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Database: PDB
Entry: 4OXF
LinkDB: 4OXF
Original site: 4OXF 
HEADER    HYDROLASE                               05-FEB-14   4OXF              
TITLE     STRUCTURE OF ECP IN COMPLEX WITH CITRATE IONS AT 1.50 ANGSTROMS       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EOSINOPHIL CATIONIC PROTEIN;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ECP, RIBONUCLEASE 3, RNASE 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 TISSUE: BONE MARROW;                                                 
SOURCE   6 CELL: EOSINOPHIL;                                                    
SOURCE   7 GENE: ECP,RNASE3,RNS3;                                               
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  11 EXPRESSION_SYSTEM_CELL: BACTERIA;                                    
SOURCE  12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  13 EXPRESSION_SYSTEM_PLASMID: PET11C                                    
KEYWDS    RNASE 3, EOSINOPHIL CATIONIC PROTEIN (ECP)                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.A.BLANCO,E.BOIX,M.MOUSSAOUI,V.A.SALAZAR                             
REVDAT   1   04-MAR-15 4OXF    0                                                
JRNL        AUTH   J.A.BLANCO,E.BOIX,M.MOUSSAOUI,V.A.SALAZAR                    
JRNL        TITL   STRUCTURE OF ECP IN COMPLEX WITH CITRATE IONS AT 1.50        
JRNL        TITL 2 ANGSTROMS                                                    
JRNL        REF    TO BE PUBLISHED                                              
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   G.MALLORQUI-FERNANDEZ,J.POUS,R.PERACAULA,J.AYMAMI,T.MAEDA,   
REMARK   1  AUTH 2 H.TADA,H.YAMADA,M.SENO,R.DE LLORENS,F.X.GOMIS-RUTH,M.COLL    
REMARK   1  TITL   THREE-DIMENSIONAL CRYSTAL STRUCTURE OF HUMAN EOSINOPHIL      
REMARK   1  TITL 2 CATIONIC PROTEIN (RNASE 3) AT 1.75 A RESOLUTION.             
REMARK   1  REF    J.MOL.BIOL.                   V. 300  1297 2000              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   10903870                                                     
REMARK   1  DOI    10.1006/JMBI.2000.3939                                       
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   E.BOIX,D.PULIDO,M.MOUSSAOUI,M.V.NOGUES,S.RUSSI               
REMARK   1  TITL   THE SULFATE-BINDING SITE STRUCTURE OF THE HUMAN EOSINOPHIL   
REMARK   1  TITL 2 CATIONIC PROTEIN AS REVEALED BY A NEW CRYSTAL FORM.          
REMARK   1  REF    J.STRUCT.BIOL.                V. 179     1 2012              
REMARK   1  REFN                   ESSN 1095-8657                               
REMARK   1  PMID   22579681                                                     
REMARK   1  DOI    10.1016/J.JSB.2012.04.023                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.4_1496)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.88                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 55982                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2834                            
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 50.9114 -  4.0710    0.94     2813   140  0.1836 0.2276        
REMARK   3     2  4.0710 -  3.2314    0.96     2688   144  0.1595 0.1673        
REMARK   3     3  3.2314 -  2.8230    0.98     2685   135  0.1932 0.2226        
REMARK   3     4  2.8230 -  2.5649    0.98     2660   151  0.2014 0.2393        
REMARK   3     5  2.5649 -  2.3810    0.98     2646   141  0.1991 0.2742        
REMARK   3     6  2.3810 -  2.2407    0.99     2654   129  0.1998 0.2548        
REMARK   3     7  2.2407 -  2.1284    0.99     2670   147  0.2091 0.2434        
REMARK   3     8  2.1284 -  2.0358    0.99     2657   143  0.2032 0.2450        
REMARK   3     9  2.0358 -  1.9574    0.99     2600   159  0.2110 0.2596        
REMARK   3    10  1.9574 -  1.8899    0.99     2678   132  0.2101 0.2350        
REMARK   3    11  1.8899 -  1.8308    1.00     2651   145  0.2153 0.2363        
REMARK   3    12  1.8308 -  1.7784    1.00     2653   127  0.2276 0.2718        
REMARK   3    13  1.7784 -  1.7316    1.00     2644   142  0.2281 0.2441        
REMARK   3    14  1.7316 -  1.6894    1.00     2630   144  0.2233 0.2430        
REMARK   3    15  1.6894 -  1.6510    1.00     2657   135  0.2256 0.2258        
REMARK   3    16  1.6510 -  1.6158    1.00     2636   155  0.2283 0.2561        
REMARK   3    17  1.6158 -  1.5835    1.00     2620   162  0.2431 0.2669        
REMARK   3    18  1.5835 -  1.5536    1.00     2647   125  0.2459 0.2862        
REMARK   3    19  1.5536 -  1.5259    1.00     2592   151  0.2524 0.3187        
REMARK   3    20  1.5259 -  1.5000    1.00     2667   127  0.2570 0.2748        
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)     : 0.150            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.600           
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      :  0.007           2465                                  
REMARK   3   ANGLE     :  1.149           3354                                  
REMARK   3   CHIRALITY :  0.049            356                                  
REMARK   3   PLANARITY :  0.006            451                                  
REMARK   3   DIHEDRAL  : 18.228            970                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 4OXF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-FEB-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000200187.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUL-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0 - 5.2                          
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALBA                               
REMARK 200  BEAMLINE                       : XALOC                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61922                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 52.530                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 8.600                              
REMARK 200  R MERGE                    (I) : 0.03000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 32.3000                            
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) : 1.62                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
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         : 3.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.97                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN RESUSPENDED IN SODIUM            
REMARK 280  CACODYLATE BUFFER (20MM, PH5.0). 1 UL OF PROTEIN SAMPLE WAS         
REMARK 280  MIXED WITH 1 UL OF CRYSTALLISATION BUFFER (0.1M SODIUM CITRATE      
REMARK 280  PH5.2, 8% JEFFAMINE M-600, 10MM IRON(III) CHLORIDE), VAPOR          
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
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       87.52500            
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      131.28750            
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       43.76250            
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       87.52500            
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       43.76250            
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      131.28750            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      -62.53500            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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 B     0                                                      
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   O2   CIT B   302     O    HOH B   401              1.92            
REMARK 500   CG   ARG A   101     O    HOH A   591              1.97            
REMARK 500   OE1  GLN B    58     O    HOH B   402              2.09            
REMARK 500   O6   CIT A   302     O    HOH A   401              2.13            
REMARK 500   C4   CIT B   302    FE     FE B   303              2.14            
REMARK 500   O6   CIT B   302     O    HOH B   403              2.15            
REMARK 500   O    HOH A   433     O    HOH A   470              2.15            
REMARK 500   O    ILE A    93     O    HOH A   536              2.18            
REMARK 500   O    HOH A   404     O    HOH A   449              2.19            
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   NH2  ARG A    34     O7   CIT A   302     5455     1.96            
REMARK 500   C3   CIT A   302    FE     FE A   304     5455     2.17            
REMARK 500   C4   CIT A   302    FE     FE A   304     5455     1.96            
REMARK 500   C6   CIT A   302    FE     FE A   304     5455     1.97            
REMARK 500   C3   CIT B   302    FE     FE B   303     5455     2.00            
REMARK 500   C6   CIT B   302    FE     FE B   303     5455     1.57            
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  37   CA  -  CB  -  SG  ANGL. DEV. =   7.1 DEGREES          
REMARK 500    CYS A  96   CA  -  CB  -  SG  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    CYS A  96   CA  -  CB  -  SG  ANGL. DEV. = -13.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN B  87       69.10   -119.43                                   
REMARK 500    ASN B  95       59.39   -145.27                                   
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 498        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH A 509        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH A 527        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH A 539        DISTANCE =  6.35 ANGSTROMS                       
REMARK 525    HOH A 571        DISTANCE =  6.20 ANGSTROMS                       
REMARK 525    HOH B 511        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH B 516        DISTANCE =  6.84 ANGSTROMS                       
REMARK 525    HOH B 547        DISTANCE =  6.19 ANGSTROMS                       
REMARK 525    HOH B 569        DISTANCE =  7.10 ANGSTROMS                       
REMARK 525    HOH B 578        DISTANCE =  5.90 ANGSTROMS                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 AUTHORS STATE THAT BOTH IRON AND CITRATE ATOMS HAVE BEEN ADJUSTED    
REMARK 600 TO THE CORRESPONDING ELECTRON DENSITY. CIT302 SURROUNDS THE SAME-    
REMARK 600 CHAIN IRON ATOM, WHICH CAN ALSO COORDINATE SOME SURROUNDING WATER    
REMARK 600 MOLECULES. THESE HAVE BEEN DIFFICULT TO ADJUST AS THE ELECTRON       
REMARK 600 DENSITY AROUND THE IRON ATOMS IS NOT SPHERICAL AND THE WATER         
REMARK 600 MOLECULES THERE WOULD NOT HAVE A DEFINED FIXED POSITION. THE         
REMARK 600 SURROUNDING CITRATE LIGAND ALSO SHOWED HIGH MOBILITY. THESE          
REMARK 600 PROBLEMS ALTOGETHER MAKE REFINEMENT STEPS MOVE THE CITRATE LIGAND    
REMARK 600 IN SUCH A POSITION THAT CLASHES APPEARED.                            
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 304  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CIT A 302   O1                                                     
REMARK 620 2 CIT A 302   O4   81.7                                              
REMARK 620 3 CIT A 302   O7   71.5  99.9                                        
REMARK 620 4 CIT A 302   O5   82.3  62.1  40.9                                  
REMARK 620 5 HOH A 451   O   176.3 101.5 109.6 100.9                            
REMARK 620 6 HOH A 422   O    93.7 172.1  84.5 123.8  83.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B 303  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CIT B 302   O1                                                     
REMARK 620 2 CIT B 302   O7   83.5                                              
REMARK 620 3 HOH B 405   O   107.9  73.9                                        
REMARK 620 4 CIT B 302   O4   77.4  77.0 149.6                                  
REMARK 620 5 CIT B 302   O5   83.8  34.2 106.3  43.6                            
REMARK 620 6 CIT B 302   O6  111.0  40.6  93.5  57.7  27.5                      
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 CIT                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CIT                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CIT                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CIT                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CIT                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE                        
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4A2Y   RELATED DB: PDB                                   
REMARK 900 ECP IN COMPLEX WITH CITRATE IONS AT 1.7 A RESOLUTION                 
REMARK 900 RELATED ID: 4OWZ   RELATED DB: PDB                                   
REMARK 900 ECP/H15A MUTANT IN COMPLEX WITH CITRATE AND IRON IONS                
REMARK 900 RELATED ID: 4OXB   RELATED DB: PDB                                   
REMARK 900 ECP IN COMPLEX WITH SULPHATE IONS                                    
DBREF  4OXF A    1   133  UNP    P12724   ECP_HUMAN       28    160             
DBREF  4OXF B    1   133  UNP    P12724   ECP_HUMAN       28    160             
SEQADV 4OXF MET A    0  UNP  P12724              INITIATING METHIONINE          
SEQADV 4OXF ARG A   97  UNP  P12724    THR   124 VARIANT                        
SEQADV 4OXF MET B    0  UNP  P12724              INITIATING METHIONINE          
SEQADV 4OXF ARG B   97  UNP  P12724    THR   124 VARIANT                        
SEQRES   1 A  134  MET ARG PRO PRO GLN PHE THR ARG ALA GLN TRP PHE ALA          
SEQRES   2 A  134  ILE GLN HIS ILE SER LEU ASN PRO PRO ARG CYS THR ILE          
SEQRES   3 A  134  ALA MET ARG ALA ILE ASN ASN TYR ARG TRP ARG CYS LYS          
SEQRES   4 A  134  ASN GLN ASN THR PHE LEU ARG THR THR PHE ALA ASN VAL          
SEQRES   5 A  134  VAL ASN VAL CYS GLY ASN GLN SER ILE ARG CYS PRO HIS          
SEQRES   6 A  134  ASN ARG THR LEU ASN ASN CYS HIS ARG SER ARG PHE ARG          
SEQRES   7 A  134  VAL PRO LEU LEU HIS CYS ASP LEU ILE ASN PRO GLY ALA          
SEQRES   8 A  134  GLN ASN ILE SER ASN CYS ARG TYR ALA ASP ARG PRO GLY          
SEQRES   9 A  134  ARG ARG PHE TYR VAL VAL ALA CYS ASP ASN ARG ASP PRO          
SEQRES  10 A  134  ARG ASP SER PRO ARG TYR PRO VAL VAL PRO VAL HIS LEU          
SEQRES  11 A  134  ASP THR THR ILE                                              
SEQRES   1 B  134  MET ARG PRO PRO GLN PHE THR ARG ALA GLN TRP PHE ALA          
SEQRES   2 B  134  ILE GLN HIS ILE SER LEU ASN PRO PRO ARG CYS THR ILE          
SEQRES   3 B  134  ALA MET ARG ALA ILE ASN ASN TYR ARG TRP ARG CYS LYS          
SEQRES   4 B  134  ASN GLN ASN THR PHE LEU ARG THR THR PHE ALA ASN VAL          
SEQRES   5 B  134  VAL ASN VAL CYS GLY ASN GLN SER ILE ARG CYS PRO HIS          
SEQRES   6 B  134  ASN ARG THR LEU ASN ASN CYS HIS ARG SER ARG PHE ARG          
SEQRES   7 B  134  VAL PRO LEU LEU HIS CYS ASP LEU ILE ASN PRO GLY ALA          
SEQRES   8 B  134  GLN ASN ILE SER ASN CYS ARG TYR ALA ASP ARG PRO GLY          
SEQRES   9 B  134  ARG ARG PHE TYR VAL VAL ALA CYS ASP ASN ARG ASP PRO          
SEQRES  10 B  134  ARG ASP SER PRO ARG TYR PRO VAL VAL PRO VAL HIS LEU          
SEQRES  11 B  134  ASP THR THR ILE                                              
HET    CIT  A 301      13                                                       
HET    CIT  A 302      13                                                       
HET    CIT  A 303      13                                                       
HET     FE  A 304       1                                                       
HET    CIT  B 301      13                                                       
HET    CIT  B 302      13                                                       
HET     FE  B 303       1                                                       
HETNAM     CIT CITRIC ACID                                                      
HETNAM      FE FE (III) ION                                                     
FORMUL   3  CIT    5(C6 H8 O7)                                                  
FORMUL   6   FE    2(FE 3+)                                                     
FORMUL  10  HOH   *400(H2 O)                                                    
HELIX    1 AA1 THR A    6  ILE A   16  1                                  11    
HELIX    2 AA2 ARG A   22  ASN A   32  1                                  11    
HELIX    3 AA3 THR A   47  CYS A   55  1                                   9    
HELIX    4 AA4 THR B    6  ILE B   16  1                                  11    
HELIX    5 AA5 ARG B   22  MET B   27  1                                   6    
HELIX    6 AA6 MET B   27  ASN B   32  1                                   6    
HELIX    7 AA7 THR B   47  CYS B   55  1                                   9    
SHEET    1 AA1 3 GLN A  40  LEU A  44  0                                        
SHEET    2 AA1 3 VAL A  78  LEU A  85 -1  O  LEU A  81   N  PHE A  43           
SHEET    3 AA1 3 TYR A  98  ARG A 105 -1  O  ARG A 101   N  HIS A  82           
SHEET    1 AA2 3 CYS A  71  ARG A  73  0                                        
SHEET    2 AA2 3 TYR A 107  ASN A 113 -1  O  VAL A 109   N  HIS A  72           
SHEET    3 AA2 3 VAL A 124  THR A 132 -1  O  VAL A 127   N  ALA A 110           
SHEET    1 AA3 5 GLN B  40  LEU B  44  0                                        
SHEET    2 AA3 5 VAL B  78  LEU B  85 -1  O  LEU B  81   N  PHE B  43           
SHEET    3 AA3 5 TYR B  98  ASN B 113 -1  O  ALA B  99   N  ASP B  84           
SHEET    4 AA3 5 CYS B  71  ARG B  73 -1  N  HIS B  72   O  VAL B 109           
SHEET    5 AA3 5 SER B  59  ILE B  60 -1  N  ILE B  60   O  CYS B  71           
SHEET    1 AA4 4 GLN B  40  LEU B  44  0                                        
SHEET    2 AA4 4 VAL B  78  LEU B  85 -1  O  LEU B  81   N  PHE B  43           
SHEET    3 AA4 4 TYR B  98  ASN B 113 -1  O  ALA B  99   N  ASP B  84           
SHEET    4 AA4 4 VAL B 124  ILE B 133 -1  O  VAL B 127   N  ALA B 110           
SSBOND   1 CYS A   23    CYS A   83                          1555   1555  2.04  
SSBOND   2 CYS A   37    CYS A   96                          1555   1555  2.05  
SSBOND   3 CYS A   55    CYS A  111                          1555   1555  2.04  
SSBOND   4 CYS A   62    CYS A   71                          1555   1555  2.06  
SSBOND   5 CYS B   23    CYS B   83                          1555   1555  2.04  
SSBOND   6 CYS B   37    CYS B   96                          1555   1555  2.04  
SSBOND   7 CYS B   55    CYS B  111                          1555   1555  2.05  
SSBOND   8 CYS B   62    CYS B   71                          1555   1555  2.05  
LINK         O1  CIT A 302                FE    FE A 304     1555   1555  2.25  
LINK         O4  CIT A 302                FE    FE A 304     1555   1555  2.71  
LINK         O1  CIT B 302                FE    FE B 303     1555   1555  2.06  
LINK         O7  CIT B 302                FE    FE B 303     1555   1555  1.78  
LINK        FE    FE B 303                 O   HOH B 405     1555   1555  1.96  
LINK         O7  CIT A 302                FE    FE A 304     1555   5455  2.57  
LINK         O5  CIT A 302                FE    FE A 304     1555   5455  1.85  
LINK        FE    FE A 304                 O   HOH A 451     1555   5455  2.21  
LINK        FE    FE A 304                 O   HOH A 422     1555   5455  1.83  
LINK         O4  CIT B 302                FE    FE B 303     1555   5455  1.98  
LINK         O5  CIT B 302                FE    FE B 303     1555   5455  2.04  
LINK         O6  CIT B 302                FE    FE B 303     1555   5455  2.12  
SITE     1 AC1 11 THR A  46  ASN A  50  SER A  74  ARG A  75                    
SITE     2 AC1 11 PHE A  76  TYR A 107  HOH A 407  HOH A 410                    
SITE     3 AC1 11 HOH A 438  HOH A 506  ARG B 121                               
SITE     1 AC2 10 ARG A  34  CYS A  37  LYS A  38  ASN A  39                    
SITE     2 AC2 10 GLN A  40   FE A 304  HOH A 401  HOH A 408                    
SITE     3 AC2 10 HOH A 422  HOH A 451                                          
SITE     1 AC3  8 ARG A  45  HOH A 404  HOH A 425  HOH A 449                    
SITE     2 AC3  8 HOH A 514  HOH A 596  ARG B 114  PRO B 116                    
SITE     1 AC4  3 CIT A 302  HOH A 422  HOH A 451                               
SITE     1 AC5 15 ARG A  61  ARG A  66  THR B  46  ASN B  50                    
SITE     2 AC5 15 VAL B  54  ASN B  57  SER B  74  ARG B  75                    
SITE     3 AC5 15 PHE B  76  VAL B  78  TYR B 107  HOH B 411                    
SITE     4 AC5 15 HOH B 412  HOH B 487  HOH B 577                               
SITE     1 AC6  9 ARG B  34  ARG B  36  CYS B  37  LYS B  38                    
SITE     2 AC6  9 ASN B  39   FE B 303  HOH B 401  HOH B 403                    
SITE     3 AC6  9 HOH B 405                                                     
SITE     1 AC7  2 CIT B 302  HOH B 405                                          
CRYST1   62.535   62.535  175.050  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      0.015991  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015991  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005713        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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