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Database: PDB
Entry: 1Y67
LinkDB: 1Y67
Original site: 1Y67 
HEADER    OXIDOREDUCTASE                          03-DEC-04   1Y67              
TITLE     CRYSTAL STRUCTURE OF MANGANESE SUPEROXIDE DISMUTASE FROM              
TITLE    2 DEINOCOCCUS RADIODURANS                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MANGANESE SUPEROXIDE DISMUTASE;                            
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: MNSOD;                                                      
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;                        
SOURCE   3 ORGANISM_TAXID: 1299;                                                
SOURCE   4 GENE: SODA;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21-GOLD (DE3);                           
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET22B                                    
KEYWDS    SUPEROXIDE DISMUTASE, MANGANESE ENZYME, METALLOPROTEIN,               
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.CHAN,S.TANAKA,M.R.SAWAYA,L.J.PERRY                                  
REVDAT   2   24-FEB-09 1Y67    1       VERSN                                    
REVDAT   1   21-DEC-04 1Y67    0                                                
JRNL        AUTH   S.CHAN,S.TANAKA,M.R.SAWAYA,L.J.PERRY                         
JRNL        TITL   CRYSTAL STRUCTURE OF MANGANESE SUPEROXIDE                    
JRNL        TITL 2 DISMUTASE FROM DEINOCOCCUS RADIODURANS                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   G.N.MURSHUDOV                                                
REMARK   1  TITL   REFINEMENT OF MACROMOLECULAR STRUCTURES BY THE               
REMARK   1  TITL 2 MAXIMUM-LIKELIHOOD METHOD                                    
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  53   240 1997              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 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 : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 119.52                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 74526                          
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) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.205                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.961                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3697                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5071                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.18                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2410                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 266                          
REMARK   3   BIN FREE R VALUE                    : 0.2790                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6565                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : NULL                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.12                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.90300                                              
REMARK   3    B22 (A**2) : -0.95900                                             
REMARK   3    B33 (A**2) : -1.01600                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.79700                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.140         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.121         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.949                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6743 ; 0.009 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9172 ; 1.093 ; 1.918       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   825 ; 5.212 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   352 ;35.443 ;24.830       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1029 ;12.946 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    29 ;12.197 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   953 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5333 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2992 ; 0.186 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4663 ; 0.298 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   420 ; 0.106 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     1 ; 0.025 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    36 ; 0.141 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    17 ; 0.117 ; 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):  4241 ; 0.540 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6570 ; 0.862 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2933 ; 1.446 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2602 ; 2.279 ; 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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    93                          
REMARK   3    RESIDUE RANGE :   A    97        A   213                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.9494  16.4962  14.2350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1359 T22:  -0.1242                                     
REMARK   3      T33:  -0.1349 T12:  -0.0249                                     
REMARK   3      T13:   0.0135 T23:  -0.0019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6603 L22:   2.4764                                     
REMARK   3      L33:   1.5235 L12:   0.3411                                     
REMARK   3      L13:   0.5030 L23:   0.3781                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0502 S12:  -0.0190 S13:   0.0351                       
REMARK   3      S21:  -0.3158 S22:   0.0077 S23:   0.0475                       
REMARK   3      S31:  -0.0491 S32:   0.0661 S33:   0.0424                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B    90                          
REMARK   3    RESIDUE RANGE :   B    98        B   211                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.3050  27.9594  39.7315              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1419 T22:  -0.1051                                     
REMARK   3      T33:  -0.1491 T12:  -0.0441                                     
REMARK   3      T13:  -0.0023 T23:  -0.0310                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4630 L22:   1.9144                                     
REMARK   3      L33:   2.5240 L12:   0.2652                                     
REMARK   3      L13:   1.1158 L23:   0.1777                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1047 S12:  -0.0825 S13:   0.1760                       
REMARK   3      S21:   0.1919 S22:  -0.0810 S23:  -0.0461                       
REMARK   3      S31:  -0.2949 S32:   0.0107 S33:   0.1857                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     2        C    89                          
REMARK   3    RESIDUE RANGE :   C    98        C   213                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.3888  26.4932  72.5899              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1447 T22:  -0.0939                                     
REMARK   3      T33:  -0.1608 T12:  -0.0044                                     
REMARK   3      T13:  -0.0157 T23:  -0.0078                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2965 L22:   2.0345                                     
REMARK   3      L33:   2.3783 L12:   0.3248                                     
REMARK   3      L13:   0.4772 L23:   1.1512                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0355 S12:   0.2108 S13:  -0.0167                       
REMARK   3      S21:  -0.1621 S22:   0.1460 S23:  -0.0671                       
REMARK   3      S31:   0.0003 S32:   0.0197 S33:  -0.1815                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     2        D   215                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.9661  18.7900 100.5325              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0373 T22:  -0.2063                                     
REMARK   3      T33:  -0.1173 T12:  -0.0063                                     
REMARK   3      T13:  -0.1017 T23:   0.0129                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2085 L22:   1.3554                                     
REMARK   3      L33:   1.7743 L12:   0.1924                                     
REMARK   3      L13:   0.5607 L23:   0.3588                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1723 S12:   0.0062 S13:  -0.1939                       
REMARK   3      S21:   0.3459 S22:   0.0118 S23:  -0.1297                       
REMARK   3      S31:   0.3405 S32:  -0.0201 S33:  -0.1841                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK BULK SOLVENT                                    
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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 1Y67 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-DEC-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB031166.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-APR-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.1                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 74526                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 119.500                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.49300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: EPMR                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1VEW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200MM AMMONIUM ACETATE (PH 7.1) 20%      
REMARK 280  (W/V) PEG3350, 0.3M NACL, 0.3M IMIDAZOLE, 20MM TRIS (PH 8.0),       
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K                     
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       43.96100            
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER FORMED FROM EITHER        
REMARK 300 CHAINS A AND B OR CHAINS C AND D.                                    
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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     0                                                      
REMARK 465     GLN A    94                                                      
REMARK 465     ASN A    95                                                      
REMARK 465     GLY A    96                                                      
REMARK 465     PRO A   214                                                      
REMARK 465     ARG A   215                                                      
REMARK 465     GLY A   216                                                      
REMARK 465     SER A   217                                                      
REMARK 465     ALA A   218                                                      
REMARK 465     ALA A   219                                                      
REMARK 465     ALA A   220                                                      
REMARK 465     LEU A   221                                                      
REMARK 465     GLU A   222                                                      
REMARK 465     HIS A   223                                                      
REMARK 465     HIS A   224                                                      
REMARK 465     HIS A   225                                                      
REMARK 465     HIS A   226                                                      
REMARK 465     HIS A   227                                                      
REMARK 465     HIS A   228                                                      
REMARK 465     MET B     0                                                      
REMARK 465     GLY B    91                                                      
REMARK 465     GLN B    92                                                      
REMARK 465     GLY B    93                                                      
REMARK 465     GLN B    94                                                      
REMARK 465     ASN B    95                                                      
REMARK 465     GLY B    96                                                      
REMARK 465     ALA B    97                                                      
REMARK 465     LEU B   212                                                      
REMARK 465     VAL B   213                                                      
REMARK 465     PRO B   214                                                      
REMARK 465     ARG B   215                                                      
REMARK 465     GLY B   216                                                      
REMARK 465     SER B   217                                                      
REMARK 465     ALA B   218                                                      
REMARK 465     ALA B   219                                                      
REMARK 465     ALA B   220                                                      
REMARK 465     LEU B   221                                                      
REMARK 465     GLU B   222                                                      
REMARK 465     HIS B   223                                                      
REMARK 465     HIS B   224                                                      
REMARK 465     HIS B   225                                                      
REMARK 465     HIS B   226                                                      
REMARK 465     HIS B   227                                                      
REMARK 465     HIS B   228                                                      
REMARK 465     MET C     0                                                      
REMARK 465     ALA C     1                                                      
REMARK 465     GLN C    90                                                      
REMARK 465     GLY C    91                                                      
REMARK 465     GLN C    92                                                      
REMARK 465     GLY C    93                                                      
REMARK 465     GLN C    94                                                      
REMARK 465     ASN C    95                                                      
REMARK 465     GLY C    96                                                      
REMARK 465     ALA C    97                                                      
REMARK 465     PRO C   214                                                      
REMARK 465     ARG C   215                                                      
REMARK 465     GLY C   216                                                      
REMARK 465     SER C   217                                                      
REMARK 465     ALA C   218                                                      
REMARK 465     ALA C   219                                                      
REMARK 465     ALA C   220                                                      
REMARK 465     LEU C   221                                                      
REMARK 465     GLU C   222                                                      
REMARK 465     HIS C   223                                                      
REMARK 465     HIS C   224                                                      
REMARK 465     HIS C   225                                                      
REMARK 465     HIS C   226                                                      
REMARK 465     HIS C   227                                                      
REMARK 465     HIS C   228                                                      
REMARK 465     MET D     0                                                      
REMARK 465     ALA D     1                                                      
REMARK 465     GLY D   216                                                      
REMARK 465     SER D   217                                                      
REMARK 465     ALA D   218                                                      
REMARK 465     ALA D   219                                                      
REMARK 465     ALA D   220                                                      
REMARK 465     LEU D   221                                                      
REMARK 465     GLU D   222                                                      
REMARK 465     HIS D   223                                                      
REMARK 465     HIS D   224                                                      
REMARK 465     HIS D   225                                                      
REMARK 465     HIS D   226                                                      
REMARK 465     HIS D   227                                                      
REMARK 465     HIS D   228                                                      
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    ASN A 151     -119.84     54.84                                   
REMARK 500    TYR A 179      -10.57   -141.12                                   
REMARK 500    GLN A 184     -126.64     48.94                                   
REMARK 500    ASN B 151     -120.87     50.86                                   
REMARK 500    TYR B 179       -8.17   -142.01                                   
REMARK 500    GLN B 184     -127.30     48.36                                   
REMARK 500    LYS C  30      -60.36   -109.56                                   
REMARK 500    ASN C 151     -120.94     53.93                                   
REMARK 500    TYR C 179       -8.92   -140.51                                   
REMARK 500    GLN C 184     -129.18     50.96                                   
REMARK 500    PRO D   9        1.74    -69.78                                   
REMARK 500    LYS D  30      -65.23   -104.87                                   
REMARK 500    ASN D  95       69.27     20.71                                   
REMARK 500    ASN D 151     -119.02     54.00                                   
REMARK 500    TYR D 179       -6.98   -141.54                                   
REMARK 500    GLN D 184     -127.64     48.43                                   
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 229  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  27   NE2                                                    
REMARK 620 2 HIS A  81   NE2  88.3                                              
REMARK 620 3 ASP A 173   OD2  88.0 108.7                                        
REMARK 620 4 HIS A 177   NE2  97.8 134.8 116.2                                  
REMARK 620 5 HOH A 233   O   170.8  89.4  84.2  90.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B 229  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  27   NE2                                                    
REMARK 620 2 HIS B  81   NE2  85.0                                              
REMARK 620 3 ASP B 173   OD2  84.4 109.1                                        
REMARK 620 4 HIS B 177   NE2  99.0 136.3 114.6                                  
REMARK 620 5 HOH B 230   O   168.2  93.8  85.0  90.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE C 229  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  27   NE2                                                    
REMARK 620 2 HIS C  81   NE2  86.5                                              
REMARK 620 3 ASP C 173   OD2  89.9 106.6                                        
REMARK 620 4 HIS C 177   NE2  95.5 134.4 118.9                                  
REMARK 620 5 HOH C 230   O   171.9  91.7  83.1  91.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE D 229  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  27   NE2                                                    
REMARK 620 2 HIS D  81   NE2  84.8                                              
REMARK 620 3 ASP D 173   OD2  85.7 109.0                                        
REMARK 620 4 HIS D 177   NE2  94.1 135.8 115.0                                  
REMARK 620 5 HOH D 234   O   169.9  94.6  84.9  93.3                            
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 229                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 229                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE C 229                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE D 229                  
DBREF  1Y67 A    2   211  UNP    Q9RUV2   SODM_DEIRA       1    210             
DBREF  1Y67 B    2   211  UNP    Q9RUV2   SODM_DEIRA       1    210             
DBREF  1Y67 C    2   211  UNP    Q9RUV2   SODM_DEIRA       1    210             
DBREF  1Y67 D    2   211  UNP    Q9RUV2   SODM_DEIRA       1    210             
SEQADV 1Y67 MET A    0  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 ALA A    1  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 LEU A  212  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 VAL A  213  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 PRO A  214  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 ARG A  215  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 GLY A  216  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 SER A  217  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 ALA A  218  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 ALA A  219  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 ALA A  220  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 LEU A  221  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 GLU A  222  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 HIS A  223  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 HIS A  224  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 HIS A  225  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 HIS A  226  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 HIS A  227  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 HIS A  228  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 MET B    0  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 ALA B    1  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 LEU B  212  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 VAL B  213  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 PRO B  214  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 ARG B  215  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 GLY B  216  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 SER B  217  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 ALA B  218  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 ALA B  219  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 ALA B  220  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 LEU B  221  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 GLU B  222  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 HIS B  223  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 HIS B  224  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 HIS B  225  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 HIS B  226  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 HIS B  227  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 HIS B  228  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 MET C    0  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 ALA C    1  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 LEU C  212  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 VAL C  213  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 PRO C  214  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 ARG C  215  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 GLY C  216  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 SER C  217  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 ALA C  218  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 ALA C  219  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 ALA C  220  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 LEU C  221  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 GLU C  222  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 HIS C  223  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 HIS C  224  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 HIS C  225  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 HIS C  226  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 HIS C  227  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 HIS C  228  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 MET D    0  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 ALA D    1  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 LEU D  212  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 VAL D  213  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 PRO D  214  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 ARG D  215  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 GLY D  216  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 SER D  217  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 ALA D  218  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 ALA D  219  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 ALA D  220  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 LEU D  221  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 GLU D  222  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 HIS D  223  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 HIS D  224  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 HIS D  225  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 HIS D  226  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 HIS D  227  UNP  Q9RUV2              EXPRESSION TAG                 
SEQADV 1Y67 HIS D  228  UNP  Q9RUV2              EXPRESSION TAG                 
SEQRES   1 A  229  MET ALA ALA TYR THR LEU PRO GLN LEU PRO TYR ALA TYR          
SEQRES   2 A  229  ASP ALA LEU GLU PRO HIS ILE ASP ALA ARG THR MET GLU          
SEQRES   3 A  229  ILE HIS HIS THR LYS HIS HIS GLN THR TYR VAL ASP ASN          
SEQRES   4 A  229  ALA ASN LYS ALA LEU GLU GLY THR GLU PHE ALA ASP LEU          
SEQRES   5 A  229  PRO VAL GLU GLN LEU ILE GLN GLN LEU ASP ARG VAL PRO          
SEQRES   6 A  229  ALA ASP LYS LYS GLY ALA LEU ARG ASN ASN ALA GLY GLY          
SEQRES   7 A  229  HIS ALA ASN HIS SER MET PHE TRP GLN ILE MET GLY GLN          
SEQRES   8 A  229  GLY GLN GLY GLN ASN GLY ALA ASN GLN PRO SER GLY GLU          
SEQRES   9 A  229  LEU LEU ASP ALA ILE ASN SER ALA PHE GLY SER PHE ASP          
SEQRES  10 A  229  ALA PHE LYS GLN LYS PHE GLU ASP ALA ALA LYS THR ARG          
SEQRES  11 A  229  PHE GLY SER GLY TRP ALA TRP LEU VAL VAL LYS ASP GLY          
SEQRES  12 A  229  LYS LEU ASP VAL VAL SER THR ALA ASN GLN ASP ASN PRO          
SEQRES  13 A  229  LEU MET GLY GLU ALA ILE ALA GLY VAL SER GLY THR PRO          
SEQRES  14 A  229  ILE LEU GLY VAL ASP VAL TRP GLU HIS ALA TYR TYR LEU          
SEQRES  15 A  229  ASN TYR GLN ASN ARG ARG PRO ASP TYR LEU ALA ALA PHE          
SEQRES  16 A  229  TRP ASN VAL VAL ASN TRP ASP GLU VAL SER LYS ARG TYR          
SEQRES  17 A  229  ALA ALA ALA LYS LEU VAL PRO ARG GLY SER ALA ALA ALA          
SEQRES  18 A  229  LEU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 B  229  MET ALA ALA TYR THR LEU PRO GLN LEU PRO TYR ALA TYR          
SEQRES   2 B  229  ASP ALA LEU GLU PRO HIS ILE ASP ALA ARG THR MET GLU          
SEQRES   3 B  229  ILE HIS HIS THR LYS HIS HIS GLN THR TYR VAL ASP ASN          
SEQRES   4 B  229  ALA ASN LYS ALA LEU GLU GLY THR GLU PHE ALA ASP LEU          
SEQRES   5 B  229  PRO VAL GLU GLN LEU ILE GLN GLN LEU ASP ARG VAL PRO          
SEQRES   6 B  229  ALA ASP LYS LYS GLY ALA LEU ARG ASN ASN ALA GLY GLY          
SEQRES   7 B  229  HIS ALA ASN HIS SER MET PHE TRP GLN ILE MET GLY GLN          
SEQRES   8 B  229  GLY GLN GLY GLN ASN GLY ALA ASN GLN PRO SER GLY GLU          
SEQRES   9 B  229  LEU LEU ASP ALA ILE ASN SER ALA PHE GLY SER PHE ASP          
SEQRES  10 B  229  ALA PHE LYS GLN LYS PHE GLU ASP ALA ALA LYS THR ARG          
SEQRES  11 B  229  PHE GLY SER GLY TRP ALA TRP LEU VAL VAL LYS ASP GLY          
SEQRES  12 B  229  LYS LEU ASP VAL VAL SER THR ALA ASN GLN ASP ASN PRO          
SEQRES  13 B  229  LEU MET GLY GLU ALA ILE ALA GLY VAL SER GLY THR PRO          
SEQRES  14 B  229  ILE LEU GLY VAL ASP VAL TRP GLU HIS ALA TYR TYR LEU          
SEQRES  15 B  229  ASN TYR GLN ASN ARG ARG PRO ASP TYR LEU ALA ALA PHE          
SEQRES  16 B  229  TRP ASN VAL VAL ASN TRP ASP GLU VAL SER LYS ARG TYR          
SEQRES  17 B  229  ALA ALA ALA LYS LEU VAL PRO ARG GLY SER ALA ALA ALA          
SEQRES  18 B  229  LEU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 C  229  MET ALA ALA TYR THR LEU PRO GLN LEU PRO TYR ALA TYR          
SEQRES   2 C  229  ASP ALA LEU GLU PRO HIS ILE ASP ALA ARG THR MET GLU          
SEQRES   3 C  229  ILE HIS HIS THR LYS HIS HIS GLN THR TYR VAL ASP ASN          
SEQRES   4 C  229  ALA ASN LYS ALA LEU GLU GLY THR GLU PHE ALA ASP LEU          
SEQRES   5 C  229  PRO VAL GLU GLN LEU ILE GLN GLN LEU ASP ARG VAL PRO          
SEQRES   6 C  229  ALA ASP LYS LYS GLY ALA LEU ARG ASN ASN ALA GLY GLY          
SEQRES   7 C  229  HIS ALA ASN HIS SER MET PHE TRP GLN ILE MET GLY GLN          
SEQRES   8 C  229  GLY GLN GLY GLN ASN GLY ALA ASN GLN PRO SER GLY GLU          
SEQRES   9 C  229  LEU LEU ASP ALA ILE ASN SER ALA PHE GLY SER PHE ASP          
SEQRES  10 C  229  ALA PHE LYS GLN LYS PHE GLU ASP ALA ALA LYS THR ARG          
SEQRES  11 C  229  PHE GLY SER GLY TRP ALA TRP LEU VAL VAL LYS ASP GLY          
SEQRES  12 C  229  LYS LEU ASP VAL VAL SER THR ALA ASN GLN ASP ASN PRO          
SEQRES  13 C  229  LEU MET GLY GLU ALA ILE ALA GLY VAL SER GLY THR PRO          
SEQRES  14 C  229  ILE LEU GLY VAL ASP VAL TRP GLU HIS ALA TYR TYR LEU          
SEQRES  15 C  229  ASN TYR GLN ASN ARG ARG PRO ASP TYR LEU ALA ALA PHE          
SEQRES  16 C  229  TRP ASN VAL VAL ASN TRP ASP GLU VAL SER LYS ARG TYR          
SEQRES  17 C  229  ALA ALA ALA LYS LEU VAL PRO ARG GLY SER ALA ALA ALA          
SEQRES  18 C  229  LEU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 D  229  MET ALA ALA TYR THR LEU PRO GLN LEU PRO TYR ALA TYR          
SEQRES   2 D  229  ASP ALA LEU GLU PRO HIS ILE ASP ALA ARG THR MET GLU          
SEQRES   3 D  229  ILE HIS HIS THR LYS HIS HIS GLN THR TYR VAL ASP ASN          
SEQRES   4 D  229  ALA ASN LYS ALA LEU GLU GLY THR GLU PHE ALA ASP LEU          
SEQRES   5 D  229  PRO VAL GLU GLN LEU ILE GLN GLN LEU ASP ARG VAL PRO          
SEQRES   6 D  229  ALA ASP LYS LYS GLY ALA LEU ARG ASN ASN ALA GLY GLY          
SEQRES   7 D  229  HIS ALA ASN HIS SER MET PHE TRP GLN ILE MET GLY GLN          
SEQRES   8 D  229  GLY GLN GLY GLN ASN GLY ALA ASN GLN PRO SER GLY GLU          
SEQRES   9 D  229  LEU LEU ASP ALA ILE ASN SER ALA PHE GLY SER PHE ASP          
SEQRES  10 D  229  ALA PHE LYS GLN LYS PHE GLU ASP ALA ALA LYS THR ARG          
SEQRES  11 D  229  PHE GLY SER GLY TRP ALA TRP LEU VAL VAL LYS ASP GLY          
SEQRES  12 D  229  LYS LEU ASP VAL VAL SER THR ALA ASN GLN ASP ASN PRO          
SEQRES  13 D  229  LEU MET GLY GLU ALA ILE ALA GLY VAL SER GLY THR PRO          
SEQRES  14 D  229  ILE LEU GLY VAL ASP VAL TRP GLU HIS ALA TYR TYR LEU          
SEQRES  15 D  229  ASN TYR GLN ASN ARG ARG PRO ASP TYR LEU ALA ALA PHE          
SEQRES  16 D  229  TRP ASN VAL VAL ASN TRP ASP GLU VAL SER LYS ARG TYR          
SEQRES  17 D  229  ALA ALA ALA LYS LEU VAL PRO ARG GLY SER ALA ALA ALA          
SEQRES  18 D  229  LEU GLU HIS HIS HIS HIS HIS HIS                              
HET     FE  A 229       1                                                       
HET     FE  B 229       1                                                       
HET     FE  C 229       1                                                       
HET     FE  D 229       1                                                       
HETNAM      FE FE (III) ION                                                     
FORMUL   5   FE    4(FE 3+)                                                     
FORMUL   9  HOH   *396(H2 O)                                                    
HELIX    1   1 ASP A   20  LYS A   30  1                                  11    
HELIX    2   2 LYS A   30  GLU A   44  1                                  15    
HELIX    3   3 PRO A   52  ILE A   57  1                                   6    
HELIX    4   4 PRO A   64  ILE A   87  1                                  24    
HELIX    5   5 SER A  101  GLY A  113  1                                  13    
HELIX    6   6 SER A  114  ARG A  129  1                                  16    
HELIX    7   7 ASN A  154  MET A  157  5                                   4    
HELIX    8   8 GLY A  158  GLY A  163  1                                   6    
HELIX    9   9 TRP A  175  ALA A  178  5                                   4    
HELIX   10  10 TYR A  179  GLN A  184  1                                   6    
HELIX   11  11 ARG A  186  TRP A  195  1                                  10    
HELIX   12  12 ASN A  199  LEU A  212  1                                  14    
HELIX   13  13 ASP B   20  LYS B   30  1                                  11    
HELIX   14  14 LYS B   30  GLU B   44  1                                  15    
HELIX   15  15 PRO B   52  ILE B   57  1                                   6    
HELIX   16  16 LYS B   67  ILE B   87  1                                  21    
HELIX   17  17 SER B  101  GLY B  113  1                                  13    
HELIX   18  18 SER B  114  THR B  128  1                                  15    
HELIX   19  19 ASN B  154  MET B  157  5                                   4    
HELIX   20  20 GLY B  158  GLY B  163  1                                   6    
HELIX   21  21 TRP B  175  ALA B  178  5                                   4    
HELIX   22  22 TYR B  179  GLN B  184  1                                   6    
HELIX   23  23 ARG B  186  TRP B  195  1                                  10    
HELIX   24  24 ASN B  199  LYS B  211  1                                  13    
HELIX   25  25 ASP C   20  LYS C   30  1                                  11    
HELIX   26  26 LYS C   30  GLU C   44  1                                  15    
HELIX   27  27 PRO C   52  ILE C   57  1                                   6    
HELIX   28  28 PRO C   64  ILE C   87  1                                  24    
HELIX   29  29 SER C  101  GLY C  113  1                                  13    
HELIX   30  30 SER C  114  ARG C  129  1                                  16    
HELIX   31  31 ASN C  154  MET C  157  5                                   4    
HELIX   32  32 GLY C  158  GLY C  163  1                                   6    
HELIX   33  33 TRP C  175  ALA C  178  5                                   4    
HELIX   34  34 TYR C  179  GLN C  184  1                                   6    
HELIX   35  35 ARG C  186  TRP C  195  1                                  10    
HELIX   36  36 ASN C  199  LEU C  212  1                                  14    
HELIX   37  37 ASP D   20  LYS D   30  1                                  11    
HELIX   38  38 LYS D   30  GLU D   44  1                                  15    
HELIX   39  39 PRO D   52  ILE D   57  1                                   6    
HELIX   40  40 PRO D   64  ASP D   66  5                                   3    
HELIX   41  41 LYS D   67  ILE D   87  1                                  21    
HELIX   42  42 SER D  101  GLY D  113  1                                  13    
HELIX   43  43 SER D  114  ARG D  129  1                                  16    
HELIX   44  44 ASN D  154  MET D  157  5                                   4    
HELIX   45  45 GLY D  158  GLY D  163  1                                   6    
HELIX   46  46 TRP D  175  ALA D  178  5                                   4    
HELIX   47  47 TYR D  179  GLN D  184  1                                   6    
HELIX   48  48 ARG D  186  TRP D  195  1                                  10    
HELIX   49  49 ASN D  196  VAL D  198  5                                   3    
HELIX   50  50 ASN D  199  LYS D  211  1                                  13    
SHEET    1   A 3 LYS A 143  ALA A 150  0                                        
SHEET    2   A 3 GLY A 133  LYS A 140 -1  N  LYS A 140   O  LYS A 143           
SHEET    3   A 3 THR A 167  ASP A 173 -1  O  ILE A 169   N  LEU A 137           
SHEET    1   B 3 LYS A 143  ALA A 150  0                                        
SHEET    2   B 3 GLY A 133  LYS A 140 -1  N  TRP A 136   O  VAL A 147           
SHEET    3   B 3 THR A 167  ASP A 173 -1  O  THR A 167   N  VAL A 139           
SHEET    1   C 3 LYS A 143  ALA A 150  0                                        
SHEET    2   C 3 GLY A 133  LYS A 140 -1  N  LYS A 140   O  LYS A 143           
SHEET    3   C 3 THR A 167  ASP A 173 -1  O  ILE A 169   N  LEU A 137           
SHEET    1   D 3 LYS A 143  ALA A 150  0                                        
SHEET    2   D 3 GLY A 133  LYS A 140 -1  N  TRP A 136   O  VAL A 147           
SHEET    3   D 3 THR A 167  ASP A 173 -1  O  LEU A 170   N  LEU A 137           
LINK         NE2 HIS A  27                FE    FE A 229     1555   1555  2.12  
LINK         NE2 HIS A  81                FE    FE A 229     1555   1555  2.19  
LINK         OD2 ASP A 173                FE    FE A 229     1555   1555  1.93  
LINK         NE2 HIS A 177                FE    FE A 229     1555   1555  2.20  
LINK         NE2 HIS B  27                FE    FE B 229     1555   1555  2.18  
LINK         NE2 HIS B  81                FE    FE B 229     1555   1555  2.24  
LINK         OD2 ASP B 173                FE    FE B 229     1555   1555  1.98  
LINK         NE2 HIS B 177                FE    FE B 229     1555   1555  2.16  
LINK         NE2 HIS C  27                FE    FE C 229     1555   1555  2.17  
LINK         NE2 HIS C  81                FE    FE C 229     1555   1555  2.22  
LINK         OD2 ASP C 173                FE    FE C 229     1555   1555  1.98  
LINK         NE2 HIS C 177                FE    FE C 229     1555   1555  2.11  
LINK         NE2 HIS D  27                FE    FE D 229     1555   1555  2.20  
LINK         NE2 HIS D  81                FE    FE D 229     1555   1555  2.20  
LINK         OD2 ASP D 173                FE    FE D 229     1555   1555  1.99  
LINK         NE2 HIS D 177                FE    FE D 229     1555   1555  2.15  
LINK        FE    FE A 229                 O   HOH A 233     1555   1555  2.27  
LINK        FE    FE B 229                 O   HOH B 230     1555   1555  2.19  
LINK        FE    FE C 229                 O   HOH C 230     1555   1555  2.15  
LINK        FE    FE D 229                 O   HOH D 234     1555   1555  1.97  
CISPEP   1 GLU A   16    PRO A   17          0        -2.64                     
CISPEP   2 GLU B   16    PRO B   17          0         0.75                     
CISPEP   3 GLU C   16    PRO C   17          0        -3.23                     
CISPEP   4 GLU D   16    PRO D   17          0        -2.23                     
SITE     1 AC1  5 HIS A  27  HIS A  81  ASP A 173  HIS A 177                    
SITE     2 AC1  5 HOH A 233                                                     
SITE     1 AC2  5 HIS B  27  HIS B  81  ASP B 173  HIS B 177                    
SITE     2 AC2  5 HOH B 230                                                     
SITE     1 AC3  5 HIS C  27  HIS C  81  ASP C 173  HIS C 177                    
SITE     2 AC3  5 HOH C 230                                                     
SITE     1 AC4  5 HIS D  27  HIS D  81  ASP D 173  HIS D 177                    
SITE     2 AC4  5 HOH D 234                                                     
CRYST1   43.801   87.922  116.198  90.00  91.14  90.00 P 1 21 1      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      0.022831  0.000000  0.000454        0.00000                         
SCALE2      0.000000  0.011374  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008608        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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