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Database: PDB
Entry: 4Z82
LinkDB: 4Z82
Original site: 4Z82 
HEADER    OXIDOREDUCTASE                          08-APR-15   4Z82              
TITLE     CYSTEINE BOUND RAT CYSTEINE DIOXYGENASE C164S VARIANT AT PH 8.1       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYSTEINE DIOXYGENASE TYPE 1;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CYSTEINE DIOXYGENASE TYPE I,CDO-I;                          
COMPND   5 EC: 1.13.11.20;                                                      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: CDO1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-32A(+)                                
KEYWDS    THIOETHER BOND, POST-TRANSLATIONAL MODIFICATION, POST TRANSLATIONAL,  
KEYWDS   2 POSTTRANSLATIONAL, SUBSTRATE BOUND, OXIDOREDUCTASE                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.FELLNER,E.P.TCHESNOKOV,E.SIAKKOU,M.T.RUTLEDGE,M.KANITZ,             
AUTHOR   2 G.N.L.JAMESON,S.M.WILBANKS                                           
REVDAT   3   22-NOV-17 4Z82    1       REMARK                                   
REVDAT   2   29-JUN-16 4Z82    1       JRNL                                     
REVDAT   1   01-JUN-16 4Z82    0                                                
JRNL        AUTH   M.FELLNER,E.SIAKKOU,A.S.FAPONLE,E.P.TCHESNOKOV,              
JRNL        AUTH 2 S.P.DE VISSER,S.M.WILBANKS,G.N.JAMESON                       
JRNL        TITL   INFLUENCE OF CYSTEINE 164 ON ACTIVE SITE STRUCTURE IN RAT    
JRNL        TITL 2 CYSTEINE DIOXYGENASE.                                        
JRNL        REF    J.BIOL.INORG.CHEM.            V.  21   501 2016              
JRNL        REFN                   ESSN 1432-1327                               
JRNL        PMID   27193596                                                     
JRNL        DOI    10.1007/S00775-016-1360-0                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9-1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 23.88                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.910                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 22818                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.206                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.110                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2160                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 23.8862 -  4.1857    1.00     2781   126  0.1419 0.1770        
REMARK   3     2  4.1857 -  3.3252    0.99     2788   129  0.1486 0.1761        
REMARK   3     3  3.3252 -  2.9057    0.99     2740   140  0.1768 0.1676        
REMARK   3     4  2.9057 -  2.6404    0.98     2709   163  0.1821 0.2052        
REMARK   3     5  2.6404 -  2.4514    0.98     2686   172  0.1954 0.2363        
REMARK   3     6  2.4514 -  2.3070    0.98     2694   151  0.1943 0.2437        
REMARK   3     7  2.3070 -  2.1915    0.97     2694   136  0.1936 0.2162        
REMARK   3     8  2.1915 -  2.0962    0.97     2683   133  0.1925 0.2100        
REMARK   3     9  2.0962 -  2.0155    0.96     2652   153  0.1992 0.2319        
REMARK   3    10  2.0155 -  1.9460    0.96     2650   149  0.2010 0.2050        
REMARK   3    11  1.9460 -  1.8852    0.95     2636   147  0.2118 0.2266        
REMARK   3    12  1.8852 -  1.8313    0.95     2673   115  0.2305 0.2947        
REMARK   3    13  1.8313 -  1.7831    0.94     2600   152  0.2541 0.3098        
REMARK   3    14  1.7831 -  1.7396    0.94     2614   150  0.2439 0.2830        
REMARK   3    15  1.7396 -  1.7000    0.93     2544   144  0.2439 0.2713        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.920           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.41                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.97                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           1594                                  
REMARK   3   ANGLE     :  1.102           2161                                  
REMARK   3   CHIRALITY :  0.061            230                                  
REMARK   3   PLANARITY :  0.004            284                                  
REMARK   3   DIHEDRAL  : 13.954            584                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4Z82 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-APR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000208789.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-NOV-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 6.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54187                            
REMARK 200  MONOCHROMATOR                  : OSMIC VARIMAX OPTICS               
REMARK 200  OPTICS                         : OSMIC VARIMAX OPTICS               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM 7.1.0                      
REMARK 200  DATA SCALING SOFTWARE          : D*TREK, AIMLESS 0.3.11             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22847                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 23.880                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY                : 12.40                              
REMARK 200  R MERGE                    (I) : 0.05800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.60                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.83200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.6                                          
REMARK 200 STARTING MODEL: 4KWJ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROPS OF 2 MICROL OF 50 MG/ML    
REMARK 280  C164S-CDO (10 MM SODIUM PHOSPHATE, 20 MM NACL, PH 7.5) AND 2        
REMARK 280  MICROL RESERVOIR BUFFER CONTAINING SEEDS FROM WT-CDO WERE           
REMARK 280  ALLOWED TO EQUILIBRATE ABOVE THE RESERVOIR BUFFER (26% (W/V)        
REMARK 280  POLYETHYLENE GLYCOL 4000, 200 MM AMMONIUM ACETATE, 100 MM SODIUM    
REMARK 280  CITRATE), PH 6.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K   
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       61.11500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       29.01000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       29.01000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       91.67250            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       29.01000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       29.01000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       30.55750            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       29.01000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       29.01000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       91.67250            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       29.01000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       29.01000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       30.55750            
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       61.11500            
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     THR A     4                                                      
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   536     O    HOH A   600              1.81            
REMARK 500   O    HOH A   592     O    HOH A   606              1.81            
REMARK 500   O    HOH A   605     O    HOH A   616              2.16            
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       -7.34     73.40                                   
REMARK 500    ASN A 128       -7.34     74.76                                   
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 301  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  86   NE2                                                    
REMARK 620 2 HIS A  88   NE2 100.8                                              
REMARK 620 3 HIS A 140   NE2  94.5  89.3                                        
REMARK 620 4 HOH A 401   O   143.1  92.6 120.1                                  
REMARK 620 5 CYS A 302   SG  107.9 150.2  96.3  59.4                            
REMARK 620 6 CYS A 302   N    90.4  93.6 173.7  54.3  78.5                      
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 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CYS A 302                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4YYO   RELATED DB: PDB                                   
REMARK 900 RESTING STATE OF THE SAME PROTEIN.                                   
DBREF  4Z82 A    1   200  UNP    P21816   CDO1_RAT         1    200             
SEQADV 4Z82 SER A  164  UNP  P21816    CYS   164 ENGINEERED MUTATION            
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 SER 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 301       1                                                       
HET    CYS  A 302       7                                                       
HETNAM     FE2 FE (II) ION                                                      
HETNAM     CYS CYSTEINE                                                         
FORMUL   2  FE2    FE 2+                                                        
FORMUL   3  CYS    C3 H7 N O2 S                                                 
FORMUL   4  HOH   *242(H2 O)                                                    
HELIX    1 AA1 THR A   11  PHE A   23  1                                  13    
HELIX    2 AA2 ASN A   29  TYR A   40  1                                  12    
HELIX    3 AA3 ASN A   43  ALA A   48  1                                   6    
HELIX    4 AA4 LEU A   49  ALA A   51  5                                   3    
SHEET    1 AA1 7 CYS A 130  ILE A 133  0                                        
SHEET    2 AA1 7 HIS A  92  GLN A  99 -1  N  LEU A  95   O  ALA A 131           
SHEET    3 AA1 7 ALA A 151  SER A 158 -1  O  LEU A 154   N  LYS A  96           
SHEET    4 AA1 7 ASN A  71  TRP A  77 -1  N  MET A  73   O  HIS A 155           
SHEET    5 AA1 7 THR A  59  ASP A  64 -1  N  ASN A  61   O  ILE A  74           
SHEET    6 AA1 7 SER A 183  LYS A 184  1  O  SER A 183   N  LEU A  62           
SHEET    7 AA1 7 ILE A 187  ARG A 188 -1  O  ILE A 187   N  LYS A 184           
SHEET    1 AA2 3 ILE A  85  HIS A  86  0                                        
SHEET    2 AA2 3 THR A 163  PHE A 167 -1  O  PHE A 167   N  ILE A  85           
SHEET    3 AA2 3 LYS A 174  THR A 178 -1  O  VAL A 177   N  SER A 164           
SHEET    1 AA3 3 LYS A 119  LEU A 125  0                                        
SHEET    2 AA3 3 LEU A 102  PHE A 107 -1  N  LEU A 106   O  LYS A 120           
SHEET    3 AA3 3 LEU A 139  GLU A 143 -1  O  GLU A 143   N  LYS A 103           
LINK         NE2 HIS A  86                FE   FE2 A 301     1555   1555  2.03  
LINK         NE2 HIS A  88                FE   FE2 A 301     1555   1555  2.21  
LINK         SG  CYS A  93                 CE1 TYR A 157     1555   1555  1.98  
LINK         NE2 HIS A 140                FE   FE2 A 301     1555   1555  2.35  
LINK        FE   FE2 A 301                 O   HOH A 401     1555   1555  2.28  
LINK        FE   FE2 A 301                 SG  CYS A 302     1555   1555  2.37  
LINK        FE   FE2 A 301                 N   CYS A 302     1555   1555  2.34  
CISPEP   1 SER A  158    PRO A  159          0        -4.18                     
SITE     1 AC1  5 HIS A  86  HIS A  88  HIS A 140  CYS A 302                    
SITE     2 AC1  5 HOH A 401                                                     
SITE     1 AC2 11 TYR A  58  ARG A  60  LEU A  75  HIS A  86                    
SITE     2 AC2 11 HIS A  88  HIS A 140  HIS A 155  TYR A 157                    
SITE     3 AC2 11 MET A 179  FE2 A 301  HOH A 401                               
CRYST1   58.020   58.020  122.230  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      0.017235  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017235  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008181        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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