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Database: PDB
Entry: 4XFI
LinkDB: 4XFI
Original site: 4XFI 
HEADER    OXIDOREDUCTASE                          26-DEC-14   4XFI              
TITLE     CYSTEINE DIOXYGENASE VARIANT - Y157F AT PH 6.2 WITH HOMOCYSTEINE      
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 4XFI    1       REMARK                                   
REVDAT   3   20-SEP-17 4XFI    1       REMARK                                   
REVDAT   2   14-DEC-16 4XFI    1       JRNL                                     
REVDAT   1   24-FEB-16 4XFI    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.    1.40 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) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 39392                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : 0.162                           
REMARK   3   FREE R VALUE                     : 0.192                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.790                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3855                            
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 33.3032 -  4.2485    1.00     1502   166  0.1544 0.1747        
REMARK   3     2  4.2485 -  3.3732    1.00     1403   146  0.1379 0.1694        
REMARK   3     3  3.3732 -  2.9471    1.00     1381   152  0.1488 0.1911        
REMARK   3     4  2.9471 -  2.6778    1.00     1358   154  0.1633 0.2061        
REMARK   3     5  2.6778 -  2.4859    1.00     1337   161  0.1607 0.1960        
REMARK   3     6  2.4859 -  2.3394    1.00     1354   140  0.1562 0.1928        
REMARK   3     7  2.3394 -  2.2223    1.00     1339   142  0.1527 0.1921        
REMARK   3     8  2.2223 -  2.1255    1.00     1363   132  0.1503 0.2018        
REMARK   3     9  2.1255 -  2.0437    1.00     1304   165  0.1523 0.1558        
REMARK   3    10  2.0437 -  1.9732    1.00     1343   157  0.1592 0.1963        
REMARK   3    11  1.9732 -  1.9115    1.00     1326   132  0.1626 0.1809        
REMARK   3    12  1.9115 -  1.8569    1.00     1329   137  0.1637 0.2088        
REMARK   3    13  1.8569 -  1.8080    1.00     1335   138  0.1613 0.2026        
REMARK   3    14  1.8080 -  1.7639    1.00     1348   133  0.1642 0.1939        
REMARK   3    15  1.7639 -  1.7238    1.00     1326   135  0.1747 0.1779        
REMARK   3    16  1.7238 -  1.6871    1.00     1300   149  0.1722 0.1701        
REMARK   3    17  1.6871 -  1.6534    1.00     1311   158  0.1695 0.1921        
REMARK   3    18  1.6534 -  1.6222    1.00     1319   146  0.1598 0.1954        
REMARK   3    19  1.6222 -  1.5932    1.00     1302   149  0.1711 0.1885        
REMARK   3    20  1.5932 -  1.5662    0.99     1291   148  0.1753 0.2305        
REMARK   3    21  1.5662 -  1.5409    0.99     1306   149  0.1892 0.2009        
REMARK   3    22  1.5409 -  1.5172    0.95     1215   127  0.2096 0.2382        
REMARK   3    23  1.5172 -  1.4949    0.88     1178   129  0.2291 0.2516        
REMARK   3    24  1.4949 -  1.4739    0.85     1120   115  0.2372 0.2750        
REMARK   3    25  1.4739 -  1.4539    0.79     1014   123  0.2514 0.3013        
REMARK   3    26  1.4539 -  1.4351    0.76     1018    90  0.2962 0.2795        
REMARK   3    27  1.4351 -  1.4171    0.71      938   103  0.3160 0.3249        
REMARK   3    28  1.4171 -  1.4000    0.67      877    79  0.3590 0.3599        
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)     : 0.140            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.820           
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           1660                                  
REMARK   3   ANGLE     :  1.315           2259                                  
REMARK   3   CHIRALITY :  0.081            242                                  
REMARK   3   PLANARITY :  0.006            298                                  
REMARK   3   DIHEDRAL  : 13.586            629                                  
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): -17.4493   2.9762 -50.0681              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0727 T22:   0.0928                                     
REMARK   3      T33:   0.0851 T12:   0.0020                                     
REMARK   3      T13:  -0.0080 T23:   0.0126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5759 L22:   2.0993                                     
REMARK   3      L33:   1.6009 L12:   0.5238                                     
REMARK   3      L13:  -0.4060 L23:   0.1565                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0224 S12:  -0.0025 S13:   0.0481                       
REMARK   3      S21:   0.0651 S22:   0.0371 S23:   0.0876                       
REMARK   3      S31:   0.0718 S32:  -0.0869 S33:  -0.0174                       
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 4XFI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JAN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000205581.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
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   : 39392                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.7                               
REMARK 200  DATA REDUNDANCY                : 23.30                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 67.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
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: 4IEU                                                 
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 6.2, VAPOR DIFFUSION, HANGING    
REMARK 280  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 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     GLU A   5    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 112    CG   CD   CE   NZ                                   
REMARK 470     LYS A 184    CE   NZ                                             
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   NE2  HIS A    88     O    HOH A   880              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   663     O    HOH A   678     6454     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       -7.28     77.40                                   
REMARK 500    ASN A 128      -16.50     77.40                                   
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 100.3                                              
REMARK 620 3 HIS A 140   NE2  95.7  99.2                                        
REMARK 620 4 HOH A 880   O   169.0  68.8  85.1                                  
REMARK 620 5 HCS A 502   SD  117.7 117.6 121.9  70.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HCS 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         
REMARK 900 RELATED ID: 4XF3   RELATED DB: PDB                                   
REMARK 900 CYSTEINE DIOXYGENASE VARIANT - Y157F AT PH 8.0 WITH CYSTEINE AND     
REMARK 900 DITHIONITE                                                           
REMARK 900 RELATED ID: 4XF4   RELATED DB: PDB                                   
REMARK 900 CYSTEINE DIOXYGENASE AT PH 8.0 IN COMPLEX WITH HOMOCYSTEINE          
REMARK 900 RELATED ID: 4XF9   RELATED DB: PDB                                   
REMARK 900 CYSTEINE DIOXYGENASE VARIANT - C93A AT PH 8.0 IN COMPLEX WITH        
REMARK 900 HOMOCYSTEINE                                                         
REMARK 900 RELATED ID: 4XFA   RELATED DB: PDB                                   
REMARK 900 CYSTEINE DIOXYGENASE VARIANT - Y157F AT PH 8.0 IN COMPLEX WITH       
REMARK 900 HOMOCYSTEINE                                                         
REMARK 900 RELATED ID: 4XFB   RELATED DB: PDB                                   
REMARK 900 CYSTEINE DIOXYGENASE VARIANT - C93A AT PH 8.0 UNLIGANDED             
REMARK 900 RELATED ID: 4XFC   RELATED DB: PDB                                   
REMARK 900 CYSTEINE DIOXYGENASE VARIANT - Y157F AT PH 6.2 UNLIGANDED            
REMARK 900 RELATED ID: 4XFF   RELATED DB: PDB                                   
REMARK 900 CYSTEINE DIOXYGENASE VARIANT - Y157F AT PH 6.2 WITH DITHIONITE       
REMARK 900 RELATED ID: 4XFG   RELATED DB: PDB                                   
REMARK 900 CYSTEINE DIOXYGENASE VARIANT - C93A AT PH 6.2 WITH CYSTEINE          
REMARK 900 RELATED ID: 4XFH   RELATED DB: PDB                                   
REMARK 900 CYSTEINE DIOXYGENASE VARIANT - Y157F AT PH 6.2 WITH CYSTEINE         
DBREF  4XFI A    1   200  UNP    P21816   CDO1_RAT         1    200             
SEQADV 4XFI 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    HCS  A 502       8                                                       
HETNAM      FE FE (III) ION                                                     
HETNAM     HCS 2-AMINO-4-MERCAPTO-BUTYRIC ACID                                  
FORMUL   2   FE    FE 3+                                                        
FORMUL   3  HCS    C4 H9 N O2 S                                                 
FORMUL   4  HOH   *281(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    
HELIX    5 AA5 GLN A   65  LYS A   69  5                                   5    
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 SER A 121  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  2.06  
LINK         NE2 HIS A  88                FE    FE A 501     1555   1555  2.08  
LINK         NE2 HIS A 140                FE    FE A 501     1555   1555  2.06  
LINK        FE    FE A 501                 O   HOH A 880     1555   1555  1.70  
LINK        FE    FE A 501                 SD  HCS A 502     1555   1555  2.22  
CISPEP   1 SER A  158    PRO A  159          0        -6.98                     
SITE     1 AC1  5 HIS A  86  HIS A  88  HIS A 140  HCS A 502                    
SITE     2 AC1  5 HOH A 880                                                     
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  HIS A 155  PHE A 157                    
SITE     3 AC2 12 MET A 179   FE A 501  HOH A 787  HOH A 880                    
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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