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Database: PDB
Entry: 4A2Y
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Original site: 4A2Y 
HEADER    HYDROLASE                               29-SEP-11   4A2Y              
TITLE     STRUCTURE OF THE HUMAN EOSINOPHIL CATIONIC PROTEIN IN COMPLEX WITH    
TITLE    2 CITRATE ANIONS                                                       
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 CELL: EOSINOPHIL;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PET11C;                                    
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET11C/ECP                                
KEYWDS    HYDROLASE, OXIDOREDUCTASE, ANTIMICROBIAL, CYTOTOXIC                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.BOIX,D.PULIDO,M.MOUSSAOUI,V.NOGUES,S.RUSSI                          
REVDAT   2   17-JUL-19 4A2Y    1       REMARK                                   
REVDAT   1   27-JUN-12 4A2Y    0                                                
JRNL        AUTH   E.BOIX,D.PULIDO,M.MOUSSAOUI,V.NOGUES,S.RUSSI                 
JRNL        TITL   THE SULFATE-BINDING SITE STRUCTURE OF THE HUMAN EOSINOPHIL   
JRNL        TITL 2 CATIONIC PROTEIN AS REVEALED BY A NEW CRYSTAL FORM.          
JRNL        REF    J.STRUCT.BIOL.                V. 179     1 2012              
JRNL        REFN                   ISSN 1047-8477                               
JRNL        PMID   22579681                                                     
JRNL        DOI    10.1016/J.JSB.2012.04.023                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0110                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 62.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 36817                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1944                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2605                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.55                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2740                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 147                          
REMARK   3   BIN FREE R VALUE                    : 0.2930                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2158                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 73                                      
REMARK   3   SOLVENT ATOMS            : 310                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.44000                                              
REMARK   3    B22 (A**2) : 0.44000                                              
REMARK   3    B33 (A**2) : -0.88000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.103         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.100         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.071         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.503         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2306 ; 0.027 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3156 ; 2.280 ; 1.952       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   266 ; 6.374 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   120 ;38.861 ;22.167       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   341 ;14.402 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    32 ;18.033 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   328 ; 0.162 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1846 ; 0.013 ; 0.022       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1353 ; 1.137 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2224 ; 1.846 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   953 ; 3.451 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   931 ; 5.062 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 4A2Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-SEP-11.                  
REMARK 100 THE DEPOSITION ID IS D_1290049830.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-DEC-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X13                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8123                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36817                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 62.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.79                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1DYT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NA CITRATE, PH 5.2, 6% JEFFAMINE   
REMARK 280  M-600, 10 MM KH2PO4/K2HPO4, PH 7, 10 MM FECL3.                      
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       87.42850            
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      131.14275            
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       43.71425            
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       87.42850            
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       43.71425            
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      131.14275            
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 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  22    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 101    NH1  NH2                                            
REMARK 470     ARG B  61    CZ   NH1  NH2                                       
REMARK 470     ASN B  69    ND2                                                 
REMARK 470     ARG B  75    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG B  97    CZ   NH1  NH2                                       
REMARK 470     ARG B 101    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG B 104    CG   CD   NE                                        
REMARK 470     ARG B 105    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   ND2  ASN A    95     O    HOH A  2178              1.59            
REMARK 500   CB   VAL A    78     O    HOH A  2112              1.83            
REMARK 500   O    HOH A  2156     O    HOH A  2157              1.87            
REMARK 500   ND2  ASN A    95     O    HOH A  2173              1.92            
REMARK 500   O    HOH A  2205     O    HOH A  2214              1.94            
REMARK 500   O    HOH A  2010     O    HOH A  2011              1.98            
REMARK 500   C1   CIT A   302     O    HOH A  2092              2.00            
REMARK 500   O    HOH A  2073     O    HOH A  2167              2.01            
REMARK 500   O    HOH A  2073     O    HOH A  2168              2.02            
REMARK 500   O    HOH A  2133     O    HOH A  2136              2.06            
REMARK 500   O    HOH A  2191     O    HOH A  2192              2.11            
REMARK 500   O    HOH A  2065     O    HOH A  2189              2.14            
REMARK 500   O    HOH A  2034     O    HOH A  2035              2.14            
REMARK 500   O    HOH A  2098     O    HOH A  2176              2.14            
REMARK 500   O1   CIT B   303     O    HOH B  2066              2.15            
REMARK 500   OG1  THR A    47     O    HOH A  2116              2.16            
REMARK 500   ND2  ASN A    19     O    HOH A  2057              2.16            
REMARK 500   CG2  VAL A    78     O    HOH A  2112              2.17            
REMARK 500   O    HOH A  2116     O    HOH A  2117              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   OE1  GLN B    91     CE1  HIS B   128     5656     1.62            
REMARK 500   O    HOH A  2226     O    HOH B  2051     1545     1.98            
REMARK 500   OE1  GLN B    91     ND1  HIS B   128     5656     2.00            
REMARK 500   O    HOH A  2136     O    HOH B  2046     4465     2.02            
REMARK 500   OE1  GLN B    91     NE2  HIS B   128     5656     2.05            
REMARK 500   OD1  ASN B    39     O    HOH B  2079     5656     2.11            
REMARK 500   C1   MPD A  1134     C1   MPD A  1134     8665     2.12            
REMARK 500   NE2  GLN A    91     ND1  HIS A   128     5656     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A  37   CB    CYS A  37   SG      0.131                       
REMARK 500    CYS A  96   CB    CYS A  96   SG      0.191                       
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    ARG A   1   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A   1   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    CYS A  37   CA  -  CB  -  SG  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    ARG A  66   CG  -  CD  -  NE  ANGL. DEV. = -15.7 DEGREES          
REMARK 500    ARG A  66   NE  -  CZ  -  NH1 ANGL. DEV. =   7.6 DEGREES          
REMARK 500    ARG A  66   NE  -  CZ  -  NH2 ANGL. DEV. = -10.9 DEGREES          
REMARK 500    ASN A  92   CB  -  CA  -  C   ANGL. DEV. = -12.7 DEGREES          
REMARK 500    CYS A  96   CA  -  CB  -  SG  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    ASP A 115   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG B   7   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG B  36   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG B 114   CG  -  CD  -  NE  ANGL. DEV. = -15.5 DEGREES          
REMARK 500    ARG B 114   CD  -  NE  -  CZ  ANGL. DEV. =  11.4 DEGREES          
REMARK 500    ARG B 114   NE  -  CZ  -  NH1 ANGL. DEV. =  10.0 DEGREES          
REMARK 500    ARG B 114   NE  -  CZ  -  NH2 ANGL. DEV. = -12.3 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  95       60.66   -151.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    HIS B 128        -11.91                                           
REMARK 500    HIS B 128        -12.68                                           
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 A2022        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH A2023        DISTANCE =  6.43 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 1134                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4A2O   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE HUMAN EOSINOPHIL CATIONIC PROTEIN IN COMPLEX WITH   
REMARK 900 SULFATE ANIONS                                                       
REMARK 900 RELATED ID: 1QMT   RELATED DB: PDB                                   
REMARK 900 RECOMBINANT HUMAN EOSINOPHIL CATIONIC PROTEIN                        
REMARK 900 RELATED ID: 1H1H   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF EOSINOPHIL CATIONIC PROTEIN IN COMPLEX WITH 2', 
REMARK 900 5'-ADP AT 2.0 A RESOLUTION REVEALS THE DETAILS OF THE                
REMARK 900 RIBONUCLEOLYTIC ACTIVE SITE                                          
REMARK 900 RELATED ID: 1DYT   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF ECP (RNASE 3) AT 1.75 A                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 RECOMBINANT PROTEIN EXPRESSED USING A SYNTHETIC GENE                 
REMARK 999 (BOIX ET AL. J.BIOL.CHEM. 274, 15605) BASED ON THE NP_002926         
REMARK 999 NATURAL VARIANT (THR97ARG)                                           
DBREF  4A2Y A    1   133  UNP    P12724   ECP_HUMAN       28    160             
DBREF  4A2Y B    1   133  UNP    P12724   ECP_HUMAN       28    160             
SEQADV 4A2Y ARG A   97  UNP  P12724    THR   124 VARIANT                        
SEQADV 4A2Y ARG B   97  UNP  P12724    THR   124 VARIANT                        
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    CIT  A 301      13                                                       
HET    CIT  A 302      13                                                       
HET    MPD  A1134       8                                                       
HET    CIT  B 301      13                                                       
HET    CIT  B 302      13                                                       
HET    CIT  B 303      13                                                       
HETNAM     CIT CITRIC ACID                                                      
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
FORMUL   3  CIT    5(C6 H8 O7)                                                  
FORMUL   5  MPD    C6 H14 O2                                                    
FORMUL   9  HOH   *310(H2 O)                                                    
HELIX    1   1 THR A    6  ILE A   16  1                                  11    
HELIX    2   2 ARG A   22  ASN A   32  1                                  11    
HELIX    3   3 THR A   47  CYS A   55  1                                   9    
HELIX    4   4 THR B    6  ILE B   16  1                                  11    
HELIX    5   5 ARG B   22  MET B   27  1                                   6    
HELIX    6   6 MET B   27  ASN B   32  1                                   6    
HELIX    7   7 THR B   47  CYS B   55  1                                   9    
SHEET    1  AA 3 GLN A  40  LEU A  44  0                                        
SHEET    2  AA 3 VAL A  78  LEU A  85 -1  O  LEU A  81   N  PHE A  43           
SHEET    3  AA 3 TYR A  98  ARG A 105 -1  O  ALA A  99   N  ASP A  84           
SHEET    1  AB 3 CYS A  71  ARG A  73  0                                        
SHEET    2  AB 3 TYR A 107  ASN A 113 -1  O  VAL A 109   N  HIS A  72           
SHEET    3  AB 3 VAL A 124  THR A 132 -1  O  VAL A 125   N  ASP A 112           
SHEET    1  BA 3 GLN B  40  LEU B  44  0                                        
SHEET    2  BA 3 VAL B  78  LEU B  85 -1  O  LEU B  81   N  PHE B  43           
SHEET    3  BA 3 TYR B  98  ARG B 105 -1  O  ALA B  99   N  ASP B  84           
SHEET    1  BB 4 SER B  59  ILE B  60  0                                        
SHEET    2  BB 4 CYS B  71  ARG B  73 -1  O  CYS B  71   N  ILE B  60           
SHEET    3  BB 4 TYR B 107  ASN B 113 -1  O  VAL B 109   N  HIS B  72           
SHEET    4  BB 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  1.93  
SSBOND   3 CYS A   55    CYS A  111                          1555   1555  2.06  
SSBOND   4 CYS A   62    CYS A   71                          1555   1555  2.03  
SSBOND   5 CYS B   23    CYS B   83                          1555   1555  2.02  
SSBOND   6 CYS B   37    CYS B   96                          1555   1555  2.03  
SSBOND   7 CYS B   55    CYS B  111                          1555   1555  2.02  
SSBOND   8 CYS B   62    CYS B   71                          1555   1555  2.05  
SITE     1 AC1 14 THR A  46  ASN A  50  SER A  74  ARG A  75                    
SITE     2 AC1 14 PHE A  76  VAL A  78  TYR A 107  HOH A2119                    
SITE     3 AC1 14 HOH A2121  HOH A2126  HOH A2129  HOH A2222                    
SITE     4 AC1 14 HOH A2223  ARG B 121                                          
SITE     1 AC2  5 ARG A  34  LYS A  38  ASN A  39  HOH A2092                    
SITE     2 AC2  5 HOH A2224                                                     
SITE     1 AC3 14 ARG A  61  ARG A  66  HOH A2149  THR B  46                    
SITE     2 AC3 14 ASN B  50  VAL B  54  ASN B  57  SER B  74                    
SITE     3 AC3 14 ARG B  75  PHE B  76  VAL B  78  TYR B 107                    
SITE     4 AC3 14 HOH B2047  HOH B2048                                          
SITE     1 AC4  6 ARG B  34  CYS B  37  LYS B  38  ASN B  39                    
SITE     2 AC4  6 HOH B2078  HOH B2079                                          
SITE     1 AC5 10 ARG A  45  HOH A2057  HOH A2058  HOH A2059                    
SITE     2 AC5 10 ARG B 114  PRO B 116  HOH B2064  HOH B2065                    
SITE     3 AC5 10 HOH B2066  HOH B2082                                          
SITE     1 AC6 11 ARG A  97  HOH A2065  HOH A2066  HOH A2188                    
SITE     2 AC6 11 HOH A2189  HOH A2226  HOH A2227  HOH A2228                    
SITE     3 AC6 11 ARG B  77  HOH B2050  HOH B2051                               
CRYST1   62.511   62.511  174.857  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      0.015997  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015997  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005719        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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