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Database: PDB
Entry: 1MY6
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HEADER    OXIDOREDUCTASE                          03-OCT-02   1MY6              
TITLE     THE 1.6 A STRUCTURE OF FE-SUPEROXIDE DISMUTASE FROM THE               
TITLE    2 THERMOPHILIC CYANOBACTERIUM THERMOSYNECHOCOCCUS ELONGATUS            
TITLE    3 : CORRELATION OF EPR AND STRUCTURAL CHARACTERISTICS                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: IRON (III) SUPEROXIDE DISMUTASE;                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE   3 ORGANISM_TAXID: 146786;                                              
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    IRON SPEROXIDE DISMUTASE, THERMOPHILE, REACTIVE OXYGEN                
KEYWDS   2 SPECIES, CYANOBACTERIA, THERMOSYNECHOCOCCUS,                         
KEYWDS   3 THERMOSYNECHOCOCCUS ELONGATUS, SUPEROXIDE DISMUTASE, SOD,            
KEYWDS   4 FESOD, IRON(III) SUPEROXIDE DISMUTASE, OXIDOREDUCTASE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.M.YOSHIDA,D.CASCIO,M.R.SAWAYA,T.O.YEATES,C.A.KERFELD                
REVDAT   3   24-FEB-09 1MY6    1       VERSN                                    
REVDAT   2   23-SEP-03 1MY6    1       JRNL                                     
REVDAT   1   29-JUL-03 1MY6    0                                                
JRNL        AUTH   C.A.KERFELD,S.YOSHIDA,K.T.TRAN,T.O.YEATES,D.CASCIO,          
JRNL        AUTH 2 H.BOTTIN,C.BERTHOMIEU,M.SUGIURA,A.BOUSSAC                    
JRNL        TITL   THE 1.6 A RESOLUTION STRUCTURE OF FE-SUPEROXIDE              
JRNL        TITL 2 DISMUTASE FROM THE THERMOPHILIC CYANOBACTERIUM               
JRNL        TITL 3 THERMOSYNECHOCOCCUS ELONGATUS.                               
JRNL        REF    J.BIOL.INORG.CHEM.            V.   8   707 2003              
JRNL        REFN                   ISSN 0949-8257                               
JRNL        PMID   12827458                                                     
JRNL        DOI    10.1007/S00775-003-0469-0                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.19                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 70.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 53851                          
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) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.232                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2896                            
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) : 1.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4063                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1590                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 215                          
REMARK   3   BIN FREE R VALUE                    : 0.2500                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3128                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 565                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.67                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.64000                                              
REMARK   3    B22 (A**2) : -1.54000                                             
REMARK   3    B33 (A**2) : 0.48000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.82000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.136         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.101         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.065         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.748         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.923                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3224 ; 0.016 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2744 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4396 ; 1.623 ; 1.914       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6392 ; 0.903 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   394 ; 6.880 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   462 ; 0.107 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3686 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   686 ; 0.011 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   739 ; 0.231 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3169 ; 0.247 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1715 ; 0.087 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   387 ; 0.213 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     7 ; 0.177 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    30 ; 0.297 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    35 ; 0.206 ; 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):  1966 ; 1.312 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3138 ; 1.910 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1258 ; 2.616 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1258 ; 3.693 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  3224 ; 1.522 ; 2.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   567 ; 3.671 ; 2.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  3130 ; 2.124 ; 2.000       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS. REFINED WITH ANISOTROPIC TEMPERATURE              
REMARK   3  FACTORS. NCS RESTRAINTS WERE NOT APPLIED ON THE 2 MOLECULES IN      
REMARK   3  THE ASYMMETRIC UNIT.                                                
REMARK   4                                                                      
REMARK   4 1MY6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-OCT-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB017303.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-JUN-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X8C                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.100                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53851                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 70.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY                : 16.180                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.3500                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.28                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.32000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.32000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.350                              
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: FESOD FROM E.COLI, PDB ENTRY 1ISC                    
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP,           
REMARK 280  293.15K, 0.1M SODIUM CACODYLATE PH 6.7, 0.2M MAGNESIUM ACETATE      
REMARK 280  TETRAHYDRATE, 20% PEG 6K                                            
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       31.82200            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1770 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
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 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     ALA A   199                                                      
REMARK 465     ALA B   199                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  3249     O    HOH A  3511              1.84            
REMARK 500   N    ALA A     1     O    HOH A  3033              2.01            
REMARK 500   O    HOH A  3083     O    HOH A  3497              2.04            
REMARK 500   O    HOH A  3079     O    HOH A  3562              2.04            
REMARK 500   O    HOH A  3279     O    HOH A  3299              2.08            
REMARK 500   O    HOH B  3239     O    HOH B  3304              2.08            
REMARK 500   O    HIS A    79     NE1  TRP A    83              2.09            
REMARK 500   NE   ARG A    58     O    HOH A  3254              2.15            
REMARK 500   ND2  ASN A    38     O    HOH A  3048              2.17            
REMARK 500   O    HOH A  3306     O    HOH A  3543              2.18            
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   O    HOH B  3407     O    HOH B  3508     2557     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  10   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASP A  45   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASN A 148   CB  -  CA  -  C   ANGL. DEV. =  13.0 DEGREES          
REMARK 500    ASN A 148   N   -  CA  -  CB  ANGL. DEV. = -13.9 DEGREES          
REMARK 500    ASP B  45   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP B  50   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 145     -113.49     60.85                                   
REMARK 500    GLN A 172     -123.99     39.42                                   
REMARK 500    ASN B 145     -112.73     56.03                                   
REMARK 500    GLN B 172     -125.73     44.72                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASP B   45     THR B   46                 -146.68                    
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 200  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 161   OD2                                                    
REMARK 620 2 HIS A  27   NE2  84.9                                              
REMARK 620 3 HIS A  79   NE2 109.3  92.9                                        
REMARK 620 4 HIS A 165   NE2 125.3  94.5 125.3                                  
REMARK 620 5 HOH A3001   O    90.7 175.5  88.0  88.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B 200  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 161   OD2                                                    
REMARK 620 2 HIS B  27   NE2  87.8                                              
REMARK 620 3 HIS B  79   NE2 109.5  94.8                                        
REMARK 620 4 HIS B 165   NE2 123.8  88.0 126.7                                  
REMARK 620 5 HOH B3085   O    89.8 176.6  88.3  91.3                            
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 200                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 200                  
DBREF  1MY6 A    1   199  UNP    Q8DIR2   Q8DIR2_SYNEL     2    200             
DBREF  1MY6 B    1   199  UNP    Q8DIR2   Q8DIR2_SYNEL     2    200             
SEQRES   1 A  199  ALA PHE VAL GLN GLU PRO LEU PRO PHE ASP PRO GLY ALA          
SEQRES   2 A  199  LEU GLU PRO TYR GLY MET SER ALA LYS THR LEU GLU PHE          
SEQRES   3 A  199  HIS TYR GLY LYS HIS HIS LYS GLY TYR VAL ASP ASN LEU          
SEQRES   4 A  199  ASN LYS LEU THR GLN ASP THR GLU LEU ALA ASP LYS SER          
SEQRES   5 A  199  LEU GLU ASP VAL ILE ARG THR THR TYR GLY ASP ALA ALA          
SEQRES   6 A  199  LYS VAL GLY ILE PHE ASN ASN ALA ALA GLN VAL TRP ASN          
SEQRES   7 A  199  HIS THR PHE PHE TRP ASN SER LEU LYS PRO GLY GLY GLY          
SEQRES   8 A  199  GLY VAL PRO THR GLY ASP VAL ALA ALA ARG ILE ASN SER          
SEQRES   9 A  199  ALA PHE GLY SER TYR ASP GLU PHE LYS ALA GLN PHE LYS          
SEQRES  10 A  199  ASN ALA ALA ALA THR GLN PHE GLY SER GLY TRP ALA TRP          
SEQRES  11 A  199  LEU VAL LEU GLU ALA GLY THR LEU LYS VAL THR LYS THR          
SEQRES  12 A  199  ALA ASN ALA GLU ASN PRO LEU VAL HIS GLY GLN VAL PRO          
SEQRES  13 A  199  LEU LEU THR ILE ASP VAL TRP GLU HIS ALA TYR TYR LEU          
SEQRES  14 A  199  ASP TYR GLN ASN ARG ARG PRO ASP PHE ILE ASP ASN PHE          
SEQRES  15 A  199  LEU ASN GLN LEU VAL ASN TRP ASP PHE VAL ALA LYS ASN          
SEQRES  16 A  199  LEU ALA ALA ALA                                              
SEQRES   1 B  199  ALA PHE VAL GLN GLU PRO LEU PRO PHE ASP PRO GLY ALA          
SEQRES   2 B  199  LEU GLU PRO TYR GLY MET SER ALA LYS THR LEU GLU PHE          
SEQRES   3 B  199  HIS TYR GLY LYS HIS HIS LYS GLY TYR VAL ASP ASN LEU          
SEQRES   4 B  199  ASN LYS LEU THR GLN ASP THR GLU LEU ALA ASP LYS SER          
SEQRES   5 B  199  LEU GLU ASP VAL ILE ARG THR THR TYR GLY ASP ALA ALA          
SEQRES   6 B  199  LYS VAL GLY ILE PHE ASN ASN ALA ALA GLN VAL TRP ASN          
SEQRES   7 B  199  HIS THR PHE PHE TRP ASN SER LEU LYS PRO GLY GLY GLY          
SEQRES   8 B  199  GLY VAL PRO THR GLY ASP VAL ALA ALA ARG ILE ASN SER          
SEQRES   9 B  199  ALA PHE GLY SER TYR ASP GLU PHE LYS ALA GLN PHE LYS          
SEQRES  10 B  199  ASN ALA ALA ALA THR GLN PHE GLY SER GLY TRP ALA TRP          
SEQRES  11 B  199  LEU VAL LEU GLU ALA GLY THR LEU LYS VAL THR LYS THR          
SEQRES  12 B  199  ALA ASN ALA GLU ASN PRO LEU VAL HIS GLY GLN VAL PRO          
SEQRES  13 B  199  LEU LEU THR ILE ASP VAL TRP GLU HIS ALA TYR TYR LEU          
SEQRES  14 B  199  ASP TYR GLN ASN ARG ARG PRO ASP PHE ILE ASP ASN PHE          
SEQRES  15 B  199  LEU ASN GLN LEU VAL ASN TRP ASP PHE VAL ALA LYS ASN          
SEQRES  16 B  199  LEU ALA ALA ALA                                              
HET     FE  A 200       1                                                       
HET     FE  B 200       1                                                       
HETNAM      FE FE (III) ION                                                     
FORMUL   3   FE    2(FE 3+)                                                     
FORMUL   5  HOH   *565(H2 O)                                                    
HELIX    1   1 LEU A   14  GLY A   18  5                                   5    
HELIX    2   2 SER A   20  LYS A   30  1                                  11    
HELIX    3   3 LYS A   30  GLN A   44  1                                  15    
HELIX    4   4 THR A   46  LYS A   51  5                                   6    
HELIX    5   5 SER A   52  TYR A   61  1                                  10    
HELIX    6   6 LYS A   66  SER A   85  1                                  20    
HELIX    7   7 THR A   95  GLY A  107  1                                  13    
HELIX    8   8 SER A  108  GLN A  123  1                                  16    
HELIX    9   9 ASN A  148  GLY A  153  5                                   6    
HELIX   10  10 TRP A  163  ALA A  166  5                                   4    
HELIX   11  11 TYR A  167  GLN A  172  1                                   6    
HELIX   12  12 ARG A  174  LEU A  186  1                                  13    
HELIX   13  13 ASN A  188  ALA A  198  1                                  11    
HELIX   14  14 LEU B   14  GLY B   18  5                                   5    
HELIX   15  15 SER B   20  LYS B   30  1                                  11    
HELIX   16  16 LYS B   30  GLN B   44  1                                  15    
HELIX   17  17 THR B   46  LYS B   51  5                                   6    
HELIX   18  18 SER B   52  TYR B   61  1                                  10    
HELIX   19  19 LYS B   66  SER B   85  1                                  20    
HELIX   20  20 THR B   95  GLY B  107  1                                  13    
HELIX   21  21 SER B  108  GLN B  123  1                                  16    
HELIX   22  22 ASN B  148  GLY B  153  5                                   6    
HELIX   23  23 TRP B  163  ALA B  166  5                                   4    
HELIX   24  24 TYR B  167  GLN B  172  1                                   6    
HELIX   25  25 ARG B  174  LEU B  186  1                                  13    
HELIX   26  26 ASN B  188  ALA B  198  1                                  11    
SHEET    1   A 3 THR A 137  ALA A 144  0                                        
SHEET    2   A 3 GLY A 127  GLU A 134 -1  N  GLU A 134   O  THR A 137           
SHEET    3   A 3 VAL A 155  ASP A 161 -1  O  LEU A 157   N  LEU A 131           
SHEET    1   B 3 THR B 137  ALA B 144  0                                        
SHEET    2   B 3 GLY B 127  GLU B 134 -1  N  TRP B 130   O  THR B 141           
SHEET    3   B 3 VAL B 155  ASP B 161 -1  O  LEU B 157   N  LEU B 131           
LINK        FE    FE A 200                 OD2 ASP A 161     1555   1555  1.94  
LINK        FE    FE A 200                 NE2 HIS A  27     1555   1555  2.19  
LINK        FE    FE A 200                 NE2 HIS A  79     1555   1555  2.07  
LINK        FE    FE A 200                 NE2 HIS A 165     1555   1555  2.12  
LINK        FE    FE B 200                 OD2 ASP B 161     1555   1555  1.92  
LINK        FE    FE B 200                 NE2 HIS B  27     1555   1555  2.16  
LINK        FE    FE B 200                 NE2 HIS B  79     1555   1555  2.12  
LINK        FE    FE B 200                 NE2 HIS B 165     1555   1555  2.06  
LINK        FE    FE A 200                 O   HOH A3001     1555   1555  2.26  
LINK        FE    FE B 200                 O   HOH B3085     1555   1555  2.18  
SITE     1 AC1  5 HIS A  27  HIS A  79  ASP A 161  HIS A 165                    
SITE     2 AC1  5 HOH A3001                                                     
SITE     1 AC2  5 HIS B  27  HIS B  79  ASP B 161  HIS B 165                    
SITE     2 AC2  5 HOH B3085                                                     
CRYST1   51.749   63.644   74.709  90.00 110.45  90.00 P 1 21 1      4          
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      0.019324  0.000000  0.007206        0.00000                         
SCALE2      0.000000  0.015712  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014286        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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