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Database: PDB
Entry: 4A2O
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HEADER    HYDROLASE                               28-SEP-11   4A2O              
TITLE     STRUCTURE OF THE HUMAN EOSINOPHIL CATIONIC PROTEIN IN                 
TITLE    2 COMPLEX WITH SULFATE 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   1   27-JUN-12 4A2O    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.    1.69 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0110                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.69                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 51.62                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.54                          
REMARK   3   NUMBER OF REFLECTIONS             : 25341                          
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) : 0.16533                         
REMARK   3   R VALUE            (WORKING SET) : 0.16220                         
REMARK   3   FREE R VALUE                     : 0.22251                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1343                            
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) : 1.692                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.736                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1644                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.64                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.289                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 81                           
REMARK   3   BIN FREE R VALUE                    : 0.365                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2211                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 75                                      
REMARK   3   SOLVENT ATOMS            : 371                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.6                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.866                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.78                                                 
REMARK   3    B22 (A**2) : -0.62                                                
REMARK   3    B33 (A**2) : 0.05                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.28                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.120         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.125         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.081         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.420         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2342 ; 0.024 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3219 ; 1.941 ; 1.952       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   276 ; 6.479 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   125 ;32.089 ;21.280       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   351 ;13.069 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    37 ;19.415 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   335 ; 0.142 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1835 ; 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):  1368 ; 1.277 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2254 ; 2.110 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   974 ; 3.443 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   959 ; 5.150 ; 4.500       
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          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   3   RESIDUES 1-27 OF P12724 ARE THE SIGNAL PEPTIDE. LOOP 90-92         
REMARK   3    IS PARTIALLY DISORDERED SIDE CHAINS OF R28, W35, R73, F76,        
REMARK   3     R101, AND R105 ARE PARTIALLY DISORDERED.                         
REMARK   4                                                                      
REMARK   4 4A2O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-SEP-11.                  
REMARK 100 THE PDBE ID CODE IS EBI-49813.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JUL-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (MX-225)                       
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   : 25341                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.69                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 51.62                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 3                                  
REMARK 200  R MERGE                    (I) : 0.07                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.40                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.78                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.3                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.45                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.30                               
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   (%): 24.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       46.13200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       25.64500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       46.13200            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       25.64500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8730 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -351.5 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 S    SO4 A1137  LIES ON A SPECIAL POSITION.                          
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  73    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A  92    CG   OD1  ND2                                       
REMARK 470     GLN B  91    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 101    CD   NE   CZ   NH1  NH2                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLN B    91     O    HOH B  2126              2.10            
REMARK 500   O    HOH A  2006     O    HOH A  2008              2.18            
REMARK 500   O    HOH A  2015     O    HOH B  2018              2.13            
REMARK 500   O    HOH A  2062     O    HOH A  2147              2.08            
REMARK 500   O    HOH B  2026     O    HOH B  2027              1.91            
REMARK 500   O    HOH B  2083     O    HOH B  2147              2.17            
REMARK 500   O    HOH B  2084     O    HOH A  2179              2.12            
REMARK 500   O    HOH B  2144     O    HOH B  2169              2.00            
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 A     4     O    HOH A  2189     4556     2.16            
REMARK 500   O    HOH A  2001     O    HOH A  2159     4556     2.16            
REMARK 500   O    HOH A  2067     O    HOH A  2192     4546     2.19            
REMARK 500   O    HOH A  2101     O    HOH B  2174     3445     2.17            
REMARK 500   O    HOH B  2032     O    HOH A  2116     4556     2.09            
REMARK 500   O    HOH B  2094     O    HOH B  2115     2555     1.94            
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 111   CB    CYS A 111   SG      0.122                       
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. =  -7.0 DEGREES          
REMARK 500    ARG A  61   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A  61   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG A  77   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A  77   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    CYS A  96   CA  -  CB  -  SG  ANGL. DEV. =  -6.9 DEGREES          
REMARK 500    ARG A 114   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG B  77   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG B  97   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG B  97   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.8 DEGREES          
REMARK 500    ARG B 121   CD  -  NE  -  CZ  ANGL. DEV. =  11.2 DEGREES          
REMARK 500    ARG B 121   CG  -  CD  -  NE  ANGL. DEV. = -16.9 DEGREES          
REMARK 500    ARG B 121   NE  -  CZ  -  NH1 ANGL. DEV. =   8.5 DEGREES          
REMARK 500    ARG B 121   NE  -  CZ  -  NH2 ANGL. DEV. = -11.7 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 A  19       71.16   -152.33                                   
REMARK 500    ALA A  90      118.32    -36.58                                   
REMARK 500    PRO A 120       -7.97    -59.92                                   
REMARK 500    ASN B  19       73.59   -153.32                                   
REMARK 500    ASN B  70       40.78   -108.09                                   
REMARK 500    GLN B  91      -83.05    -52.23                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1134                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1135                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1136                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1137                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1138                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1134                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1135                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1136                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1137                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1138                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1139                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1140                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1142                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1H1H   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF EOSINOPHIL CATIONIC PROTEIN IN                 
REMARK 900  COMPLEX WITH 2',5'-ADP AT 2.0 A RESOLUTION REVEALS                  
REMARK 900   THE DETAILS OF THE RIBONUCLEOLYTIC ACTIVE SITE                     
REMARK 900 RELATED ID: 1QMT   RELATED DB: PDB                                   
REMARK 900  RECOMBINANT HUMAN EOSINOPHIL CATIONIC PROTEIN                       
REMARK 900 RELATED ID: 4A2Y   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE HUMAN EOSINOPHIL CATIONIC PROTEIN IN               
REMARK 900  COMPLEX WITH CITRATE ANIONS                                         
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  4A2O A    1   133  UNP    P12724   ECP_HUMAN       28    160             
DBREF  4A2O B    1   133  UNP    P12724   ECP_HUMAN       28    160             
SEQADV 4A2O ARG A   97  UNP  P12724    THR   124 VARIANT                        
SEQADV 4A2O 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    SO4  A1134       5                                                       
HET    SO4  A1135       5                                                       
HET    SO4  A1136       5                                                       
HET    SO4  A1137       5                                                       
HET    SO4  A1138       5                                                       
HET    SO4  B1134       5                                                       
HET    SO4  B1135       5                                                       
HET    SO4  B1136       5                                                       
HET    SO4  B1137       5                                                       
HET    SO4  B1138       5                                                       
HET    SO4  B1139       5                                                       
HET    SO4  B1140       5                                                       
HET    SO4  B1141       5                                                       
HET    SO4  B1142      10                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    14(O4 S 2-)                                                  
FORMUL   4  HOH   *371(H2 O)                                                    
HELIX    1   1 THR A    6  ILE A   16  1                                  11    
HELIX    2   2 ARG A   22  MET A   27  1                                   6    
HELIX    3   3 MET A   27  ASN A   32  1                                   6    
HELIX    4   4 THR A   47  CYS A   55  1                                   9    
HELIX    5   5 ASN A   92  CYS A   96  5                                   5    
HELIX    6   6 THR B    6  ILE B   16  1                                  11    
HELIX    7   7 ARG B   22  ASN B   32  1                                  11    
HELIX    8   8 THR B   47  GLY B   56  1                                  10    
HELIX    9   9 ASN B   92  CYS B   96  5                                   5    
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 4 SER A  59  ILE A  60  0                                        
SHEET    2  AB 4 CYS A  71  ARG A  73 -1  O  CYS A  71   N  ILE A  60           
SHEET    3  AB 4 TYR A 107  ASN A 113 -1  O  VAL A 109   N  HIS A  72           
SHEET    4  AB 4 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  2.06  
SSBOND   2 CYS A   37    CYS A   96                          1555   1555  2.01  
SSBOND   3 CYS A   55    CYS A  111                          1555   1555  2.10  
SSBOND   4 CYS A   62    CYS A   71                          1555   1555  2.06  
SSBOND   5 CYS B   23    CYS B   83                          1555   1555  2.07  
SSBOND   6 CYS B   37    CYS B   96                          1555   1555  1.97  
SSBOND   7 CYS B   55    CYS B  111                          1555   1555  2.08  
SSBOND   8 CYS B   62    CYS B   71                          1555   1555  2.08  
SITE     1 AC1  7 ARG A  34  ARG A  36  LYS A  38  ASN A  39                    
SITE     2 AC1  7 HOH A2074  HOH A2075  ARG B 104                               
SITE     1 AC2  3 ARG A   1  ARG A   7  HOH A2191                               
SITE     1 AC3  4 ARG A  77  ARG A 104  ARG B  36  HOH B2060                    
SITE     1 AC4  6 ARG A 121  HOH A2193  HOH A2194  HOH A2195                    
SITE     2 AC4  6 VAL B  52  PRO B 123                                          
SITE     1 AC5  9 ARG A  28  ASN A  32  ARG A  61  ARG A  66                    
SITE     2 AC5  9 HOH A2055  HOH A2112  HOH A2196  HOH A2197                    
SITE     3 AC5  9 ARG B  22                                                     
SITE     1 AC6  7 ARG A 104  ARG B  34  LYS B  38  ASN B  39                    
SITE     2 AC6  7 HOH B2061  HOH B2068  HOH B2072                               
SITE     1 AC7  8 GLN B  14  LYS B  38  HIS B 128  HOH B2016                    
SITE     2 AC7  8 HOH B2024  HOH B2058  HOH B2166  HOH B2167                    
SITE     1 AC8  3 ARG B   1  ARG B   7  HOH B2170                               
SITE     1 AC9  4 ARG A  36  HOH A2068  ARG B  77  ARG B 104                    
SITE     1 BC1  5 ASN B  57  GLN B  58  ARG B  73  ARG B  75                    
SITE     2 BC1  5 HOH B2091                                                     
SITE     1 BC2  8 ARG A  75  HOH A2096  HOH A2099  ASN B  87                    
SITE     2 BC2  8 PRO B  88  GLY B  89  HOH B2119  HOH B2172                    
SITE     1 BC3  6 GLN A  58  SER A  59  HOH A2110  ARG B  97                    
SITE     2 BC3  6 HOH B2045  HOH B2134                                          
SITE     1 BC4  7 HOH A2044  ARG B  28  ASN B  32  ARG B  61                    
SITE     2 BC4  7 ARG B  66  HOH B2132  HOH B2173                               
SITE     1 BC5  9 ASN A  57  GLN A  58  ARG A  75  HOH A2101                    
SITE     2 BC5  9 ASN B  87  ALA B  90  ARG B  97  HOH B2133                    
SITE     3 BC5  9 HOH B2174                                                     
CRYST1   92.264   51.290   55.394  90.00 111.28  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010838  0.000000  0.004221        0.00000                         
SCALE2      0.000000  0.019497  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019373        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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