GenomeNet

Database: PDB
Entry: 4XF3
LinkDB: 4XF3
Original site: 4XF3 
HEADER    OXIDOREDUCTASE                          25-DEC-14   4XF3              
TITLE     CYSTEINE DIOXYGENASE VARIANT - Y157F AT PH 8.0 WITH CYSTEINE AND      
TITLE    2 DITHIONITE                                                           
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: 562                                         
KEYWDS    CUPIN FOLD, CYSTEINE TO CYSTEINE SULFINIC ACID CATALYSIS, THIOL       
KEYWDS   2 DIOXYGENASE, OXIDOREDUCTASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.M.DRIGGERS,P.A.KARPLUS                                              
REVDAT   4   04-DEC-19 4XF3    1       REMARK                                   
REVDAT   3   06-SEP-17 4XF3    1       REMARK                                   
REVDAT   2   14-DEC-16 4XF3    1       JRNL                                     
REVDAT   1   06-APR-16 4XF3    0                                                
JRNL        AUTH   C.M.DRIGGERS,K.M.KEAN,L.L.HIRSCHBERGER,R.B.COOLEY,           
JRNL        AUTH 2 M.H.STIPANUK,P.A.KARPLUS                                     
JRNL        TITL   STRUCTURE-BASED INSIGHTS INTO THE ROLE OF THE CYS-TYR        
JRNL        TITL 2 CROSSLINK AND INHIBITOR RECOGNITION BY MAMMALIAN CYSTEINE    
JRNL        TITL 3 DIOXYGENASE.                                                 
JRNL        REF    J. MOL. BIOL.                 V. 428  3999 2016              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   27477048                                                     
JRNL        DOI    10.1016/J.JMB.2016.07.012                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.4_1496)                   
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) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.91                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 30399                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.870                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3001                            
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 33.9150 -  4.2736    1.00     1476   163  0.1370 0.1723        
REMARK   3     2  4.2736 -  3.3931    1.00     1366   142  0.1501 0.1820        
REMARK   3     3  3.3931 -  2.9645    1.00     1362   150  0.1867 0.1891        
REMARK   3     4  2.9645 -  2.6936    1.00     1341   143  0.1953 0.2363        
REMARK   3     5  2.6936 -  2.5006    1.00     1290   170  0.1971 0.2502        
REMARK   3     6  2.5006 -  2.3532    1.00     1348   133  0.2032 0.2768        
REMARK   3     7  2.3532 -  2.2354    0.99     1311   136  0.2040 0.2522        
REMARK   3     8  2.2354 -  2.1381    1.00     1299   136  0.2040 0.2558        
REMARK   3     9  2.1381 -  2.0558    1.00     1310   143  0.2131 0.2504        
REMARK   3    10  2.0558 -  1.9848    1.00     1297   158  0.2158 0.2792        
REMARK   3    11  1.9848 -  1.9228    1.00     1297   144  0.2521 0.2774        
REMARK   3    12  1.9228 -  1.8678    0.99     1307   131  0.2473 0.2708        
REMARK   3    13  1.8678 -  1.8187    1.00     1318   133  0.2834 0.3193        
REMARK   3    14  1.8187 -  1.7743    1.00     1303   129  0.2670 0.3663        
REMARK   3    15  1.7743 -  1.7340    1.00     1297   131  0.2767 0.2858        
REMARK   3    16  1.7340 -  1.6971    1.00     1265   152  0.2767 0.3059        
REMARK   3    17  1.6971 -  1.6631    1.00     1322   147  0.2879 0.3150        
REMARK   3    18  1.6631 -  1.6317    1.00     1268   140  0.2861 0.3426        
REMARK   3    19  1.6317 -  1.6026    1.00     1314   130  0.3063 0.3244        
REMARK   3    20  1.6026 -  1.5754    1.00     1265   161  0.3477 0.3776        
REMARK   3    21  1.5754 -  1.5500    0.81     1042   129  0.3508 0.4025        
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)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.540           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  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      :  0.014           1620                                  
REMARK   3   ANGLE     :  1.297           2199                                  
REMARK   3   CHIRALITY :  0.058            236                                  
REMARK   3   PLANARITY :  0.007            291                                  
REMARK   3   DIHEDRAL  : 13.439            604                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND RESID 5 THROUGH 190                      
REMARK   3    ORIGIN FOR THE GROUP (A): -17.0976   3.1498 -50.0532              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1763 T22:   0.2714                                     
REMARK   3      T33:   0.2274 T12:  -0.0059                                     
REMARK   3      T13:  -0.0322 T23:  -0.0336                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4717 L22:   3.3535                                     
REMARK   3      L33:   2.0884 L12:   0.9444                                     
REMARK   3      L13:  -0.8830 L23:   0.6039                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0575 S12:  -0.0510 S13:   0.3114                       
REMARK   3      S21:  -0.0013 S22:   0.0840 S23:   0.0608                       
REMARK   3      S31:   0.1074 S32:  -0.1381 S33:  -0.0239                       
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 4XF3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-DEC-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000205559.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-JUL-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : DOUBLE-CRYSTAL, SI(111) LIQUID     
REMARK 200                                   N2 COOLED                          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30399                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 26.00                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 16.30                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 4IEO                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRI-SODIUM CITRATE PH=5.6, 24%      
REMARK 280  PEG 4000, 0.15M AMMONIUM ACETATE. 1:1 DROP RATIO WITH               
REMARK 280  MICROSEEDING.; SOAK SOLUTION AT PH 8.0, PH 6.2, VAPOR DIFFUSION,    
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
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       61.20000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       28.80000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       28.80000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       91.80000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       28.80000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       28.80000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       30.60000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       28.80000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       28.80000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       91.80000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       28.80000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       28.80000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       30.60000            
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       61.20000            
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 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 9470 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 112    CG   CD   CE   NZ                                   
REMARK 470     LYS A 120    CD   CE   NZ                                        
REMARK 470     LYS A 184    CE   NZ                                             
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      -10.61     76.32                                   
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 501  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  86   NE2                                                    
REMARK 620 2 HIS A  88   NE2 102.3                                              
REMARK 620 3 HIS A 140   NE2  91.8  93.6                                        
REMARK 620 4 CYS A 502   N    87.4  93.1 173.3                                  
REMARK 620 5 CYS A 502   SG  107.5 148.8  94.5  79.4                            
REMARK 620 6 CYS A 502   SG  135.6 108.7 116.6  60.4  41.5                      
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 FE A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CYS A 502                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4IEO   RELATED DB: PDB                                   
REMARK 900 UNLIGANDED WT CDO AT PH 4.0 IN THE PRESENCE OF CYS                   
REMARK 900 RELATED ID: 4IEP   RELATED DB: PDB                                   
REMARK 900 UNLIGANDED WT CDO AT PH 4.5 IN THE PRESENCE OF CYS                   
REMARK 900 RELATED ID: 4IEQ   RELATED DB: PDB                                   
REMARK 900 UNLIGANDED WT CDO AT PH 5.0 IN THE PRESENCE OF CYS                   
REMARK 900 RELATED ID: 4IER   RELATED DB: PDB                                   
REMARK 900 CYS-PERSULFENATE BOUND WT CDO AT PH 5.5 IN THE PRESENCE OF CYS       
REMARK 900 RELATED ID: 4IES   RELATED DB: PDB                                   
REMARK 900 CYS-PERSULFEANTE BOUND WT CDO AT PH 6.2 IN THE PRESENCE OF CYS       
REMARK 900 RELATED ID: 4IET   RELATED DB: PDB                                   
REMARK 900 CYS-PERSULFEANTE BOUND WT CDO AT PH 6.8 IN THE PRESENCE OF CYS       
REMARK 900 RELATED ID: 4IEU   RELATED DB: PDB                                   
REMARK 900 CYS-PERSULFENATE BOUND WT CDO AT PH 7.0 IN THE PRESENCE OF CYS       
REMARK 900 RELATED ID: 4IEV   RELATED DB: PDB                                   
REMARK 900 CYS-ONLY BOUND WT CDO AT PH 8.0 IN THE PRESENCE OF CYS               
REMARK 900 RELATED ID: 4IEW   RELATED DB: PDB                                   
REMARK 900 CYS-ONLY BOUND CYSTEINE DIOXYGENASE AT PH 9.0 IN THE PRESENCE OF CYS 
REMARK 900 RELATED ID: 4IEX   RELATED DB: PDB                                   
REMARK 900 UNLIGANDED ROOM-TEMP WT CDO AT PH 6.2                                
REMARK 900 RELATED ID: 4IEY   RELATED DB: PDB                                   
REMARK 900 CYS-PERSULFEANTE BOUND WT CDO AT PH 7.0 IN THE PRESENCE OF CYS,HOME- 
REMARK 900 SOURCE STRUCTURE                                                     
REMARK 900 RELATED ID: 4IEZ   RELATED DB: PDB                                   
REMARK 900 UNLIGANDED WT CDO AT PH 8.0                                          
REMARK 900 RELATED ID: 4JTN   RELATED DB: PDB                                   
REMARK 900 WT CDO AT PH 8.0 IN THE PRESENCE OF DITHIONITE                       
REMARK 900 RELATED ID: 4JTO   RELATED DB: PDB                                   
REMARK 900 CYS-ONLY BOUND WT CDO AT PH 8.0 IN THE PRESENCE OF CYS AND           
REMARK 900 DITHIONITE                                                           
REMARK 900 RELATED ID: 4KWK   RELATED DB: PDB                                   
REMARK 900 CYS-PERSULFIDE BOUND WT CDO                                          
REMARK 900 RELATED ID: 4KWL   RELATED DB: PDB                                   
REMARK 900 3-MERCAPTOPROPIONATE-PERSULFIDE BOUND WT CDO                         
REMARK 900 RELATED ID: 4PIX   RELATED DB: PDB                                   
REMARK 900 UNLIGANDED C93A CDO AT PH 6.2                                        
REMARK 900 RELATED ID: 4PIY   RELATED DB: PDB                                   
REMARK 900 HOMOCYSTEINE-BOUND C93A CDO AT PH 6.2                                
REMARK 900 RELATED ID: 4PIZ   RELATED DB: PDB                                   
REMARK 900 HOMOCYSTEINE-BOUND WT CDO AT PH 6.2                                  
REMARK 900 RELATED ID: 4PJY   RELATED DB: PDB                                   
REMARK 900 AZIDE-BOUND WT CDO AT PH 6.2                                         
REMARK 900 RELATED ID: 4EXT   RELATED DB: PDB                                   
REMARK 900 FE-CL BOUND Y157F AT PH ~7.0 IN THE PRESENCE OF AZIDE                
REMARK 900 RELATED ID: 4XEZ   RELATED DB: PDB                                   
REMARK 900 CYSTEINE DIOXYGENASE VARIANT - Y157F AT PH 8.0 WITH DITHIONITE       
REMARK 900 RELATED ID: 4XF0   RELATED DB: PDB                                   
REMARK 900 CYSTEINE DIOXYGENASE VARIANT - C93A AT PH 8.0 WITH CYSTEINE          
REMARK 900 RELATED ID: 4XF1   RELATED DB: PDB                                   
REMARK 900 CYSTEINE DIOXYGENASE VARIANT - Y157F AT PH 8.0 WITH CYSTEINE         
DBREF  4XF3 A    1   200  UNP    P21816   CDO1_RAT         1    200             
SEQADV 4XF3 PHE A  157  UNP  P21816    TYR   157 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  PHE 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     FE  A 501       1                                                       
HET    CYS  A 502      14                                                       
HETNAM      FE FE (III) ION                                                     
HETNAM     CYS CYSTEINE                                                         
FORMUL   2   FE    FE 3+                                                        
FORMUL   3  CYS    C3 H7 N O2 S                                                 
FORMUL   4  HOH   *133(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  CYS 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 102   O  LEU A 125           
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    FE A 501     1555   1555  1.98  
LINK         NE2 HIS A  88                FE    FE A 501     1555   1555  2.21  
LINK         NE2 HIS A 140                FE    FE A 501     1555   1555  2.15  
LINK        FE    FE A 501                 N  ACYS A 502     1555   1555  2.39  
LINK        FE    FE A 501                 SG ACYS A 502     1555   1555  2.34  
LINK        FE    FE A 501                 SG BCYS A 502     1555   1555  2.19  
CISPEP   1 SER A  158    PRO A  159          0        -5.74                     
SITE     1 AC1  4 HIS A  86  HIS A  88  HIS A 140  CYS A 502                    
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  PHE A 157                    
SITE     3 AC2 11 MET A 179   FE A 501  HOH A 689                               
CRYST1   57.600   57.600  122.400  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      0.017361  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017361  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008170        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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