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Entry: 3NBT
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HEADER    ELECTRON TRANSPORT                      04-JUN-10   3NBT              
TITLE     CRYSTAL STRUCTURE OF TRIMERIC CYTOCHROME C FROM HORSE HEART           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME C;                                              
COMPND   3 CHAIN: A, B, C, D, E, F                                              
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;                                 
SOURCE   3 ORGANISM_COMMON: DOMESTIC HORSE,EQUINE;                              
SOURCE   4 ORGANISM_TAXID: 9796;                                                
SOURCE   5 ORGAN: HEART                                                         
KEYWDS    CYTOCHROME C, POLYMERIZATION, DOMAIN SWAPPING, ELECTRON TRANSPORT     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.TAKETA,H.KOMORI,S.HIROTA,Y.HIGUCHI                                  
REVDAT   5   02-OCT-19 3NBT    1       COMPND REMARK HET    HETNAM              
REVDAT   5 2                   1       HETSYN FORMUL LINK   SITE                
REVDAT   5 3                   1       ATOM                                     
REVDAT   4   08-NOV-17 3NBT    1       REMARK                                   
REVDAT   3   28-JUL-10 3NBT    1       JRNL                                     
REVDAT   2   21-JUL-10 3NBT    1       JRNL                                     
REVDAT   1   14-JUL-10 3NBT    0                                                
JRNL        AUTH   S.HIROTA,Y.HATTORI,S.NAGAO,M.TAKETA,H.KOMORI,H.KAMIKUBO,     
JRNL        AUTH 2 Z.WANG,I.TAKAHASHI,S.NEGI,Y.SUGIURA,M.KATAOKA,Y.HIGUCHI      
JRNL        TITL   CYTOCHROME C POLYMERIZATION BY SUCCESSIVE DOMAIN SWAPPING AT 
JRNL        TITL 2 THE C-TERMINAL HELIX                                         
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 107 12854 2010              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   20615990                                                     
JRNL        DOI    10.1073/PNAS.1001839107                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.54                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 77168.570                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 40288                          
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 SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 4052                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.23                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.20                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5766                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2470                       
REMARK   3   BIN FREE R VALUE                    : 0.3050                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.10                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 646                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.012                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4938                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 384                                     
REMARK   3   SOLVENT ATOMS            : 345                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.98000                                             
REMARK   3    B22 (A**2) : -4.59000                                             
REMARK   3    B33 (A**2) : 6.57000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.26                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.16                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.33                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.26                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.200                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.770                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.320 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.980 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.020 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.900 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 48.75                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : PARAM19X_MOD.H                                 
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : PEG.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : TOPH19.HEM                                     
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : PEG.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 3NBT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JUN-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000059632.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-JUL-09                          
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               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL26B2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8                                
REMARK 200  MONOCHROMATOR                  : SI DOUBLE CRYSTAL                  
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-225                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43002                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
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     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.09600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.590                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1CRC                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 200, 0.1M TRIS-HCL, 0.2M         
REMARK 280  AMMONIUM PHOSPHATE, PH 8.5, VAPOR DIFFUSION, SITTING DROP,          
REMARK 280  TEMPERATURE 277K                                                    
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       28.60200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.46750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.83050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.46750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.60200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.83050            
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: 7750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, 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 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, D                               
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 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   SG   CYS F    17     CBC  HEC F   105              2.18            
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    LYS A  27     -134.88   -130.91                                   
REMARK 500    ASN A  70       89.78   -162.46                                   
REMARK 500    PHE A  82      125.55    -36.24                                   
REMARK 500    LYS B  27     -138.00   -131.96                                   
REMARK 500    ASN B  70       87.80   -161.33                                   
REMARK 500    LYS C  27     -139.29   -129.23                                   
REMARK 500    ASN C  70       88.11   -160.00                                   
REMARK 500    LYS D  27     -129.83   -127.83                                   
REMARK 500    ASN D  70       88.25   -166.84                                   
REMARK 500    LYS E  27     -132.12   -124.38                                   
REMARK 500    ASN E  70       87.67   -163.05                                   
REMARK 500    PHE E  82      123.12    -36.72                                   
REMARK 500    LYS F  27     -134.97   -131.82                                   
REMARK 500    ASN F  70       92.01   -164.43                                   
REMARK 500    PHE F  82      119.66    -38.65                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                             HEC E 105  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  18   NE2                                                    
REMARK 620 2 HEC E 105   NA   95.2                                              
REMARK 620 3 HEC E 105   NB   94.5  91.8                                        
REMARK 620 4 HEC E 105   NC   87.4 177.1  89.4                                  
REMARK 620 5 HEC E 105   ND   85.1  89.4 178.8  89.5                            
REMARK 620 6 HOH E 205   O   175.1  88.3  88.8  89.0  91.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC A 105  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  18   NE2                                                    
REMARK 620 2 HEC A 105   NA   89.9                                              
REMARK 620 3 HEC A 105   NB   95.7  91.7                                        
REMARK 620 4 HEC A 105   NC   93.0 175.5  91.3                                  
REMARK 620 5 HEC A 105   ND   84.7  87.8 179.4  89.1                            
REMARK 620 6 HOH A 201   O   171.2  87.6  92.8  89.0  86.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC F 105  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  18   NE2                                                    
REMARK 620 2 HEC F 105   NA   93.7                                              
REMARK 620 3 HEC F 105   NB   88.8  90.1                                        
REMARK 620 4 HEC F 105   NC   88.4 177.9  89.7                                  
REMARK 620 5 HEC F 105   ND   86.9  88.2 175.2  92.2                            
REMARK 620 6 HOH F 206   O   169.1  95.8  96.5  82.1  88.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC C 105  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  18   NE2                                                    
REMARK 620 2 HEC C 105   NA   95.0                                              
REMARK 620 3 HEC C 105   NB   89.1  91.4                                        
REMARK 620 4 HEC C 105   NC   87.3 177.7  88.3                                  
REMARK 620 5 HEC C 105   ND   87.8  89.2 176.9  91.2                            
REMARK 620 6 HOH C 203   O   176.0  88.8  89.7  88.9  93.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC D 105  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  18   NE2                                                    
REMARK 620 2 HEC D 105   NA   89.9                                              
REMARK 620 3 HEC D 105   NB   89.0  90.9                                        
REMARK 620 4 HEC D 105   NC   90.4 179.7  89.2                                  
REMARK 620 5 HEC D 105   ND   91.2  88.3 179.2  91.6                            
REMARK 620 6 HOH D 204   O   176.5  90.6  94.5  89.1  85.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC B 105  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  18   NE2                                                    
REMARK 620 2 HEC B 105   NA   95.8                                              
REMARK 620 3 HEC B 105   NB   91.2  91.4                                        
REMARK 620 4 HEC B 105   NC   87.7 176.1  90.1                                  
REMARK 620 5 HEC B 105   ND   87.1  90.1 177.9  88.5                            
REMARK 620 6 HOH B 202   O   176.7  87.3  87.6  89.3  94.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 105                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 105                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 105                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 C 1005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 1009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 105                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 D 1006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE D 1010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM E 105                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 E 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG E 1011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM F 105                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 F 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE F 1012                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3NBS   RELATED DB: PDB                                   
REMARK 900 DIMERIC STRUCTURE                                                    
DBREF  3NBT A    1   104  UNP    P00004   CYC_HORSE        2    105             
DBREF  3NBT B    1   104  UNP    P00004   CYC_HORSE        2    105             
DBREF  3NBT C    1   104  UNP    P00004   CYC_HORSE        2    105             
DBREF  3NBT D    1   104  UNP    P00004   CYC_HORSE        2    105             
DBREF  3NBT E    1   104  UNP    P00004   CYC_HORSE        2    105             
DBREF  3NBT F    1   104  UNP    P00004   CYC_HORSE        2    105             
SEQRES   1 A  104  GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN LYS          
SEQRES   2 A  104  CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS HIS          
SEQRES   3 A  104  LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG LYS          
SEQRES   4 A  104  THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA ASN          
SEQRES   5 A  104  LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU MET          
SEQRES   6 A  104  GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR          
SEQRES   7 A  104  LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU ARG          
SEQRES   8 A  104  GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU          
SEQRES   1 B  104  GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN LYS          
SEQRES   2 B  104  CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS HIS          
SEQRES   3 B  104  LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG LYS          
SEQRES   4 B  104  THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA ASN          
SEQRES   5 B  104  LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU MET          
SEQRES   6 B  104  GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR          
SEQRES   7 B  104  LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU ARG          
SEQRES   8 B  104  GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU          
SEQRES   1 C  104  GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN LYS          
SEQRES   2 C  104  CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS HIS          
SEQRES   3 C  104  LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG LYS          
SEQRES   4 C  104  THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA ASN          
SEQRES   5 C  104  LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU MET          
SEQRES   6 C  104  GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR          
SEQRES   7 C  104  LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU ARG          
SEQRES   8 C  104  GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU          
SEQRES   1 D  104  GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN LYS          
SEQRES   2 D  104  CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS HIS          
SEQRES   3 D  104  LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG LYS          
SEQRES   4 D  104  THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA ASN          
SEQRES   5 D  104  LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU MET          
SEQRES   6 D  104  GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR          
SEQRES   7 D  104  LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU ARG          
SEQRES   8 D  104  GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU          
SEQRES   1 E  104  GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN LYS          
SEQRES   2 E  104  CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS HIS          
SEQRES   3 E  104  LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG LYS          
SEQRES   4 E  104  THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA ASN          
SEQRES   5 E  104  LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU MET          
SEQRES   6 E  104  GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR          
SEQRES   7 E  104  LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU ARG          
SEQRES   8 E  104  GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU          
SEQRES   1 F  104  GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN LYS          
SEQRES   2 F  104  CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS HIS          
SEQRES   3 F  104  LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG LYS          
SEQRES   4 F  104  THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA ASN          
SEQRES   5 F  104  LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU MET          
SEQRES   6 F  104  GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR          
SEQRES   7 F  104  LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU ARG          
SEQRES   8 F  104  GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU          
HET    HEC  A 105      43                                                       
HET    PG4  A1001      13                                                       
HET    PEG  A1007       7                                                       
HET    HEC  B 105      43                                                       
HET    PG4  B1004      13                                                       
HET    PEG  B1008       7                                                       
HET    HEC  C 105      43                                                       
HET    PG4  C1005      13                                                       
HET    PEG  C1009       7                                                       
HET    HEC  D 105      43                                                       
HET    PG4  D1006      13                                                       
HET    PGE  D1010      10                                                       
HET    HEC  E 105      43                                                       
HET    PG4  E1002      13                                                       
HET    PEG  E1011       7                                                       
HET    HEC  F 105      43                                                       
HET    PG4  F1003      13                                                       
HET    PGE  F1012      10                                                       
HETNAM     HEC HEME C                                                           
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     PGE TRIETHYLENE GLYCOL                                               
FORMUL   7  HEC    6(C34 H34 FE N4 O4)                                          
FORMUL   8  PG4    6(C8 H18 O5)                                                 
FORMUL   9  PEG    4(C4 H10 O3)                                                 
FORMUL  18  PGE    2(C6 H14 O4)                                                 
FORMUL  25  HOH   *345(H2 O)                                                    
HELIX    1   1 ASP A    2  CYS A   14  1                                  13    
HELIX    2   2 THR A   49  LYS A   55  1                                   7    
HELIX    3   3 LYS A   60  LEU A   68  1                                   9    
HELIX    4   4 ASN A   70  ILE A   75  1                                   6    
HELIX    5   5 LYS A   87  THR A  102  1                                  16    
HELIX    6   6 ASP B    2  CYS B   14  1                                  13    
HELIX    7   7 THR B   49  LYS B   55  1                                   7    
HELIX    8   8 LYS B   60  ASN B   70  1                                  11    
HELIX    9   9 ASN B   70  ILE B   75  1                                   6    
HELIX   10  10 LYS B   87  THR B  102  1                                  16    
HELIX   11  11 ASP C    2  CYS C   14  1                                  13    
HELIX   12  12 THR C   49  ASN C   54  1                                   6    
HELIX   13  13 LYS C   60  ASN C   70  1                                  11    
HELIX   14  14 ASN C   70  ILE C   75  1                                   6    
HELIX   15  15 LYS C   87  THR C  102  1                                  16    
HELIX   16  16 ASP D    2  CYS D   14  1                                  13    
HELIX   17  17 THR D   49  ASN D   54  1                                   6    
HELIX   18  18 LYS D   60  ASN D   70  1                                  11    
HELIX   19  19 ASN D   70  ILE D   75  1                                   6    
HELIX   20  20 LYS D   87  THR D  102  1                                  16    
HELIX   21  21 ASP E    2  CYS E   14  1                                  13    
HELIX   22  22 THR E   49  LYS E   55  1                                   7    
HELIX   23  23 LYS E   60  ASN E   70  1                                  11    
HELIX   24  24 ASN E   70  ILE E   75  1                                   6    
HELIX   25  25 LYS E   87  THR E  102  1                                  16    
HELIX   26  26 ASP F    2  CYS F   14  1                                  13    
HELIX   27  27 THR F   49  ASN F   54  1                                   6    
HELIX   28  28 LYS F   60  ASN F   70  1                                  11    
HELIX   29  29 ASN F   70  ILE F   75  1                                   6    
HELIX   30  30 LYS F   87  THR F  102  1                                  16    
LINK         NE2 HIS E  18                FE   HEC E 105     1555   1555  1.96  
LINK         NE2 HIS A  18                FE   HEC A 105     1555   1555  1.96  
LINK         NE2 HIS F  18                FE   HEC F 105     1555   1555  1.98  
LINK         NE2 HIS C  18                FE   HEC C 105     1555   1555  1.99  
LINK         NE2 HIS D  18                FE   HEC D 105     1555   1555  1.99  
LINK         NE2 HIS B  18                FE   HEC B 105     1555   1555  2.00  
LINK         SG  CYS A  14                 CAB HEC A 105     1555   1555  1.85  
LINK         SG  CYS A  17                 CAC HEC A 105     1555   1555  1.85  
LINK         SG  CYS B  14                 CAB HEC B 105     1555   1555  1.85  
LINK         SG  CYS B  17                 CAC HEC B 105     1555   1555  1.84  
LINK         SG  CYS C  14                 CAB HEC C 105     1555   1555  1.85  
LINK         SG  CYS C  17                 CAC HEC C 105     1555   1555  1.86  
LINK         SG  CYS D  14                 CAB HEC D 105     1555   1555  1.85  
LINK         SG  CYS D  17                 CAC HEC D 105     1555   1555  1.84  
LINK         SG  CYS E  14                 CAB HEC E 105     1555   1555  1.85  
LINK         SG  CYS E  17                 CAC HEC E 105     1555   1555  1.86  
LINK         SG  CYS F  14                 CAB HEC F 105     1555   1555  1.84  
LINK         SG  CYS F  17                 CAC HEC F 105     1555   1555  1.83  
LINK        FE   HEC C 105                 O   HOH C 203     1555   1555  2.09  
LINK        FE   HEC D 105                 O   HOH D 204     1555   1555  2.11  
LINK        FE   HEC F 105                 O   HOH F 206     1555   1555  2.11  
LINK        FE   HEC A 105                 O   HOH A 201     1555   1555  2.11  
LINK        FE   HEC E 105                 O   HOH E 205     1555   1555  2.11  
LINK        FE   HEC B 105                 O   HOH B 202     1555   1555  2.12  
SITE     1 AC1 24 LYS A  13  CYS A  14  CYS A  17  HIS A  18                    
SITE     2 AC1 24 THR A  28  GLY A  29  PRO A  30  THR A  40                    
SITE     3 AC1 24 GLY A  41  TYR A  48  THR A  49  ASN A  52                    
SITE     4 AC1 24 TRP A  59  TYR A  67  LEU A  68  THR A  78                    
SITE     5 AC1 24 LYS A  79  MET A  80  HOH A 201  HOH A 243                    
SITE     6 AC1 24 HOH A 437  PEG A1007  PHE E  82  LEU E  94                    
SITE     1 AC2  7 LYS A  55  ILE A  57  GLU A  66  LYS A  73                    
SITE     2 AC2  7 TYR A  74  PRO A  76  HOH A 305                               
SITE     1 AC3  7 THR A  28  THR A  47  LYS A  79  GLY A  84                    
SITE     2 AC3  7 HEC A 105  HOH A 238  HOH A 496                               
SITE     1 AC4 21 LYS B  13  CYS B  14  CYS B  17  HIS B  18                    
SITE     2 AC4 21 THR B  28  GLY B  29  ARG B  38  THR B  40                    
SITE     3 AC4 21 GLY B  41  TYR B  48  THR B  49  ASN B  52                    
SITE     4 AC4 21 TRP B  59  TYR B  67  THR B  78  LYS B  79                    
SITE     5 AC4 21 MET B  80  HOH B 202  HOH B 495  PEG B1008                    
SITE     6 AC4 21 PHE C  82                                                     
SITE     1 AC5  6 LYS B  55  ILE B  57  GLU B  66  LYS B  73                    
SITE     2 AC5  6 TYR B  74  ASP E  50                                          
SITE     1 AC6  8 THR B  47  TYR B  48  THR B  49  LYS B  79                    
SITE     2 AC6  8 ILE B  81  GLY B  84  HEC B 105  HOH B 407                    
SITE     1 AC7 23 LYS C  13  CYS C  14  CYS C  17  HIS C  18                    
SITE     2 AC7 23 THR C  28  GLY C  29  PRO C  30  THR C  40                    
SITE     3 AC7 23 GLY C  41  TYR C  48  THR C  49  ASN C  52                    
SITE     4 AC7 23 TRP C  59  TYR C  67  LEU C  68  THR C  78                    
SITE     5 AC7 23 LYS C  79  MET C  80  HOH C 203  HOH C 227                    
SITE     6 AC7 23 HOH C 265  PHE D  82  LEU D  94                               
SITE     1 AC8  7 ASP A  50  LYS C  55  ILE C  57  LYS C  73                    
SITE     2 AC8  7 TYR C  74  PRO C  76  HOH C 545                               
SITE     1 AC9  7 THR C  28  THR C  47  THR C  49  ILE C  81                    
SITE     2 AC9  7 GLY C  84  HOH C 419  HOH C 433                               
SITE     1 BC1 21 PHE B  82  LEU B  94  LYS D  13  CYS D  14                    
SITE     2 BC1 21 CYS D  17  HIS D  18  THR D  28  GLY D  29                    
SITE     3 BC1 21 THR D  40  GLY D  41  TYR D  48  THR D  49                    
SITE     4 BC1 21 ASN D  52  TRP D  59  TYR D  67  THR D  78                    
SITE     5 BC1 21 LYS D  79  MET D  80  HOH D 204  HOH D 247                    
SITE     6 BC1 21 PGE D1010                                                     
SITE     1 BC2  6 LYS D  55  GLU D  66  LYS D  73  TYR D  74                    
SITE     2 BC2  6 PRO D  76  HOH F 411                                          
SITE     1 BC3 11 THR D  28  THR D  47  TYR D  48  THR D  49                    
SITE     2 BC3 11 LYS D  79  ILE D  81  PHE D  82  GLY D  84                    
SITE     3 BC3 11 HEC D 105  HOH D 234  HOH D 516                               
SITE     1 BC4 21 LYS E  13  CYS E  14  CYS E  17  HIS E  18                    
SITE     2 BC4 21 THR E  28  GLY E  29  THR E  40  GLY E  41                    
SITE     3 BC4 21 TYR E  48  THR E  49  ASN E  52  TRP E  59                    
SITE     4 BC4 21 LEU E  64  TYR E  67  THR E  78  LYS E  79                    
SITE     5 BC4 21 MET E  80  HOH E 205  PEG E1011  PHE F  82                    
SITE     6 BC4 21 LEU F  94                                                     
SITE     1 BC5  7 ASP B  50  LYS E  55  GLU E  66  LYS E  73                    
SITE     2 BC5  7 TYR E  74  PRO E  76  HOH E 279                               
SITE     1 BC6  7 THR E  28  THR E  47  THR E  49  LYS E  79                    
SITE     2 BC6  7 ILE E  81  HEC E 105  HOH E 288                               
SITE     1 BC7 21 PHE A  82  LEU A  94  LYS F  13  CYS F  14                    
SITE     2 BC7 21 CYS F  17  HIS F  18  THR F  28  GLY F  29                    
SITE     3 BC7 21 THR F  40  GLY F  41  TYR F  48  THR F  49                    
SITE     4 BC7 21 ASN F  52  TRP F  59  TYR F  67  THR F  78                    
SITE     5 BC7 21 LYS F  79  MET F  80  HOH F 206  HOH F 289                    
SITE     6 BC7 21 PGE F1012                                                     
SITE     1 BC8  5 HOH D 325  LYS F  55  LYS F  73  TYR F  74                    
SITE     2 BC8  5 PRO F  76                                                     
SITE     1 BC9  9 THR F  47  THR F  49  ILE F  81  PHE F  82                    
SITE     2 BC9  9 GLY F  84  HEC F 105  HOH F 253  HOH F 374                    
SITE     3 BC9  9 HOH F 392                                                     
CRYST1   57.204   95.661  130.935  90.00  90.00  90.00 P 21 21 21   24          
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      0.017481  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010454  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007637        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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