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Database: PDB
Entry: 4IEV
LinkDB: 4IEV
Original site: 4IEV 
HEADER    OXIDOREDUCTASE                          13-DEC-12   4IEV              
TITLE     CYS-ONLY BOUND CYSTEINE DIOXYGENASE AT PH 8.0 IN THE PRESENCE OF CYS  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYSTEINE DIOXYGENASE TYPE 1;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CYSTEINE DIOXYGENASE TYPE I, CDO, CDO-I;                    
COMPND   5 EC: 1.13.11.20;                                                      
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;                                 
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: CDO1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CUPIN FOLD, CATALYZES OXIDATION, CYSTEINE TO CYSTEINE SULFINATE, C93- 
KEYWDS   2 Y157 CROSSLINK, CYTOSOL, OXIDOREDUCTASE                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.M.DRIGGERS,R.B.COOLEY,P.A.KARPLUS                                   
REVDAT   3   11-SEP-13 4IEV    1       JRNL                                     
REVDAT   2   21-AUG-13 4IEV    1       JRNL                                     
REVDAT   1   26-JUN-13 4IEV    0                                                
JRNL        AUTH   C.M.DRIGGERS,R.B.COOLEY,B.SANKARAN,L.L.HIRSCHBERGER,         
JRNL        AUTH 2 M.H.STIPANUK,P.A.KARPLUS                                     
JRNL        TITL   CYSTEINE DIOXYGENASE STRUCTURES FROM PH4 TO 9: CONSISTENT    
JRNL        TITL 2 CYS-PERSULFENATE FORMATION AT INTERMEDIATE PH AND A          
JRNL        TITL 3 CYS-BOUND ENZYME AT HIGHER PH.                               
JRNL        REF    J.MOL.BIOL.                   V. 425  3121 2013              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   23747973                                                     
JRNL        DOI    10.1016/J.JMB.2013.05.028                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.91                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 27708                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.820                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2720                            
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 33.9145 -  4.2668    1.00     1490   165  0.1478 0.1700        
REMARK   3     2  4.2668 -  3.3876    1.00     1377   143  0.1399 0.1610        
REMARK   3     3  3.3876 -  2.9597    1.00     1374   154  0.1641 0.1846        
REMARK   3     4  2.9597 -  2.6892    1.00     1349   141  0.1770 0.2386        
REMARK   3     5  2.6892 -  2.4965    1.00     1310   169  0.1832 0.2607        
REMARK   3     6  2.4965 -  2.3494    1.00     1345   138  0.1684 0.2346        
REMARK   3     7  2.3494 -  2.2318    1.00     1321   139  0.1701 0.2387        
REMARK   3     8  2.2318 -  2.1346    1.00     1321   133  0.1689 0.2514        
REMARK   3     9  2.1346 -  2.0525    1.00     1322   149  0.1968 0.2387        
REMARK   3    10  2.0525 -  1.9816    1.00     1291   155  0.1982 0.2650        
REMARK   3    11  1.9816 -  1.9197    1.00     1324   145  0.2327 0.2769        
REMARK   3    12  1.9197 -  1.8648    1.00     1321   135  0.2510 0.2882        
REMARK   3    13  1.8648 -  1.8157    1.00     1308   130  0.2555 0.3004        
REMARK   3    14  1.8157 -  1.7714    1.00     1315   134  0.2836 0.3158        
REMARK   3    15  1.7714 -  1.7312    1.00     1324   125  0.3115 0.3665        
REMARK   3    16  1.7312 -  1.6943    1.00     1266   156  0.3328 0.3430        
REMARK   3    17  1.6943 -  1.6604    1.00     1314   151  0.3513 0.3670        
REMARK   3    18  1.6604 -  1.6291    0.99     1251   152  0.3639 0.3838        
REMARK   3    19  1.6291 -  1.6000    0.82     1065   106  0.3811 0.3539        
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)     : 0.250            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.140           
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      :  0.013           1575                                  
REMARK   3   ANGLE     :  1.334           2137                                  
REMARK   3   CHIRALITY :  0.087            228                                  
REMARK   3   PLANARITY :  0.006            276                                  
REMARK   3   DIHEDRAL  : 14.651            582                                  
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 5:190 OR RESID 501:502 ) )         
REMARK   3    ORIGIN FOR THE GROUP (A): -17.2383   3.0621 -49.7928              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1134 T22:   0.1888                                     
REMARK   3      T33:   0.1350 T12:  -0.0040                                     
REMARK   3      T13:  -0.0156 T23:  -0.0180                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9421 L22:   2.7962                                     
REMARK   3      L33:   2.2293 L12:   0.5804                                     
REMARK   3      L13:  -0.2713 L23:   0.1685                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0410 S12:  -0.0118 S13:   0.0805                       
REMARK   3      S21:  -0.0142 S22:   0.0239 S23:   0.0452                       
REMARK   3      S31:   0.1261 S32:  -0.1352 S33:   0.0070                       
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 4IEV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JAN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB076664.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUN-12                          
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                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL, SI(111)            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28421                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX (PHENIX.REFINE: 1.8_1069)                      
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PURIFIED ENZYME WAS CONCENTRATED TO ~8   
REMARK 280  MG/ML AND THEN ADDED INTO A CRYSTALLIZATION SCREEN CONTAINING 0.1   
REMARK 280  M TRI-SODIUM CITRATE PH=5.6, 24-34% PEG 4K, AND 0.1-0.25 M          
REMARK 280  AMMONIUM ACETATE. 1.5L OF PROTEIN SOLUTION WAS ADDED TO EACH WELL   
REMARK 280  AND MIXED WITH AN EQUIVALENT VOLUME OF RESERVOIR SOLUTION., PH      
REMARK 280  6.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 141   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 128      -10.95     74.83                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 A 501  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  86   NE2                                                    
REMARK 620 2 HIS A 140   NE2  95.9                                              
REMARK 620 3 HIS A  88   NE2 101.1  91.6                                        
REMARK 620 4 CYS A 502   SG  107.4  93.3 150.3                                  
REMARK 620 5 CYS A 502   N    91.9 170.9  91.5  79.8                            
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 FE2 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 RELATED ID: 4IEP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IEQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IER   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IES   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IET   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IEU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IEW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IEX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IEY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IEZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IF0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IF1   RELATED DB: PDB                                   
DBREF  4IEV A    1   200  UNP    P21816   CDO1_RAT         1    200             
SEQRES   1 A  200  MET GLU ARG THR GLU LEU LEU LYS PRO ARG THR LEU ALA          
SEQRES   2 A  200  ASP LEU ILE ARG ILE LEU HIS GLU LEU PHE ALA GLY ASP          
SEQRES   3 A  200  GLU VAL ASN VAL GLU GLU VAL GLN ALA VAL LEU GLU ALA          
SEQRES   4 A  200  TYR GLU SER ASN PRO ALA GLU TRP ALA LEU TYR ALA LYS          
SEQRES   5 A  200  PHE ASP GLN TYR ARG TYR THR ARG ASN LEU VAL ASP GLN          
SEQRES   6 A  200  GLY ASN GLY LYS PHE ASN LEU MET ILE LEU CYS TRP GLY          
SEQRES   7 A  200  GLU GLY HIS GLY SER SER ILE HIS ASP HIS THR ASP SER          
SEQRES   8 A  200  HIS CYS PHE LEU LYS LEU LEU GLN GLY ASN LEU LYS GLU          
SEQRES   9 A  200  THR LEU PHE ASP TRP PRO ASP LYS LYS SER ASN GLU MET          
SEQRES  10 A  200  ILE LYS LYS SER GLU ARG THR LEU ARG GLU ASN GLN CYS          
SEQRES  11 A  200  ALA TYR ILE ASN ASP SER ILE GLY LEU HIS ARG VAL GLU          
SEQRES  12 A  200  ASN VAL SER HIS THR GLU PRO ALA VAL SER LEU HIS LEU          
SEQRES  13 A  200  TYR SER PRO PRO PHE ASP THR CYS HIS ALA PHE ASP GLN          
SEQRES  14 A  200  ARG THR GLY HIS LYS ASN LYS VAL THR MET THR PHE HIS          
SEQRES  15 A  200  SER LYS PHE GLY ILE ARG THR PRO PHE THR THR SER GLY          
SEQRES  16 A  200  SER LEU GLU ASN ASN                                          
HET    FE2  A 501       1                                                       
HET    CYS  A 502       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   *186(H2 O)                                                    
HELIX    1   1 THR A   11  PHE A   23  1                                  13    
HELIX    2   2 ASN A   29  TYR A   40  1                                  12    
HELIX    3   3 ASN A   43  ALA A   48  1                                   6    
HELIX    4   4 LEU A   49  ALA A   51  5                                   3    
SHEET    1   A 7 CYS A 130  ILE A 133  0                                        
SHEET    2   A 7 HIS A  92  GLN A  99 -1  N  LEU A  95   O  ALA A 131           
SHEET    3   A 7 ALA A 151  SER A 158 -1  O  LEU A 154   N  LYS A  96           
SHEET    4   A 7 ASN A  71  TRP A  77 -1  N  MET A  73   O  HIS A 155           
SHEET    5   A 7 THR A  59  ASP A  64 -1  N  VAL A  63   O  LEU A  72           
SHEET    6   A 7 SER A 183  LYS A 184  1  O  SER A 183   N  LEU A  62           
SHEET    7   A 7 ILE A 187  ARG A 188 -1  O  ILE A 187   N  LYS A 184           
SHEET    1   B 3 ILE A  85  HIS A  86  0                                        
SHEET    2   B 3 THR A 163  PHE A 167 -1  O  PHE A 167   N  ILE A  85           
SHEET    3   B 3 LYS A 174  THR A 178 -1  O  VAL A 177   N  CYS A 164           
SHEET    1   C 3 LYS A 119  LEU A 125  0                                        
SHEET    2   C 3 LEU A 102  PHE A 107 -1  N  LEU A 106   O  LYS A 120           
SHEET    3   C 3 LEU A 139  GLU A 143 -1  O  GLU A 143   N  LYS A 103           
LINK         SG  CYS A  93                 CE2 TYR A 157     1555   1555  1.80  
LINK         NE2 HIS A  86                FE   FE2 A 501     1555   1555  2.06  
LINK         NE2 HIS A 140                FE   FE2 A 501     1555   1555  2.15  
LINK         NE2 HIS A  88                FE   FE2 A 501     1555   1555  2.31  
LINK        FE   FE2 A 501                 SG  CYS A 502     1555   1555  2.35  
LINK        FE   FE2 A 501                 N   CYS A 502     1555   1555  2.35  
CISPEP   1 SER A  158    PRO A  159          0        -5.30                     
SITE     1 AC1  4 HIS A  86  HIS A  88  HIS A 140  CYS A 502                    
SITE     1 AC2 10 TYR A  58  ARG A  60  LEU A  75  HIS A  86                    
SITE     2 AC2 10 HIS A  88  HIS A 140  HIS A 155  TYR A 157                    
SITE     3 AC2 10 MET A 179  FE2 A 501                                          
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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