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Database: PDB
Entry: 4IEY
LinkDB: 4IEY
Original site: 4IEY 
HEADER    OXIDOREDUCTASE                          13-DEC-12   4IEY              
TITLE     CYS-PERSULFENATE BOUND CYSTEINE DIOXYGENASE AT PH 7.0 IN THE PRESENCE 
TITLE    2 OF CYS, HOME-SOURCE STRUCTURE                                        
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 4IEY    1       JRNL                                     
REVDAT   2   21-AUG-13 4IEY    1       JRNL                                     
REVDAT   1   26-JUN-13 4IEY    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.    1.63 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) : 1.63                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.29                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 25094                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.810                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2461                            
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 33.3007 -  4.2690    1.00     1483   165  0.1549 0.1746        
REMARK   3     2  4.2690 -  3.3895    0.97     1329   137  0.1599 0.2047        
REMARK   3     3  3.3895 -  2.9613    1.00     1370   152  0.1820 0.2199        
REMARK   3     4  2.9613 -  2.6907    1.00     1347   141  0.1909 0.2205        
REMARK   3     5  2.6907 -  2.4979    1.00     1294   169  0.1935 0.2664        
REMARK   3     6  2.4979 -  2.3507    1.00     1352   139  0.2142 0.3150        
REMARK   3     7  2.3507 -  2.2330    0.86     1141   111  0.3425 0.4050        
REMARK   3     8  2.2330 -  2.1358    0.84     1105   116  0.3352 0.3841        
REMARK   3     9  2.1358 -  2.0536    1.00     1316   145  0.2216 0.2814        
REMARK   3    10  2.0536 -  1.9827    0.99     1284   158  0.2490 0.3287        
REMARK   3    11  1.9827 -  1.9207    0.95     1243   136  0.2856 0.3083        
REMARK   3    12  1.9207 -  1.8658    0.66      876    82  0.5027 0.5592        
REMARK   3    13  1.8658 -  1.8167    0.99     1302   132  0.2731 0.3172        
REMARK   3    14  1.8167 -  1.7724    0.99     1286   128  0.2483 0.3011        
REMARK   3    15  1.7724 -  1.7321    0.98     1302   127  0.2839 0.3211        
REMARK   3    16  1.7321 -  1.6953    0.98     1248   149  0.3188 0.3594        
REMARK   3    17  1.6953 -  1.6613    0.96     1256   141  0.3378 0.3614        
REMARK   3    18  1.6613 -  1.6300    0.87     1099   133  0.3724 0.4181        
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)     : 0.260            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.500           
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      :  0.015           1587                                  
REMARK   3   ANGLE     :  1.496           2143                                  
REMARK   3   CHIRALITY :  0.081            227                                  
REMARK   3   PLANARITY :  0.007            281                                  
REMARK   3   DIHEDRAL  : 15.239            576                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain A                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -16.9665   3.5367 -49.7259              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1336 T22:   0.1716                                     
REMARK   3      T33:   0.1417 T12:   0.0006                                     
REMARK   3      T13:  -0.0111 T23:   0.0032                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9598 L22:   1.7912                                     
REMARK   3      L33:   1.5767 L12:   0.5349                                     
REMARK   3      L13:  -0.5108 L23:   0.2309                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0059 S12:  -0.0025 S13:  -0.0561                       
REMARK   3      S21:   0.0483 S22:  -0.0263 S23:   0.0470                       
REMARK   3      S31:   0.0988 S32:  -0.0968 S33:   0.0149                       
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 4IEY 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 RCSB076667.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAY-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) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU300                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26578                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.630                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.294                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
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 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   761     O    HOH A   797              2.10            
REMARK 500   OD2  ASP A   108     O    HOH A   826              2.14            
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   OD1  ASN A    67     O    HOH A   831     8554     1.92            
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    GLU A 127      128.67    -38.61                                   
REMARK 500    ASN A 128      -13.65     77.97                                   
REMARK 500    THR A 189       79.90   -119.97                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 799        DISTANCE =  7.91 ANGSTROMS                       
REMARK 525    HOH A 800        DISTANCE =  9.82 ANGSTROMS                       
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 2CO A 502   OD  137.4                                              
REMARK 620 3 HIS A 140   NE2 101.5 112.4                                        
REMARK 620 4 HIS A  88   NE2  99.7 107.0  87.0                                  
REMARK 620 5 2CO A 502   SG  107.6  46.2  95.1 151.6                            
REMARK 620 6 2CO A 502   N    82.5  63.1 175.6  94.3  81.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2CO A 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: 4IEV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IEW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IEX   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  4IEY A    1   200  UNP    P21816   CDO1_RAT         1    200             
SEQRES   1 A  200  MET GLU ARG THR GLU LEU LEU LYS PRO ARG THR LEU ALA          
SEQRES   2 A  200  ASP LEU ILE ARG ILE LEU HIS GLU LEU PHE ALA GLY ASP          
SEQRES   3 A  200  GLU VAL ASN VAL GLU GLU VAL GLN ALA VAL LEU GLU ALA          
SEQRES   4 A  200  TYR GLU SER ASN PRO ALA GLU TRP ALA LEU TYR ALA LYS          
SEQRES   5 A  200  PHE ASP GLN TYR ARG TYR THR ARG ASN LEU VAL ASP GLN          
SEQRES   6 A  200  GLY ASN GLY LYS PHE ASN LEU MET ILE LEU CYS TRP GLY          
SEQRES   7 A  200  GLU GLY HIS GLY SER SER ILE HIS ASP HIS THR ASP SER          
SEQRES   8 A  200  HIS CYS PHE LEU LYS LEU LEU GLN GLY ASN LEU LYS GLU          
SEQRES   9 A  200  THR LEU PHE ASP TRP PRO ASP LYS LYS SER ASN GLU MET          
SEQRES  10 A  200  ILE LYS LYS SER GLU ARG THR LEU ARG GLU ASN GLN CYS          
SEQRES  11 A  200  ALA TYR ILE ASN ASP SER ILE GLY LEU HIS ARG VAL GLU          
SEQRES  12 A  200  ASN VAL SER HIS THR GLU PRO ALA VAL SER LEU HIS LEU          
SEQRES  13 A  200  TYR SER PRO PRO PHE ASP THR CYS HIS ALA PHE ASP GLN          
SEQRES  14 A  200  ARG THR GLY HIS LYS ASN LYS VAL THR MET THR PHE HIS          
SEQRES  15 A  200  SER LYS PHE GLY ILE ARG THR PRO PHE THR THR SER GLY          
SEQRES  16 A  200  SER LEU GLU ASN ASN                                          
HET    FE2  A 501       1                                                       
HET    2CO  A 502       9                                                       
HETNAM     FE2 FE (II) ION                                                      
HETNAM     2CO S-HYDROPEROXYCYSTEINE                                            
FORMUL   2  FE2    FE 2+                                                        
FORMUL   3  2CO    C3 H7 N O4 S                                                 
FORMUL   4  HOH   *247(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  ARG A 126  0                                        
SHEET    2   C 3 ASN A 101  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         NE2 HIS A  86                FE   FE2 A 501     1555   1555  2.02  
LINK        FE   FE2 A 501                 OD  2CO A 502     1555   1555  2.03  
LINK         NE2 HIS A 140                FE   FE2 A 501     1555   1555  2.18  
LINK         NE2 HIS A  88                FE   FE2 A 501     1555   1555  2.30  
LINK        FE   FE2 A 501                 SG  2CO A 502     1555   1555  2.32  
LINK        FE   FE2 A 501                 N   2CO A 502     1555   1555  2.36  
LINK         SG  CYS A  93                 CE2 TYR A 157     1555   1555  1.81  
CISPEP   1 SER A  158    PRO A  159          0         1.72                     
SITE     1 AC1  4 HIS A  86  HIS A  88  HIS A 140  2CO A 502                    
SITE     1 AC2 13 TYR A  58  ARG A  60  HIS A  86  HIS A  88                    
SITE     2 AC2 13 CYS A  93  LEU A  95  HIS A 140  VAL A 142                    
SITE     3 AC2 13 HIS A 155  TYR A 157  MET A 179  FE2 A 501                    
SITE     4 AC2 13 HOH A 829                                                     
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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