GenomeNet

Database: PDB
Entry: 2GH2
LinkDB: 2GH2
Original site: 2GH2 
HEADER    OXIDOREDUCTASE                          24-MAR-06   2GH2              
TITLE     1.5 A RESOLUTION R. NORVEGICUS CYSTEINE DIOXYGENASE STRUCTURE         
TITLE    2 CRYSTALLIZED IN THE PRESENCE OF CYSTEINE                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYSTEINE DIOXYGENASE TYPE I;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: 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: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: CDO1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET32A                                    
KEYWDS    THIOETHER, CYSTEINYL-TYROSINE, CUPIN, BETA-SANDWICH, TETRAHEDRAL IRON 
KEYWDS   2 COORDINATION, OXIDOREDUCTASE                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.R.SIMMONS,P.A.KARPLUS,M.H.STIPANUK                                  
REVDAT   4   24-JAN-18 2GH2    1       AUTHOR                                   
REVDAT   3   24-FEB-09 2GH2    1       VERSN                                    
REVDAT   2   18-JUL-06 2GH2    1       JRNL                                     
REVDAT   1   11-APR-06 2GH2    0                                                
JRNL        AUTH   C.R.SIMMONS,Q.LIU,Q.HUANG,Q.HAO,T.P.BEGLEY,P.A.KARPLUS,      
JRNL        AUTH 2 M.H.STIPANUK                                                 
JRNL        TITL   CRYSTAL STRUCTURE OF MAMMALIAN CYSTEINE DIOXYGENASE: A NOVEL 
JRNL        TITL 2 MONONUCLEAR IRON CENTER FOR CYSTEINE THIOL OXIDATION.        
JRNL        REF    J.BIOL.CHEM.                  V. 281 18723 2006              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   16611640                                                     
JRNL        DOI    10.1074/JBC.M601555200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.84                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 32403                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3201                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1512                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 6                                       
REMARK   3   SOLVENT ATOMS            : 343                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.64                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.75500                                             
REMARK   3    B22 (A**2) : -0.75500                                             
REMARK   3    B33 (A**2) : 1.51000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.16                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.10                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.18                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.11                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.000                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.271 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.925 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.206 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.316 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 46.48                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : CNS_TOPPAR:PROTEIN_REP.PARAM                   
REMARK   3  PARAMETER FILE  2  : CNS_TOPPAR:WATER.PARAM                         
REMARK   3  PARAMETER FILE  3  : CNS_TOPPAR:ION.PARAM                           
REMARK   3  PARAMETER FILE  4  : CYSTYR_NEW.PARAM                               
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2GH2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000037108.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F2                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9790                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33961                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.840                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 13.80                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.20                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.71300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NATIVE CDO (2B5H)                                    
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15 M AMMONIUM SULFATE, 0.2 M SODIUM    
REMARK 280  CACODYLATE, 26% PEG 8K, 5 MM CYSTEINE , PH 6.5, VAPOR DIFFUSION,    
REMARK 280  SITTING 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       61.40200            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       28.74200            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       28.74200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       92.10300            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       28.74200            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       28.74200            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       30.70100            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       28.74200            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       28.74200            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       92.10300            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       28.74200            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       28.74200            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       30.70100            
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       61.40200            
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 300 REMARK: THE BIOLOGICAL UNIT IS A MONOMER, AND THERE IS A SINGLE      
REMARK 300 MONOMER PER ASYMMETRIC UNIT.                                         
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 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     PHE A   191                                                      
REMARK 465     THR A   192                                                      
REMARK 465     THR A   193                                                      
REMARK 465     SER A   194                                                      
REMARK 465     GLY A   195                                                      
REMARK 465     SER A   196                                                      
REMARK 465     LEU A   197                                                      
REMARK 465     GLU A   198                                                      
REMARK 465     ASN A   199                                                      
REMARK 465     ASN A   200                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   SG   CYS A    93     CE2  TYR A   157              1.82            
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       -5.57     76.05                                   
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 103.2                                              
REMARK 620 3 HIS A 140   NE2  95.7  97.5                                        
REMARK 620 4 HOH A 505   O   124.4 125.3 102.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 451                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 501                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2B5H   RELATED DB: PDB                                   
REMARK 900 NATIVE CDO STRUCTURE                                                 
DBREF  2GH2 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    SO4  A 451       5                                                       
HET     FE  A 501       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      FE FE (III) ION                                                     
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3   FE    FE 3+                                                        
FORMUL   4  HOH   *343(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    
HELIX    5   5 GLN A   65  LYS A   69  5                                   5    
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 SER A 121  LEU A 125  0                                        
SHEET    2   C 3 LEU A 102  PHE A 107 -1  N  LEU A 102   O  LEU A 125           
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    FE A 501     1555   1555  2.08  
LINK         NE2 HIS A  88                FE    FE A 501     1555   1555  2.05  
LINK         NE2 HIS A 140                FE    FE A 501     1555   1555  2.08  
LINK         O   HOH A 505                FE    FE A 501     1555   1555  2.15  
CISPEP   1 SER A  158    PRO A  159          0        -0.61                     
SITE     1 AC1  6 GLN A  34  ARG A 123  ALA A 131  TYR A 132                    
SITE     2 AC1  6 HOH A 553  HOH A 630                                          
SITE     1 AC2  4 HIS A  86  HIS A  88  HIS A 140  HOH A 505                    
CRYST1   57.484   57.484  122.804  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      0.017396  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017396  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008143        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system