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Database: PDB
Entry: 1DYT
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Original site: 1DYT 
HEADER    HYDROLASE                               08-FEB-00   1DYT              
TITLE     X-RAY CRYSTAL STRUCTURE OF ECP (RNASE 3) AT 1.75 A                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EOSINOPHIL CATIONIC PROTEIN;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: RIBONUCLEASE 3;                                             
COMPND   5 EC: 3.1.27.-;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELL: EOSINOPHIL;                                                    
SOURCE   6 GENE: RNASE3;                                                        
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    HYDROLASE, EOSINOPHIL CATIONIC PROTEIN, ECP, RNASE 3                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.MALLORQUI-FERNANDEZ,J.POUS,R.PERACAULA,T.MAEDA,H.TADA,              
AUTHOR   2 H.YAMADA,M.SENO,R.DE LLORENS,F.X.GOMIS-RUETH,M.COLL                  
REVDAT   2   24-FEB-09 1DYT    1       VERSN                                    
REVDAT   1   08-FEB-01 1DYT    0                                                
JRNL        AUTH   G.MALLORQUI-FERNANDEZ,J.POUS,R.PERACAULA,T.MAEDA,            
JRNL        AUTH 2 H.TADA,H.YAMADA,M.SENO,R.DE LLORENS,                         
JRNL        AUTH 3 F.X.GOMIS-RUETH,M.COLL                                       
JRNL        TITL   THREE-DIMENSIONAL CRYSTAL STRUCTURE OF HUMAN                 
JRNL        TITL 2 EOSINOPHIL CATIONIC PROTEIN (RNASE 3) AT 1.75 A              
JRNL        TITL 3 RESOLUTION.                                                  
JRNL        REF    J.MOL.BIOL.                   V. 300  1297 2000              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   10903870                                                     
JRNL        DOI    10.1006/JMBI.2000.3939                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.9                                              
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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20                             
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000                          
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 31866                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : MLF                             
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.0                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 3524                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.00008                         
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            : 2205                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 54                                      
REMARK   3   SOLVENT ATOMS            : 332                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.403                         
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.013                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.752                           
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) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : DENSITY MODIFICATION                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : CIT_XPLOR_PAR.TXT                              
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN_REP.TOP                                
REMARK   3  TOPOLOGY FILE  2   : WATER_REP.TOP                                  
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : CIT_XPLOR_TOP.TXT                              
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1DYT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  09-FEB-00.                 
REMARK 100 THE PDBE ID CODE IS EBI-4595.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.20                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ELETTRA                            
REMARK 200  BEAMLINE                       : 5.2R                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.05271                            
REMARK 200  MONOCHROMATOR                  : TOROIDAL MIRROR                    
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35401                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 22.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 1.900                              
REMARK 200  R MERGE                    (I) : 0.03300                            
REMARK 200  R SYM                      (I) : 0.03300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.03000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.03000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.750                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: EOSINOPHIL DERIVED PROTEIN                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 50                                         
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.8                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% JEFFAMINE M-600,                      
REMARK 280  0.1M SODIUM CITRATE PH 5.2, 0.01M IRON CHLORIDE                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 2 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,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z+1/2                                             
REMARK 290       7555   Y,X,-Z+1/4                                              
REMARK 290       8555   -Y,-X,-Z+3/4                                            
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       87.29500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      130.94250            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       43.64750            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       87.29500            
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       43.64750            
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      130.94250            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 GENERATING THE BIOMOLECULE                                           
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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 350                                                                      
REMARK 350 BIOMOLECULE:  2                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER;                                
REMARK 480 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 480 I=INSERTION CODE):                                                   
REMARK 480   M RES CSSEQI  ATOMS                                                
REMARK 480     ARG A  22    CG   CD   NE   CZ  NH1  NH2                         
REMARK 480     ARG A  28   NH1  NH2                                             
REMARK 480     GLN A  58   NE2                                                  
REMARK 480     ARG A  77    CZ  NH1  NH2                                        
REMARK 480     GLN A  91    CD  OE1  NE2                                        
REMARK 480     ASN A  92     O  OD1  ND2                                        
REMARK 480     ARG A  97    NE   CZ  NH1  NH2                                   
REMARK 480     ARG A 101   NH1  NH2                                             
REMARK 480     ARG A 105    CZ  NH1  NH2                                        
REMARK 480     ARG B  22    CG   CD   NE   CZ  NH1  NH2                         
REMARK 480     ARG B  36    NE   CZ  NH2                                        
REMARK 480     ASN B  57   OD1  ND2                                             
REMARK 480     ARG B  61    CZ  NH1  NH2                                        
REMARK 480     ARG B  66    CZ  NH1  NH2                                        
REMARK 480     ASN B  69   ND2                                                  
REMARK 480     ARG B  75    CD   NE   CZ  NH1  NH2                              
REMARK 480     ARG B  97    CZ  NH1  NH2                                        
REMARK 480     ARG B 101    CD   NE   CZ  NH1  NH2                              
REMARK 480     ARG B 104    CG   CD   NE                                        
REMARK 480     ARG B 105    NE   CZ  NH1  NH2                                   
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   OD1  ASN A    95  -  O    HOH A  2148              2.02            
REMARK 500   O    HOH A  2094  -  O    HOH A  2140              2.03            
REMARK 500   O    HOH A  2113  -  O    HOH A  2119              2.09            
REMARK 500   O    HOH A  2117  -  O    HOH A  2119              2.15            
REMARK 500   O    HOH A  2138  -  O    HOH A  2140              2.17            
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                                                                      
REMARK 500   O    HOH A  2093     O    HOH A  2093     5656      0.43           
REMARK 500   O    HOH A  2113     O    HOH A  2113     5556      0.43           
REMARK 500   O    HOH B  2046     O    HOH B  2046     8775      0.32           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    CYS A  96   CA  -  CB  -  SG  ANGL. DEV. =  10.1 DEGREES          
REMARK 500    ARG B  34   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 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 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    THR A  46     -157.80   -153.54                                   
REMARK 500    PRO B  21     -169.58    -77.66                                   
REMARK 500    ARG B  66      -15.73    -48.29                                   
REMARK 500    ASN B  87       70.81   -118.63                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ARG A  66        24.8      L          L   OUTSIDE RANGE           
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 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 300  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CIT A 302   O6                                                     
REMARK 620 2 CIT A 302   O4   52.1                                              
REMARK 620 3 CIT A 302   O7  126.8 114.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B 300  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CIT B 302   O5                                                     
REMARK 620 2 CIT B 302   O7  102.8                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE B 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE A 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 302                 
DBREF  1DYT A    1   133  UNP    P12724   ECP_HUMAN       28    160             
DBREF  1DYT B    1   133  UNP    P12724   ECP_HUMAN       28    160             
SEQRES   1 A  133  ARG PRO PRO GLN PHE THR ARG ALA GLN TRP PHE ALA ILE          
SEQRES   2 A  133  GLN HIS ILE SER LEU ASN PRO PRO ARG CYS THR ILE ALA          
SEQRES   3 A  133  MET ARG ALA ILE ASN ASN TYR ARG TRP ARG CYS LYS ASN          
SEQRES   4 A  133  GLN ASN THR PHE LEU ARG THR THR PHE ALA ASN VAL VAL          
SEQRES   5 A  133  ASN VAL CYS GLY ASN GLN SER ILE ARG CYS PRO HIS ASN          
SEQRES   6 A  133  ARG THR LEU ASN ASN CYS HIS ARG SER ARG PHE ARG VAL          
SEQRES   7 A  133  PRO LEU LEU HIS CYS ASP LEU ILE ASN PRO GLY ALA GLN          
SEQRES   8 A  133  ASN ILE SER ASN CYS ARG TYR ALA ASP ARG PRO GLY ARG          
SEQRES   9 A  133  ARG PHE TYR VAL VAL ALA CYS ASP ASN ARG ASP PRO ARG          
SEQRES  10 A  133  ASP SER PRO ARG TYR PRO VAL VAL PRO VAL HIS LEU ASP          
SEQRES  11 A  133  THR THR ILE                                                  
SEQRES   1 B  133  ARG PRO PRO GLN PHE THR ARG ALA GLN TRP PHE ALA ILE          
SEQRES   2 B  133  GLN HIS ILE SER LEU ASN PRO PRO ARG CYS THR ILE ALA          
SEQRES   3 B  133  MET ARG ALA ILE ASN ASN TYR ARG TRP ARG CYS LYS ASN          
SEQRES   4 B  133  GLN ASN THR PHE LEU ARG THR THR PHE ALA ASN VAL VAL          
SEQRES   5 B  133  ASN VAL CYS GLY ASN GLN SER ILE ARG CYS PRO HIS ASN          
SEQRES   6 B  133  ARG THR LEU ASN ASN CYS HIS ARG SER ARG PHE ARG VAL          
SEQRES   7 B  133  PRO LEU LEU HIS CYS ASP LEU ILE ASN PRO GLY ALA GLN          
SEQRES   8 B  133  ASN ILE SER ASN CYS ARG TYR ALA ASP ARG PRO GLY ARG          
SEQRES   9 B  133  ARG PHE TYR VAL VAL ALA CYS ASP ASN ARG ASP PRO ARG          
SEQRES  10 B  133  ASP SER PRO ARG TYR PRO VAL VAL PRO VAL HIS LEU ASP          
SEQRES  11 B  133  THR THR ILE                                                  
HET     FE  B 300       1                                                       
HET     FE  A 300       1                                                       
HET    CIT  A 301      13                                                       
HET    CIT  B 301      13                                                       
HET    CIT  A 302      13                                                       
HET    CIT  B 302      13                                                       
HETNAM      FE FE (III) ION                                                     
HETNAM     CIT CITRIC ACID                                                      
HETSYN     CIT CITRATE                                                          
FORMUL   3   FE    2(FE 3+)                                                     
FORMUL   5  CIT    4(C6 H8 O7)                                                  
FORMUL   9  HOH   *332(H2 O1)                                                   
HELIX    1   1 THR A    6  ILE A   16  1                                  11    
HELIX    2   2 ARG A   22  MET A   27  1                                   6    
HELIX    3   3 MET A   27  ASN A   32  1                                   6    
HELIX    4   4 THR A   47  CYS A   55  1                                   9    
HELIX    5   5 THR B    6  ILE B   16  1                                  11    
HELIX    6   6 ARG B   22  MET B   27  1                                   6    
HELIX    7   7 MET B   27  ASN B   32  1                                   6    
HELIX    8   8 THR B   47  CYS B   55  1                                   9    
HELIX    9   9 ASN B   92  CYS B   96  5                                   5    
SHEET    1   A 3 GLN A  40  LEU A  44  0                                        
SHEET    2   A 3 VAL A  78  LEU A  85 -1  O  LEU A  81   N  PHE A  43           
SHEET    3   A 3 TYR A  98  ARG A 105 -1  O  ALA A  99   N  ASP A  84           
SHEET    1   B 4 SER A  59  ILE A  60  0                                        
SHEET    2   B 4 CYS A  71  ARG A  73                                           
SHEET    3   B 4 TYR A 107  ASN A 113 -1  O  VAL A 109   N  HIS A  72           
SHEET    4   B 4 VAL A 124  THR A 132 -1  O  VAL A 125   N  ASP A 112           
SHEET    1   C 3 GLN B  40  LEU B  44  0                                        
SHEET    2   C 3 VAL B  78  LEU B  85 -1  O  LEU B  81   N  PHE B  43           
SHEET    3   C 3 TYR B  98  ARG B 105 -1  O  ALA B  99   N  ASP B  84           
SHEET    1   D 4 SER B  59  ILE B  60  0                                        
SHEET    2   D 4 CYS B  71  ARG B  73                                           
SHEET    3   D 4 TYR B 107  ASN B 113 -1  O  VAL B 109   N  HIS B  72           
SHEET    4   D 4 VAL B 124  THR B 132 -1  O  VAL B 125   N  ASP B 112           
SSBOND   1 CYS A   23    CYS A   83                          1555   1555  2.03  
SSBOND   2 CYS A   37    CYS A   96                          1555   1555  1.99  
SSBOND   3 CYS A   55    CYS A  111                          1555   1555  2.05  
SSBOND   4 CYS A   62    CYS A   71                          1555   1555  2.02  
SSBOND   5 CYS B   23    CYS B   83                          1555   1555  2.04  
SSBOND   6 CYS B   37    CYS B   96                          1555   1555  2.01  
SSBOND   7 CYS B   55    CYS B  111                          1555   1555  2.04  
SSBOND   8 CYS B   62    CYS B   71                          1555   1555  2.03  
LINK        FE    FE A 300                 O6  CIT A 302     1555   5656  1.52  
LINK        FE    FE A 300                 O4  CIT A 302     1555   1555  2.28  
LINK        FE    FE A 300                 O7  CIT A 302     1555   1555  2.27  
LINK        FE    FE A 300                 O7  CIT A 302     1555   5656  2.32  
LINK        FE    FE A 300                 O6  CIT A 302     5656   1555  1.52  
LINK        FE    FE A 300                 C3  CIT A 302     5656   1555  1.60  
LINK        FE    FE B 300                 O7  CIT B 302     1555   5656  1.64  
LINK        FE    FE B 300                 C3  CIT B 302     5656   1555  1.58  
LINK        FE    FE B 300                 O7  CIT B 302     5656   1555  1.64  
LINK        FE    FE B 300                 C2  CIT B 302     5656   1555  1.79  
LINK        FE    FE B 300                 O5  CIT B 302     1555   5656  2.48  
SITE     1 AC1  3 ARG B  34  CIT B 302  HOH B2144                               
SITE     1 AC2  1 CIT A 302                                                     
SITE     1 AC3 13 THR A  46  ASN A  50  VAL A  54  SER A  74                    
SITE     2 AC3 13 ARG A  75  PHE A  76  VAL A  78  TYR A 107                    
SITE     3 AC3 13 HOH A2109  HOH A2180  HOH A2181  HOH A2182                    
SITE     4 AC3 13 ARG B 121                                                     
SITE     1 AC4 13 ARG A  61  ARG A  66  THR B  46  ASN B  50                    
SITE     2 AC4 13 VAL B  54  SER B  74  ARG B  75  PHE B  76                    
SITE     3 AC4 13 VAL B  78  TYR B 107  HOH B2083  HOH B2142                    
SITE     4 AC4 13 HOH B2143                                                     
SITE     1 AC5 10 ARG A  34  LYS A  38  ASN A  39  GLN A  40                    
SITE     2 AC5 10  FE A 300  HOH A2094  HOH A2096  HOH A2183                    
SITE     3 AC5 10 HOH A2184  HOH A2185                                          
SITE     1 AC6 12 ARG B  34  ARG B  36  CYS B  37  LYS B  38                    
SITE     2 AC6 12 ASN B  39  GLN B  40   FE B 300  HOH B2068                    
SITE     3 AC6 12 HOH B2144  HOH B2145  HOH B2146  HOH B2147                    
CRYST1   62.163   62.163  174.590  90.00  90.00  90.00 P 43 2 2     16          
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      0.016087  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016087  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005728        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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