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Database: PDB
Entry: 1WEJ
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Original site: 1WEJ 
HEADER    COMPLEX (ANTIBODY/ELECTRON TRANSPORT)   26-MAR-98   1WEJ              
TITLE     IGG1 FAB FRAGMENT (OF E8 ANTIBODY) COMPLEXED WITH HORSE               
TITLE    2 CYTOCHROME C AT 1.8 A RESOLUTION                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: E8 ANTIBODY;                                               
COMPND   3 CHAIN: L;                                                            
COMPND   4 FRAGMENT: FAB;                                                       
COMPND   5 SYNONYM: FAB E8;                                                     
COMPND   6 OTHER_DETAILS: IGG1 KAPPA MOUSE MONOCLONAL ANTIBODY;                 
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: E8 ANTIBODY;                                               
COMPND   9 CHAIN: H;                                                            
COMPND  10 FRAGMENT: FAB;                                                       
COMPND  11 SYNONYM: FAB E8;                                                     
COMPND  12 OTHER_DETAILS: IGG1 KAPPA MOUSE MONOCLONAL ANTIBODY;                 
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: CYTOCHROME C;                                              
COMPND  15 CHAIN: F;                                                            
COMPND  16 SYNONYM: CYT C, ANTIGEN;                                             
COMPND  17 OTHER_DETAILS: ELECTRON TRANSPORT PROTEIN WITH HEME                  
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 STRAIN: BALB/C;                                                      
SOURCE   6 CELL_LINE: P3-X63-AG8.653;                                           
SOURCE   7 ORGAN: SPLEEN;                                                       
SOURCE   8 OTHER_DETAILS: E8 ANTIBODY PURIFIED FROM ASCITES;                    
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  11 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  12 ORGANISM_TAXID: 10090;                                               
SOURCE  13 STRAIN: BALB-C;                                                      
SOURCE  14 CELL_LINE: P3-X63-AG8.653;                                           
SOURCE  15 ORGAN: SPLEEN;                                                       
SOURCE  16 OTHER_DETAILS: E8 ANTIBODY PURIFIED FROM ASCITES;                    
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;                                 
SOURCE  19 ORGANISM_COMMON: HORSE;                                              
SOURCE  20 ORGANISM_TAXID: 9796;                                                
SOURCE  21 ORGAN: HEART;                                                        
SOURCE  22 OTHER_DETAILS: OBTAINED FROM SIGMA                                   
KEYWDS    IMMUNOGLOBULIN, IGG1 KAPPA, FAB FRAGMENT, HORSE CYTOCHROME            
KEYWDS   2 C, COMPLEX (ANTIBODY/ELECTRON TRANSPORT)                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.E.MYLVAGANAM,Y.PATERSON,E.D.GETZOFF                                 
REVDAT   2   24-FEB-09 1WEJ    1       VERSN                                    
REVDAT   1   09-DEC-98 1WEJ    0                                                
JRNL        AUTH   S.E.MYLVAGANAM,Y.PATERSON,E.D.GETZOFF                        
JRNL        TITL   STRUCTURAL BASIS FOR THE BINDING OF AN                       
JRNL        TITL 2 ANTI-CYTOCHROME C ANTIBODY TO ITS ANTIGEN: CRYSTAL           
JRNL        TITL 3 STRUCTURES OF FABE8-CYTOCHROME C COMPLEX TO 1.8 A            
JRNL        TITL 4 RESOLUTION AND FABE8 TO 2.26 A RESOLUTION.                   
JRNL        REF    J.MOL.BIOL.                   V. 281   301 1998              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   9698550                                                      
JRNL        DOI    10.1006/JMBI.1998.1942                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.E.MYLVAGANAM,Y.PATERSON,K.KAISER,K.BOWDISH,                
REMARK   1  AUTH 2 E.D.GETZOFF                                                  
REMARK   1  TITL   BIOCHEMICAL IMPLICATIONS FROM THE VARIABLE GENE              
REMARK   1  TITL 2 SEQUENCES OF AN ANTI-CYTOCHROME C ANTIBODY AND               
REMARK   1  TITL 3 CRYSTALLOGRAPHIC CHARACTERIZATION OF ITS                     
REMARK   1  TITL 4 ANTIGEN-BINDING FRAGMENT IN FREE AND                         
REMARK   1  TITL 5 ANTIGEN-COMPLEXED FORMS                                      
REMARK   1  REF    J.MOL.BIOL.                   V. 221   455 1991              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   F.R.CARBONE,Y.PATERSON                                       
REMARK   1  TITL   MONOCLONAL ANTIBODIES TO HORSE CYTOCHROME C                  
REMARK   1  TITL 2 EXPRESSING FOUR DISTINCT IDIOTYPES DISTRIBUTE                
REMARK   1  TITL 3 AMONG TWO SITES ON THE NATIVE PROTEIN                        
REMARK   1  REF    J.IMMUNOL.                    V. 135  2609 1985              
REMARK   1  REFN                   ISSN 0022-1767                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.8                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 47993                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.88                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5745                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3160                       
REMARK   3   BIN FREE R VALUE                    : 8.0000                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4166                                    
REMARK   3   NUCLEIC ACID ATOMS       : NULL                                    
REMARK   3   HETEROGEN ATOMS          : 43                                      
REMARK   3   SOLVENT ATOMS            : 637                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.06                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.96                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.94200                                             
REMARK   3    B22 (A**2) : -2.04200                                             
REMARK   3    B33 (A**2) : 2.07000                                              
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.33                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 20.00                           
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.30                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.47                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 27.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.54                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARAM19X.HEME                                  
REMARK   3  PARAMETER FILE  2  : PARHCSDXB.PRO                                  
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPH19X.HEM                                    
REMARK   3  TOPOLOGY FILE  2   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1WEJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : JAN-95                             
REMARK 200  TEMPERATURE           (KELVIN) : 90                                 
REMARK 200  PH                             : 6.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48348                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 36.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.28200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 12.000                             
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.8                                            
REMARK 200 STARTING MODEL: 2.26 A RESOLUTION FABE8 X-RAY STRUCTURE (FREE        
REMARK 200  FAB E8) (MYLVAGANAM ET AL., 1998, JMB, 281, 301-32; PDB ENTRY       
REMARK 200  1QBL) AND HORSE CYTOCHROME C 1.9 A X-RAY STRUCTURE (BUSHNELL        
REMARK 200  ET. AL., 1990; PDB ENTRY 1HRC).                                     
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM ZINC ACETATE BUFFER, PH 6.4,        
REMARK 280  25% (W/V) PEG 4000.                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       39.79000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       47.19000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.27000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       47.19000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.79000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.27000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, F                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6040 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F                                     
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      -94.38000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H                                  
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 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 H 223   CA  -  CB  -  SG  ANGL. DEV. =   6.6 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    ALA L  51      -39.27     68.18                                   
REMARK 500    SER H  76       -0.02   -144.14                                   
REMARK 500    ALA H  92     -178.23   -177.80                                   
REMARK 500    ASP H 100     -124.93   -133.29                                   
REMARK 500    LYS H 136       58.30   -109.21                                   
REMARK 500    PRO H 151     -164.82   -102.67                                   
REMARK 500    CYS H 219       29.09     80.06                                   
REMARK 500    ASP H 222      148.55    153.64                                   
REMARK 500    LYS F  27     -129.04   -113.20                                   
REMARK 500    ASN F  70       85.73   -162.19                                   
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 F 666        DISTANCE =  5.11 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     HEM F  105                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN L 215  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP L 151   OD2                                                    
REMARK 620 2 HIS L 189   ND1 118.3                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 215                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM F 105                 
DBREF  1WEJ L    1   214  GB     2072141  AAB53778        15    228             
DBREF  1WEJ H    2   217  PIR    S49220   S49220           2    219             
DBREF  1WEJ F    1   104  UNP    P00004   CYC_HORSE        1    104             
SEQADV 1WEJ SER L   85  GB   2072141   THR    99 CONFLICT                       
SEQADV 1WEJ GLN L   89  GB   2072141   HIS   103 CONFLICT                       
SEQADV 1WEJ ILE L  106  GB   2072141   VAL   120 CONFLICT                       
SEQADV 1WEJ PHE L  118  GB   2072141   LEU   132 CONFLICT                       
SEQADV 1WEJ GLN H    3  PIR  S49220    LYS     3 CONFLICT                       
SEQADV 1WEJ GLN H    5  PIR  S49220    LEU     5 CONFLICT                       
SEQADV 1WEJ GLN H    6  PIR  S49220    GLU     6 CONFLICT                       
SEQADV 1WEJ PRO H   14  PIR  S49220    SER    14 CONFLICT                       
SEQADV 1WEJ LYS H   43  PIR  S49220    GLN    43 CONFLICT                       
SEQADV 1WEJ SER H   55  PIR  S49220    ASN    55 CONFLICT                       
SEQADV 1WEJ ASN H   57  PIR  S49220    GLU    57 CONFLICT                       
SEQADV 1WEJ THR H   58  PIR  S49220    ILE    58 CONFLICT                       
SEQADV 1WEJ ASP H   66  PIR  S49220    GLY    66 CONFLICT                       
SEQADV 1WEJ LYS H   67  PIR  S49220    THR    67 CONFLICT                       
SEQADV 1WEJ SER H   76  PIR  S49220    THR    76 CONFLICT                       
SEQADV 1WEJ     H       PIR  S49220    VAL    97 DELETION                       
SEQADV 1WEJ     H       PIR  S49220    ARG    98 DELETION                       
SEQADV 1WEJ ALA H   97  PIR  S49220    ARG    99 CONFLICT                       
SEQADV 1WEJ ASP H  100  PIR  S49220    GLY   102 CONFLICT                       
SEQADV 1WEJ TYR H  101  PIR  S49220    SER   103 CONFLICT                       
SEQADV 1WEJ GLY H  102  PIR  S49220    SER   104 CONFLICT                       
SEQADV 1WEJ ASN H  103  PIR  S49220    GLN   105 CONFLICT                       
SEQADV 1WEJ PHE H  104  PIR  S49220    GLU   106 CONFLICT                       
SEQADV 1WEJ ASP H  105  PIR  S49220    PRO   107 CONFLICT                       
SEQADV 1WEJ GLU H  119  PIR  S49220    LYS   121 CONFLICT                       
SEQADV 1WEJ THR H  132  PIR  S49220    SER   134 CONFLICT                       
SEQADV 1WEJ LEU H  135  PIR  S49220    GLN   137 CONFLICT                       
SEQADV 1WEJ LYS H  136  PIR  S49220    THR   138 CONFLICT                       
SEQADV 1WEJ SER H  137  PIR  S49220    ASN   139 CONFLICT                       
SEQADV 1WEJ THR H  182  PIR  S49220    SER   184 CONFLICT                       
SEQADV 1WEJ GLN H  195  PIR  S49220    GLU   197 CONFLICT                       
SEQRES   1 L  214  ASP ILE GLN MET THR GLN SER PRO ALA SER LEU SER ALA          
SEQRES   2 L  214  SER VAL GLY GLU THR VAL THR ILE THR CYS ARG ALA SER          
SEQRES   3 L  214  GLY ASN ILE HIS ASN TYR LEU ALA TRP TYR GLN GLN LYS          
SEQRES   4 L  214  GLN GLY LYS SER PRO GLN LEU LEU VAL TYR ASN ALA LYS          
SEQRES   5 L  214  THR LEU ALA ASP GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 L  214  GLY SER GLY THR GLN TYR SER LEU LYS ILE ASN SER LEU          
SEQRES   7 L  214  GLN PRO GLU ASP PHE GLY SER TYR TYR CYS GLN HIS PHE          
SEQRES   8 L  214  TRP SER THR PRO TRP THR PHE GLY GLY GLY THR LYS LEU          
SEQRES   9 L  214  GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE          
SEQRES  10 L  214  PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA          
SEQRES  11 L  214  SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP          
SEQRES  12 L  214  ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN          
SEQRES  13 L  214  ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS          
SEQRES  14 L  214  ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR          
SEQRES  15 L  214  LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU          
SEQRES  16 L  214  ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER          
SEQRES  17 L  214  PHE ASN ARG ASN GLU CYS                                      
SEQRES   1 H  223  GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS          
SEQRES   2 H  223  PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY          
SEQRES   3 H  223  PHE ASN ILE LYS ASP THR TYR MET HIS TRP VAL LYS GLN          
SEQRES   4 H  223  ARG PRO GLU LYS GLY LEU GLU TRP ILE GLY ARG ILE ASP          
SEQRES   5 H  223  PRO ALA SER GLY ASN THR LYS TYR ASP PRO LYS PHE GLN          
SEQRES   6 H  223  ASP LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR          
SEQRES   7 H  223  ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR          
SEQRES   8 H  223  ALA VAL TYR TYR CYS ALA GLY TYR ASP TYR GLY ASN PHE          
SEQRES   9 H  223  ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SER          
SEQRES  10 H  223  ALA GLU THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO          
SEQRES  11 H  223  GLY THR ALA ALA LEU LYS SER SER MET VAL THR LEU GLY          
SEQRES  12 H  223  CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL          
SEQRES  13 H  223  THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS THR          
SEQRES  14 H  223  PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU THR          
SEQRES  15 H  223  SER SER VAL THR VAL PRO SER SER THR TRP PRO SER GLN          
SEQRES  16 H  223  THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER THR          
SEQRES  17 H  223  LYS VAL ASP LYS LYS ILE VAL PRO ARG ASN CYS GLY GLY          
SEQRES  18 H  223  ASP CYS                                                      
SEQRES   1 F  105  ACE GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN          
SEQRES   2 F  105  LYS CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS          
SEQRES   3 F  105  HIS LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG          
SEQRES   4 F  105  LYS THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA          
SEQRES   5 F  105  ASN LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU          
SEQRES   6 F  105  MET GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY          
SEQRES   7 F  105  THR LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU          
SEQRES   8 F  105  ARG GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN          
SEQRES   9 F  105  GLU                                                          
HET    ACE  F   0       3                                                       
HET     ZN  L 215       1                                                       
HET    HEM  F 105      42                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM      ZN ZINC ION                                                         
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETSYN     HEM HEME                                                             
FORMUL   3  ACE    C2 H4 O                                                      
FORMUL   4   ZN    ZN 2+                                                        
FORMUL   5  HEM    C34 H32 FE N4 O4                                             
FORMUL   6  HOH   *637(H2 O)                                                    
HELIX    1   1 PRO L   80  ASP L   82  5                                   3    
HELIX    2   2 SER L  122  SER L  127  1                                   6    
HELIX    3   3 LYS L  183  ARG L  188  1                                   6    
HELIX    4   4 ILE H   29  ASP H   31  5                                   3    
HELIX    5   5 PRO H   62  PHE H   64  5                                   3    
HELIX    6   6 SER H   88  ASP H   90  5                                   3    
HELIX    7   7 THR H  132  LEU H  135  5                                   4    
HELIX    8   8 ASN H  159  GLY H  161  5                                   3    
HELIX    9   9 PRO H  204  SER H  206  5                                   3    
HELIX   10  10 VAL F    3  LYS F   13  1                                  11    
HELIX   11  11 ASP F   50  ASN F   54  1                                   5    
HELIX   12  12 GLU F   61  GLU F   69  1                                   9    
HELIX   13  13 PRO F   71  TYR F   74  1                                   4    
HELIX   14  14 LYS F   88  ALA F  101  1                                  14    
SHEET    1   A 4 MET L   4  SER L   7  0                                        
SHEET    2   A 4 VAL L  19  ALA L  25 -1  N  ARG L  24   O  THR L   5           
SHEET    3   A 4 GLN L  70  ILE L  75 -1  N  ILE L  75   O  VAL L  19           
SHEET    4   A 4 PHE L  62  SER L  67 -1  N  SER L  67   O  GLN L  70           
SHEET    1   B 5 SER L  10  ALA L  13  0                                        
SHEET    2   B 5 THR L 102  ILE L 106  1  N  LYS L 103   O  LEU L  11           
SHEET    3   B 5 GLY L  84  HIS L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4   B 5 LEU L  33  GLN L  38 -1  N  GLN L  38   O  SER L  85           
SHEET    5   B 5 GLN L  45  VAL L  48 -1  N  VAL L  48   O  TRP L  35           
SHEET    1   C 4 THR L 114  PHE L 118  0                                        
SHEET    2   C 4 GLY L 129  ASN L 137 -1  N  ASN L 137   O  THR L 114           
SHEET    3   C 4 MET L 175  THR L 182 -1  N  LEU L 181   O  ALA L 130           
SHEET    4   C 4 VAL L 159  TRP L 163 -1  N  SER L 162   O  SER L 176           
SHEET    1   D 4 SER L 153  ARG L 155  0                                        
SHEET    2   D 4 ASN L 145  ILE L 150 -1  N  ILE L 150   O  SER L 153           
SHEET    3   D 4 SER L 191  THR L 197 -1  N  THR L 197   O  ASN L 145           
SHEET    4   D 4 ILE L 205  ASN L 210 -1  N  PHE L 209   O  TYR L 192           
SHEET    1   E 4 GLN H   3  GLN H   6  0                                        
SHEET    2   E 4 VAL H  18  SER H  25 -1  N  SER H  25   O  GLN H   3           
SHEET    3   E 4 THR H  78  LEU H  83 -1  N  LEU H  83   O  VAL H  18           
SHEET    4   E 4 ALA H  68  ASP H  73 -1  N  ASP H  73   O  THR H  78           
SHEET    1   F 6 GLU H  10  VAL H  12  0                                        
SHEET    2   F 6 THR H 111  VAL H 115  1  N  THR H 114   O  GLU H  10           
SHEET    3   F 6 ALA H  92  GLY H  98 -1  N  TYR H  94   O  THR H 111           
SHEET    4   F 6 TYR H  33  GLN H  39 -1  N  GLN H  39   O  VAL H  93           
SHEET    5   F 6 LEU H  45  ASP H  52 -1  N  ILE H  51   O  MET H  34           
SHEET    6   F 6 ASN H  57  TYR H  60 -1  N  LYS H  59   O  ARG H  50           
SHEET    1   G 2 ALA H  97  TYR H  99  0                                        
SHEET    2   G 2 ASP H 105  TRP H 107 -1  N  TYR H 106   O  GLY H  98           
SHEET    1   H 4 SER H 124  LEU H 128  0                                        
SHEET    2   H 4 MET H 139  TYR H 149 -1  N  LYS H 147   O  SER H 124           
SHEET    3   H 4 TYR H 179  PRO H 188 -1  N  VAL H 187   O  VAL H 140           
SHEET    4   H 4 VAL H 167  THR H 169 -1  N  HIS H 168   O  SER H 184           
SHEET    1   I 3 THR H 155  TRP H 158  0                                        
SHEET    2   I 3 THR H 198  HIS H 203 -1  N  ALA H 202   O  THR H 155           
SHEET    3   I 3 THR H 208  LYS H 213 -1  N  LYS H 212   O  CYS H 199           
SHEET    1   J 2 VAL H 173  GLN H 175  0                                        
SHEET    2   J 2 LEU H 178  THR H 180 -1  N  THR H 180   O  VAL H 173           
SSBOND   1 CYS L   23    CYS L   88                          1555   1555  2.03  
SSBOND   2 CYS L  134    CYS L  194                          1555   1555  2.02  
SSBOND   3 CYS L  214    CYS H  219                          1555   1555  2.03  
SSBOND   4 CYS H   22    CYS H   96                          1555   1555  2.02  
SSBOND   5 CYS H  144    CYS H  199                          1555   1555  2.03  
LINK         C   ACE F   0                 N   GLY F   1     1555   1555  1.33  
LINK         CAB HEM F 105                 SG  CYS F  14     1555   1555  1.79  
LINK         CAC HEM F 105                 SG  CYS F  17     1555   1555  1.78  
LINK        ZN    ZN L 215                 OD2 ASP L 151     1555   1555  1.76  
LINK        ZN    ZN L 215                 ND1 HIS L 189     1555   1555  2.45  
CISPEP   1 SER L    7    PRO L    8          0        -0.33                     
CISPEP   2 THR L   94    PRO L   95          0        -0.01                     
CISPEP   3 TYR L  140    PRO L  141          0        -0.06                     
CISPEP   4 PHE H  150    PRO H  151          0        -0.17                     
CISPEP   5 GLU H  152    PRO H  153          0        -0.08                     
CISPEP   6 TRP H  192    PRO H  193          0         0.23                     
SITE     1 AC1  3 ASP L 151  HIS L 189  HOH L 368                               
SITE     1 AC2 21 LYS F  13  CYS F  14  GLN F  16  CYS F  17                    
SITE     2 AC2 21 HIS F  18  THR F  28  GLY F  29  PRO F  30                    
SITE     3 AC2 21 THR F  40  GLY F  41  TYR F  48  THR F  49                    
SITE     4 AC2 21 ASN F  52  TRP F  59  TYR F  67  LEU F  68                    
SITE     5 AC2 21 THR F  78  LYS F  79  MET F  80  PHE F  82                    
SITE     6 AC2 21 HOH F 208                                                     
CRYST1   79.580   72.540   94.380  90.00  90.00  90.00 P 21 21 21    4          
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      0.012566  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013785  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010595        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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