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Database: PDB
Entry: 3ELN
LinkDB: 3ELN
Original site: 3ELN 
HEADER    OXIDOREDUCTASE                          22-SEP-08   3ELN              
TITLE     A PUTATIVE FE2+-BOUND PERSULFENATE INTERMEDIATE IN CYSTEINE           
TITLE    2 DIOXYGENASE                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYSTEINE DIOXYGENASE TYPE 1;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CYSTEINE DIOXYGENASE TYPE I, CDO-I, CDO;                    
COMPND   5 EC: 1.13.11.20;                                                      
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;                                 
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: CDO1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET32A                                
KEYWDS    PEROXYSULFENATE, NON-HEME DIOXYGENASES, FE2+ METALLOENZYME, CYSTEINE, 
KEYWDS   2 TAURINE, THIOETHER, DIOXYGENASE, IRON, METAL-BINDING,                
KEYWDS   3 OXIDOREDUCTASE, PHOSPHOPROTEIN, THIOETHER BOND                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.R.SIMMONS,M.H.STIPANUK,P.A.KARPLUS                                  
REVDAT   4   24-JUL-19 3ELN    1       REMARK                                   
REVDAT   3   24-FEB-09 3ELN    1       VERSN                                    
REVDAT   2   11-NOV-08 3ELN    1       JRNL                                     
REVDAT   1   21-OCT-08 3ELN    0                                                
JRNL        AUTH   C.R.SIMMONS,K.KRISHNAMOORTHY,S.L.GRANETT,D.J.SCHULLER,       
JRNL        AUTH 2 J.E.DOMINY,T.P.BEGLEY,M.H.STIPANUK,P.A.KARPLUS               
JRNL        TITL   A PUTATIVE FE2+-BOUND PERSULFENATE INTERMEDIATE IN CYSTEINE  
JRNL        TITL 2 DIOXYGENASE.                                                 
JRNL        REF    BIOCHEMISTRY                  V.  47 11390 2008              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   18847220                                                     
JRNL        DOI    10.1021/BI801546N                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.42 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0069                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.42                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.68                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 37576                          
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) : 0.135                           
REMARK   3   R VALUE            (WORKING SET) : 0.133                           
REMARK   3   FREE R VALUE                     : 0.177                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1989                            
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) : 1.42                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2717                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.97                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1340                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 149                          
REMARK   3   BIN FREE R VALUE                    : 0.2050                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1519                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 352                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.19                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.59000                                             
REMARK   3    B22 (A**2) : -0.59000                                             
REMARK   3    B33 (A**2) : 1.18000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.060         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.058         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.032         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.724         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.978                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.961                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1653 ; 0.016 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  1129 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2255 ; 1.605 ; 1.941       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2761 ; 1.823 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   212 ; 6.047 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    89 ;39.867 ;24.045       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   292 ;12.832 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;17.716 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   242 ; 0.102 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1866 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   346 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):   975 ; 1.752 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   390 ; 0.524 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1589 ; 2.762 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   678 ; 3.840 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   653 ; 5.640 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2782 ; 1.556 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   353 ;18.640 ; 8.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2730 ; 6.303 ; 8.000       
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   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3ELN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-SEP-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000049477.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-MAR-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 3                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9801                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39648                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.420                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.42                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.45                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PURIFIED ENZYME WAS CONCENTRATED TO ~8   
REMARK 280  MG/ML AND THEN ADDED INTO A CRYSTALLIZATION SCREEN CONTAINING       
REMARK 280  0.1 M TRI-SODIUM CITRATE PH=5.6, 24-34% PEG 4K, AND 0.1-0.25 M      
REMARK 280  AMMONIUM ACETATE. 1.5L OF PROTEIN SOLUTION WAS ADDED TO EACH        
REMARK 280  WELL AND MIXED WITH AN EQUIVALENT VOLUME OF RESERVOIR SOLUTION.,    
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K, PH 5.6             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.09500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       28.76150            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       28.76150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       91.64250            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       28.76150            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       28.76150            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       30.54750            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       28.76150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       28.76150            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       91.64250            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       28.76150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       28.76150            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       30.54750            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       61.09500            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     PHE A   191                                                      
REMARK 465     THR A   192                                                      
REMARK 465     THR A   193                                                      
REMARK 465     SER A   194                                                      
REMARK 465     GLY A   195                                                      
REMARK 465     SER A   196                                                      
REMARK 465     LEU A   197                                                      
REMARK 465     GLU A   198                                                      
REMARK 465     ASN A   199                                                      
REMARK 465     ASN A   200                                                      
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   806     O    HOH A   911              1.64            
REMARK 500   O    HOH A   890     O    HOH A   898              1.78            
REMARK 500   O    HOH A   889     O    HOH A   890              1.82            
REMARK 500   O    HOH A   600     O    HOH A   844              1.86            
REMARK 500   SG   CYS A    93     CE2  TYR A   157              1.90            
REMARK 500   O    HOH A   821     O    HOH A   868              1.90            
REMARK 500   O    HOH A   758     O    HOH A   907              1.94            
REMARK 500   O    HOH A   766     O    HOH A   894              1.95            
REMARK 500   OD1  ASN A   134     O    HOH A   884              2.08            
REMARK 500   ND2  ASN A   134     O    HOH A   771              2.08            
REMARK 500   OD1  ASN A   175     O    HOH A   864              2.13            
REMARK 500   O    HOH A   868     O    HOH A   927              2.13            
REMARK 500   O    HOH A   770     O    HOH A   791              2.19            
REMARK 500   ND1  HIS A   173     O    HOH A   903              2.19            
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 128       -9.56     77.69                                   
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                             FE2 A 501  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  86   NE2                                                    
REMARK 620 2 HIS A  88   NE2 101.0                                              
REMARK 620 3 HIS A 140   NE2  96.7  92.1                                        
REMARK 620 4 2CO A 580   SG  102.5 154.9  93.8                                  
REMARK 620 5 2CO A 580   N    88.7  92.8 171.9  79.1                            
REMARK 620 6 2CO A 580   OD  136.2 111.7 109.9  43.6  62.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2CO A 580                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2B5H   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2GH2   RELATED DB: PDB                                   
DBREF  3ELN A    1   200  UNP    P21816   CDO1_RAT         1    200             
SEQRES   1 A  200  MET GLU ARG THR GLU LEU LEU LYS PRO ARG THR LEU ALA          
SEQRES   2 A  200  ASP LEU ILE ARG ILE LEU HIS GLU LEU PHE ALA GLY ASP          
SEQRES   3 A  200  GLU VAL ASN VAL GLU GLU VAL GLN ALA VAL LEU GLU ALA          
SEQRES   4 A  200  TYR GLU SER ASN PRO ALA GLU TRP ALA LEU TYR ALA LYS          
SEQRES   5 A  200  PHE ASP GLN TYR ARG TYR THR ARG ASN LEU VAL ASP GLN          
SEQRES   6 A  200  GLY ASN GLY LYS PHE ASN LEU MET ILE LEU CYS TRP GLY          
SEQRES   7 A  200  GLU GLY HIS GLY SER SER ILE HIS ASP HIS THR ASP SER          
SEQRES   8 A  200  HIS CYS PHE LEU LYS LEU LEU GLN GLY ASN LEU LYS GLU          
SEQRES   9 A  200  THR LEU PHE ASP TRP PRO ASP LYS LYS SER ASN GLU MET          
SEQRES  10 A  200  ILE LYS LYS SER GLU ARG THR LEU ARG GLU ASN GLN CYS          
SEQRES  11 A  200  ALA TYR ILE ASN ASP SER ILE GLY LEU HIS ARG VAL GLU          
SEQRES  12 A  200  ASN VAL SER HIS THR GLU PRO ALA VAL SER LEU HIS LEU          
SEQRES  13 A  200  TYR SER PRO PRO PHE ASP THR CYS HIS ALA PHE ASP GLN          
SEQRES  14 A  200  ARG THR GLY HIS LYS ASN LYS VAL THR MET THR PHE HIS          
SEQRES  15 A  200  SER LYS PHE GLY ILE ARG THR PRO PHE THR THR SER GLY          
SEQRES  16 A  200  SER LEU GLU ASN ASN                                          
HET    FE2  A 501       1                                                       
HET    2CO  A 580       9                                                       
HETNAM     FE2 FE (II) ION                                                      
HETNAM     2CO S-HYDROPEROXYCYSTEINE                                            
FORMUL   2  FE2    FE 2+                                                        
FORMUL   3  2CO    C3 H7 N O4 S                                                 
FORMUL   4  HOH   *352(H2 O)                                                    
HELIX    1   1 THR A   11  PHE A   23  1                                  13    
HELIX    2   2 ASN A   29  TYR A   40  1                                  12    
HELIX    3   3 ASN A   43  ALA A   48  1                                   6    
HELIX    4   4 LEU A   49  ALA A   51  5                                   3    
HELIX    5   5 GLN A   65  LYS A   69  5                                   5    
SHEET    1   A 7 CYS A 130  ILE A 133  0                                        
SHEET    2   A 7 HIS A  92  GLN A  99 -1  N  LEU A  95   O  ALA A 131           
SHEET    3   A 7 ALA A 151  SER A 158 -1  O  LEU A 154   N  LYS A  96           
SHEET    4   A 7 ASN A  71  TRP A  77 -1  N  MET A  73   O  HIS A 155           
SHEET    5   A 7 THR A  59  ASP A  64 -1  N  VAL A  63   O  LEU A  72           
SHEET    6   A 7 SER A 183  LYS A 184  1  O  SER A 183   N  LEU A  62           
SHEET    7   A 7 ILE A 187  ARG A 188 -1  O  ILE A 187   N  LYS A 184           
SHEET    1   B 3 ILE A  85  HIS A  86  0                                        
SHEET    2   B 3 THR A 163  PHE A 167 -1  O  PHE A 167   N  ILE A  85           
SHEET    3   B 3 LYS A 174  THR A 178 -1  O  VAL A 177   N  CYS A 164           
SHEET    1   C 3 LYS A 119  LEU A 125  0                                        
SHEET    2   C 3 LEU A 102  PHE A 107 -1  N  LEU A 102   O  LEU A 125           
SHEET    3   C 3 LEU A 139  GLU A 143 -1  O  GLU A 143   N  LYS A 103           
LINK         NE2 HIS A  86                FE   FE2 A 501     1555   1555  2.05  
LINK         NE2 HIS A  88                FE   FE2 A 501     1555   1555  2.17  
LINK         NE2 HIS A 140                FE   FE2 A 501     1555   1555  2.19  
LINK        FE   FE2 A 501                 SG  2CO A 580     1555   1555  2.47  
LINK        FE   FE2 A 501                 N   2CO A 580     1555   1555  2.36  
LINK        FE   FE2 A 501                 OD  2CO A 580     1555   1555  2.08  
CISPEP   1 THR A    4    GLU A    5          0        -2.96                     
CISPEP   2 SER A  158    PRO A  159          0        -5.54                     
SITE     1 AC1  4 HIS A  86  HIS A  88  HIS A 140  2CO A 580                    
SITE     1 AC2 12 TYR A  58  ARG A  60  LEU A  75  HIS A  86                    
SITE     2 AC2 12 HIS A  88  CYS A  93  LEU A  95  HIS A 140                    
SITE     3 AC2 12 VAL A 142  HIS A 155  TYR A 157  FE2 A 501                    
CRYST1   57.523   57.523  122.190  90.00  90.00  90.00 P 43 21 2     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      0.017384  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017384  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008184        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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