999                 NE2 HIS H  28     1555   1555  2.36  
LINK        FE    FE H 999                 NE2 HIS H  76     1555   1555  2.28  
LINK        FE    FE H 999                 OD2 ASP H 160     1555   1555  1.97  
CISPEP   1 GLU A   17    PRO A   18          0         0.58                     
CISPEP   2 GLU B   17    PRO B   18          0         0.50                     
CISPEP   3 GLU C   17    PRO C   18          0         0.61                     
CISPEP   4 GLU D   17    PRO D   18          0         0.50                     
CISPEP   5 GLU E   17    PRO E   18          0         0.56                     
CISPEP   6 GLU F   17    PRO F   18          0         0.58                     
CISPEP   7 GLU G   17    PRO G   18          0         0.55                     
CISPEP   8 GLU H   17    PRO H   18          0         0.62                     
SITE     1 AC1  4 HIS A  28  HIS A  76  ASP A 160  HIS A 164                    
SITE     1 AC2  4 HIS B  28  HIS B  76  ASP B 160  HIS B 164                    
SITE     1 AC3  4 HIS C  28  HIS C  76  ASP C 160  HIS C 164                    
SITE     1 AC4  4 HIS D  28  HIS D  76  ASP D 160  HIS D 164                    
SITE     1 AC5  4 HIS E  28  HIS E  76  ASP E 160  HIS E 164                    
SITE     1 AC6  4 HIS F  28  HIS F  76  ASP F 160  HIS F 164                    
SITE     1 AC7  4 HIS G  28  HIS G  76  ASP G 160  HIS G 164                    
SITE     1 AC8  4 HIS H  28  HIS H  76  ASP H 160  HIS H 164                    
CRYST1  103.080  106.330   76.100  90.00  92.37  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      0.009701  0.000000  0.000401        0.00000                         
SCALE2      0.000000  0.009405  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013152        0.00000                         
MTRIX1   1 -0.665300 -0.591100  0.456000      139.33800    1                    
MTRIX2   1 -0.589700  0.041500 -0.806500       30.10700    1                    
MTRIX3   1  0.457900 -0.805500 -0.376200      -63.08100    1                    
MTRIX1   2 -0.355200 -0.309400 -0.882100      137.13699    1                    
MTRIX2   2 -0.322400 -0.845200  0.426300      -51.96000    1                    
MTRIX3   2 -0.877400  0.435800  0.200400      119.24900    1                    
MTRIX1   3  0.011700  0.909900  0.414600      134.83701    1                    
MTRIX2   3  0.905000 -0.186000  0.382500     -148.84900    1                    
MTRIX3   3  0.425200  0.370800 -0.825700       -3.33000    1                    
MTRIX1   4 -0.975400  0.210000 -0.067000       56.28800    1                    
MTRIX2   4 -0.189000 -0.953300 -0.235400       50.38700    1                    
MTRIX3   4 -0.113300 -0.216900  0.969600       42.56200    1                    
MTRIX1   5  0.496200  0.634400 -0.592800      -69.59200    1                    
MTRIX2   5  0.576800  0.269300  0.771100       10.82300    1                    
MTRIX3   5  0.648800 -0.724600 -0.232300      -41.38200    1                    
MTRIX1   6  0.330300  0.104300  0.938100      -95.46000    1                    
MTRIX2   6  0.574900  0.766000 -0.287600       46.56000    1                    
MTRIX3   6 -0.748600  0.634300  0.193100      154.66901    1                    
MTRIX1   7  0.154600 -0.947800 -0.278700     -106.55400    1                    
MTRIX2   7 -0.965100 -0.084600 -0.247700      167.28500    1                    
MTRIX3   7  0.211200  0.307300 -0.927900       57.18800    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system