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Database: PDB
Entry: 4OWZ
LinkDB: 4OWZ
Original site: 4OWZ 
HEADER    HYDROLASE                               04-FEB-14   4OWZ              
TITLE     STRUCTURE OF ECP/H15A MUTANT.                                         
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;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606;                                                
SOURCE   4 TISSUE: BONE MARROW;                                                 
SOURCE   5 CELL: EOSINOPHIL;                                                    
SOURCE   6 GENE: ECP,RNASE3,RNS3;                                               
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET11C                                    
KEYWDS    RNASE 3, EOSINOPHIL CATIONIC PROTEIN                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.A.BLANCO,V.A.SALAZAR,E.BOIX,M.MOUSSAOUI                             
REVDAT   1   04-MAR-15 4OWZ    0                                                
JRNL        AUTH   J.A.BLANCO,V.A.SALAZAR,E.BOIX,M.MOUSSAOUI                    
JRNL        TITL   STRUCTURE OF A ECP/H15A MUTANT AT 1.47 ANGSTROMS RESOLUTION  
JRNL        REF    TO BE PUBLISHED                                              
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.47 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) : 1.47                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.45                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 60201                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.050                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3038                            
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 25.4560 -  4.1135    1.00     2861   163  0.1883 0.2141        
REMARK   3     2  4.1135 -  3.2672    1.00     2666   172  0.1655 0.1453        
REMARK   3     3  3.2672 -  2.8548    1.00     2652   144  0.1910 0.2232        
REMARK   3     4  2.8548 -  2.5941    1.00     2638   143  0.2130 0.2574        
REMARK   3     5  2.5941 -  2.4083    1.00     2635   114  0.2169 0.2494        
REMARK   3     6  2.4083 -  2.2664    1.00     2611   147  0.2148 0.2221        
REMARK   3     7  2.2664 -  2.1529    1.00     2589   129  0.2120 0.2439        
REMARK   3     8  2.1529 -  2.0593    1.00     2585   158  0.2112 0.2177        
REMARK   3     9  2.0593 -  1.9800    1.00     2591   146  0.2200 0.2714        
REMARK   3    10  1.9800 -  1.9117    1.00     2582   138  0.2234 0.2544        
REMARK   3    11  1.9117 -  1.8520    1.00     2578   135  0.2185 0.2627        
REMARK   3    12  1.8520 -  1.7990    1.00     2575   127  0.2438 0.2689        
REMARK   3    13  1.7990 -  1.7517    1.00     2551   148  0.2409 0.2837        
REMARK   3    14  1.7517 -  1.7090    1.00     2549   140  0.2396 0.2906        
REMARK   3    15  1.7090 -  1.6701    1.00     2577   129  0.2407 0.2525        
REMARK   3    16  1.6701 -  1.6346    1.00     2575   131  0.2397 0.2748        
REMARK   3    17  1.6346 -  1.6019    1.00     2519   146  0.2420 0.2696        
REMARK   3    18  1.6019 -  1.5717    1.00     2560   150  0.2545 0.3171        
REMARK   3    19  1.5717 -  1.5436    1.00     2572   125  0.2665 0.2883        
REMARK   3    20  1.5436 -  1.5174    1.00     2563   118  0.2666 0.3014        
REMARK   3    21  1.5174 -  1.4930    1.00     2562   108  0.2868 0.3260        
REMARK   3    22  1.4930 -  1.4700    1.00     2572   127  0.3165 0.3216        
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)     : 0.180            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.500           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           2452                                  
REMARK   3   ANGLE     :  1.147           3330                                  
REMARK   3   CHIRALITY :  0.049            353                                  
REMARK   3   PLANARITY :  0.005            448                                  
REMARK   3   DIHEDRAL  : 17.275            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 4OWZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-FEB-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000200166.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-DEC-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0-5.2                            
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
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   : 60201                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.470                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 175.230                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 15.90                              
REMARK 200  R MERGE                    (I) : 0.04200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 34.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.47                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.90                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.44700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.800                              
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   (%): 55.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS RESUSPENDED IN 20MM SODIUM   
REMARK 280  ACETATE BUFFER, PH 5.0, 1 UL OF SAMPLE MIXED WITH 1 UL OF           
REMARK 280  CRYSTALLISATION BUFFER (0.1M SODIUM CITRATE, PH 5.2; 8%             
REMARK 280  JEFFAMINE M-600; 10MM IRON(III) CHLORIDE), VAPOR DIFFUSION,         
REMARK 280  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       87.61650            
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      131.42475            
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       43.80825            
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       87.61650            
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       43.80825            
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      131.42475            
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 TOTAL BURIED SURFACE AREA: 8870 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL                        
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 421  LIES ON A SPECIAL POSITION.                          
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; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG B   75   NH1                                                 
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   C6   CIT A   302    FE     FE A   303              1.72            
REMARK 500   C4   CIT A   302    FE     FE A   303              1.98            
REMARK 500   O7   CIT A   302     O    HOH A   401              2.02            
REMARK 500   OD1  ASN A    39     O    HOH A   402              2.06            
REMARK 500   O    HOH B   404     O    HOH B   445              2.09            
REMARK 500   O    HOH B   418     O    HOH B   459              2.16            
REMARK 500   O4   CIT B   302     O    HOH B   401              2.17            
REMARK 500   O    HOH A   596     O    HOH A   608              2.18            
REMARK 500   C3   CIT A   302    FE     FE A   303              2.18            
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   O7   CIT A   302    FE     FE A   303     5555     1.66            
REMARK 500   C3   CIT B   302    FE     FE B   303     5555     2.06            
REMARK 500   C6   CIT B   302    FE     FE B   303     5555     1.82            
REMARK 500   O    HOH A   403     O    HOH A   443     5555     1.95            
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. =   7.7 DEGREES          
REMARK 500    CYS A  96   CA  -  CB  -  SG  ANGL. DEV. = -14.0 DEGREES          
REMARK 500    CYS A  96   CA  -  CB  -  SG  ANGL. DEV. =   9.1 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       69.79   -119.13                                   
REMARK 500    ASN B  95       56.79   -151.18                                   
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 543        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH A 545        DISTANCE =  6.30 ANGSTROMS                       
REMARK 525    HOH A 571        DISTANCE =  6.26 ANGSTROMS                       
REMARK 525    HOH A 629        DISTANCE =  6.78 ANGSTROMS                       
REMARK 525    HOH B 490        DISTANCE =  6.02 ANGSTROMS                       
REMARK 525    HOH B 522        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH B 525        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH B 546        DISTANCE =  6.39 ANGSTROMS                       
REMARK 525    HOH B 564        DISTANCE =  6.78 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 303  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CIT A 302   O5                                                     
REMARK 620 2 CIT A 302   O6   58.6                                              
REMARK 620 3 HOH A 403   O    95.7  60.4                                        
REMARK 620 4 CIT A 302   O1   91.4  78.6 125.4                                  
REMARK 620 5 CIT A 302   O3  106.7 116.7 151.1  38.4                            
REMARK 620 6 HOH A 401   O    88.1 129.3  89.8 144.6 108.5                      
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  104.1                                              
REMARK 620 3 HOH B 408   O    92.1 133.1                                        
REMARK 620 4 HOH B 418   O   171.5  81.7  88.2                                  
REMARK 620 5 CIT B 302   O7  104.1   0.0 133.1  81.7                            
REMARK 620 6 CIT B 302   O5   76.9  42.1 103.2 111.3  42.1                      
REMARK 620 7 CIT B 302   O6   90.3  17.4 124.8  96.5  17.4  25.4                
REMARK 620 8 HOH B 404   O    82.6 149.8  74.8  89.3 149.8 159.4 159.5          
REMARK 620 N                    1     2     3     4     5     6     7           
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 FE                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CIT                       
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 FE                        
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4A2Y   RELATED DB: PDB                                   
REMARK 900 ECP IN COMPLEX WITH CITRATE AND IRON AT 1.7 A RESOLUTION             
REMARK 900 RELATED ID: 4OXB   RELATED DB: PDB                                   
REMARK 900 ECP IN COMPLEX WITH SULPHATE ANIONS                                  
REMARK 900 RELATED ID: 4OXF   RELATED DB: PDB                                   
REMARK 900 ECP IN COMPLEX WITH CITRATE AND IRON IONS                            
DBREF  4OWZ A    1   133  UNP    P12724   ECP_HUMAN       28    160             
DBREF  4OWZ B    1   133  UNP    P12724   ECP_HUMAN       28    160             
SEQADV 4OWZ MET A    0  UNP  P12724              INITIATING METHIONINE          
SEQADV 4OWZ ALA A   15  UNP  P12724    HIS    42 ENGINEERED MUTATION            
SEQADV 4OWZ ARG A   97  UNP  P12724    THR   124 VARIANT                        
SEQADV 4OWZ MET B    0  UNP  P12724              INITIATING METHIONINE          
SEQADV 4OWZ ALA B   15  UNP  P12724    HIS    42 ENGINEERED MUTATION            
SEQADV 4OWZ 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 ALA 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 ALA 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     FE  A 303       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    4(C6 H8 O7)                                                  
FORMUL   5   FE    2(FE 3+)                                                     
FORMUL   9  HOH   *410(H2 O)                                                    
HELIX    1 AA1 THR A    6  ILE A   16  1                                  11    
HELIX    2 AA2 ARG A   22  MET A   27  1                                   6    
HELIX    3 AA3 MET A   27  ASN A   32  1                                   6    
HELIX    4 AA4 THR A   47  CYS A   55  1                                   9    
HELIX    5 AA5 THR B    6  ILE B   16  1                                  11    
HELIX    6 AA6 ARG B   22  MET B   27  1                                   6    
HELIX    7 AA7 MET B   27  ASN B   32  1                                   6    
HELIX    8 AA8 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  ALA A  99   N  ASP A  84           
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  2.05  
SSBOND   2 CYS A   37    CYS A   96                          1555   1555  2.02  
SSBOND   3 CYS A   55    CYS A  111                          1555   1555  2.03  
SSBOND   4 CYS A   62    CYS A   71                          1555   1555  2.05  
SSBOND   5 CYS B   23    CYS B   83                          1555   1555  2.05  
SSBOND   6 CYS B   37    CYS B   96                          1555   1555  2.03  
SSBOND   7 CYS B   55    CYS B  111                          1555   1555  2.04  
SSBOND   8 CYS B   62    CYS B   71                          1555   1555  2.04  
LINK         O5  CIT A 302                FE    FE A 303     1555   1555  2.05  
LINK         O6  CIT A 302                FE    FE A 303     1555   1555  2.32  
LINK        FE    FE A 303                 O   HOH A 403     1555   1555  2.18  
LINK         O1  CIT B 302                FE    FE B 303     1555   1555  2.61  
LINK         O7  CIT B 302                FE    FE B 303     1555   1555  2.09  
LINK        FE    FE B 303                 O   HOH B 408     1555   1555  1.79  
LINK        FE    FE B 303                 O   HOH B 418     1555   1555  2.10  
LINK         O1  CIT A 302                FE    FE A 303     1555   5555  2.12  
LINK         O3  CIT A 302                FE    FE A 303     1555   5555  2.38  
LINK        FE    FE A 303                 O   HOH A 401     1555   5555  2.04  
LINK         O7  CIT B 302                FE    FE B 303     1555   5555  1.77  
LINK         O5  CIT B 302                FE    FE B 303     1555   5555  2.62  
LINK         O6  CIT B 302                FE    FE B 303     1555   5555  1.98  
LINK        FE    FE B 303                 O   HOH B 404     1555   5555  2.30  
SITE     1 AC1 10 THR A  46  ASN A  50  SER A  74  ARG A  75                    
SITE     2 AC1 10 PHE A  76  TYR A 107  HOH A 427  HOH A 459                    
SITE     3 AC1 10 HOH A 514  ARG B 121                                          
SITE     1 AC2  9 ARG A  34  ARG A  36  CYS A  37  LYS A  38                    
SITE     2 AC2  9 ASN A  39   FE A 303  HOH A 401  HOH A 403                    
SITE     3 AC2  9 HOH A 410                                                     
SITE     1 AC3  3 CIT A 302  HOH A 401  HOH A 403                               
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 B 405  HOH B 423                    
SITE     4 AC4 13 HOH B 532                                                     
SITE     1 AC5 10 ARG B  34  CYS B  37  LYS B  38  ASN B  39                    
SITE     2 AC5 10  FE B 303  HOH B 401  HOH B 404  HOH B 408                    
SITE     3 AC5 10 HOH B 418  HOH B 419                                          
SITE     1 AC6  4 CIT B 302  HOH B 404  HOH B 408  HOH B 418                    
CRYST1   62.543   62.543  175.233  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      0.015989  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015989  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005707        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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