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Database: PDB
Entry: 4NOS
LinkDB: 4NOS
Original site: 4NOS 
HEADER    OXIDOREDUCTASE                          03-FEB-99   4NOS              
TITLE     HUMAN INDUCIBLE NITRIC OXIDE SYNTHASE WITH INHIBITOR                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INDUCIBLE NITRIC OXIDE SYNTHASE;                           
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: OXYGENASE DOMAIN;                                          
COMPND   5 SYNONYM: INOS, NOS2;                                                 
COMPND   6 EC: 1.14.13.39;                                                      
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PINOS60-3                                 
KEYWDS    L-ARGININE MONOOXYGENASE, NITRIC OXIDE, HUMAN, ZNS4, OXIDOREDUCTASE   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.O.FISCHMANN,P.C.WEBER                                               
REVDAT   4   13-JUL-11 4NOS    1       VERSN                                    
REVDAT   3   24-FEB-09 4NOS    1       VERSN                                    
REVDAT   2   01-APR-03 4NOS    1       JRNL                                     
REVDAT   1   04-FEB-00 4NOS    0                                                
JRNL        AUTH   T.O.FISCHMANN,A.HRUZA,X.D.NIU,J.D.FOSSETTA,C.A.LUNN,         
JRNL        AUTH 2 E.DOLPHIN,A.J.PRONGAY,P.REICHERT,D.J.LUNDELL,S.K.NARULA,     
JRNL        AUTH 3 P.C.WEBER                                                    
JRNL        TITL   STRUCTURAL CHARACTERIZATION OF NITRIC OXIDE SYNTHASE         
JRNL        TITL 2 ISOFORMS REVEALS STRIKING ACTIVE-SITE CONSERVATION.          
JRNL        REF    NAT.STRUCT.BIOL.              V.   6   233 1999              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   10074942                                                     
JRNL        DOI    10.1038/6675                                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 0.000                          
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 88.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 109101                         
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) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.289                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5550                            
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           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.33                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 80.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 9281                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3000                       
REMARK   3   BIN FREE R VALUE                    : 0.3400                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 490                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.020                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13680                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 266                                     
REMARK   3   SOLVENT ATOMS            : 1371                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
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) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.63                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
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 : RESTRAINTS                                              
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  : NULL                                           
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4NOS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-FEB-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB000443.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-DEC-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.00                             
REMARK 200  PH                             : 6.90                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 113089                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 18.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.2                               
REMARK 200  DATA REDUNDANCY                : 2.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.29                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.23000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS                        
REMARK 200 SOFTWARE USED: SHARP, SOLOMON                                        
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.90                                  
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       44.87950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       95.02200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       78.33600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       95.02200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       44.87950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       78.33600            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 10030 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 32100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -114.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 9930 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 32360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -114.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO A    82                                                      
REMARK 465     GLU A   504                                                      
REMARK 465     LYS A   505                                                      
REMARK 465     ARG A   506                                                      
REMARK 465     ARG A   507                                                      
REMARK 465     PRO A   508                                                      
REMARK 465     PRO B    82                                                      
REMARK 465     GLU B   504                                                      
REMARK 465     LYS B   505                                                      
REMARK 465     ARG B   506                                                      
REMARK 465     ARG B   507                                                      
REMARK 465     PRO B   508                                                      
REMARK 465     PRO C    82                                                      
REMARK 465     GLU C   504                                                      
REMARK 465     LYS C   505                                                      
REMARK 465     ARG C   506                                                      
REMARK 465     ARG C   507                                                      
REMARK 465     PRO C   508                                                      
REMARK 465     PRO D    82                                                      
REMARK 465     GLU D   504                                                      
REMARK 465     LYS D   505                                                      
REMARK 465     ARG D   506                                                      
REMARK 465     ARG D   507                                                      
REMARK 465     PRO D   508                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP A 503    CA   C    O    CB   CG   OD1  OD2                   
REMARK 470     ASP B 503    CA   C    O    CB   CG   OD1  OD2                   
REMARK 470     ASP C 503    CA   C    O    CB   CG   OD1  OD2                   
REMARK 470     ASP D 503    CA   C    O    CB   CG   OD1  OD2                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    ASP C   137     O    HOH B  1165     4455     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO C 129   C   -  N   -  CA  ANGL. DEV. =   9.6 DEGREES          
REMARK 500    ARG D 221   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG D 221   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 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    LYS A 158       85.19   -152.79                                   
REMARK 500    ARG A 203      -12.67    -48.02                                   
REMARK 500    ALA A 214       39.62   -143.47                                   
REMARK 500    SER A 218      -11.03   -144.48                                   
REMARK 500    ASN A 236       43.59     36.79                                   
REMARK 500    SER A 251      -78.48    -99.72                                   
REMARK 500    LYS A 335      -33.77   -131.88                                   
REMARK 500    CYS A 367       65.62   -163.06                                   
REMARK 500    ARG A 388     -133.14   -118.07                                   
REMARK 500    CYS A 457       93.50   -174.32                                   
REMARK 500    LEU A 485     -166.80   -102.73                                   
REMARK 500    SER B 114      143.72   -171.24                                   
REMARK 500    THR B 121       66.69   -114.78                                   
REMARK 500    LYS B 158       73.70   -107.26                                   
REMARK 500    SER B 218      -23.58   -142.32                                   
REMARK 500    ASN B 236       42.97     39.25                                   
REMARK 500    SER B 251      -87.20    -98.31                                   
REMARK 500    CYS B 367       65.23   -163.13                                   
REMARK 500    ARG B 388     -137.10   -124.32                                   
REMARK 500    CYS B 457       96.15   -164.12                                   
REMARK 500    GLN B 502     -168.74   -117.75                                   
REMARK 500    SER C 114      134.97   -170.56                                   
REMARK 500    TRP C 206      -28.79    -38.79                                   
REMARK 500    ASN C 236       38.30     30.56                                   
REMARK 500    ILE C 240      133.42    -37.10                                   
REMARK 500    SER C 251      -84.47    -98.70                                   
REMARK 500    ASP C 274       38.60    -76.95                                   
REMARK 500    SER C 276      171.01    177.10                                   
REMARK 500    TYR C 299       41.32     73.32                                   
REMARK 500    LYS C 335      -33.66   -131.88                                   
REMARK 500    PRO C 365        1.78    -68.15                                   
REMARK 500    CYS C 367       56.09   -157.72                                   
REMARK 500    ARG C 388     -136.66   -130.92                                   
REMARK 500    ILE C 433      144.52   -171.34                                   
REMARK 500    CYS C 457       92.97   -167.30                                   
REMARK 500    TRP D 206      -29.83    -36.37                                   
REMARK 500    ASN D 208       79.67   -106.00                                   
REMARK 500    SER D 218      -19.44   -142.47                                   
REMARK 500    ASN D 236       45.17     31.90                                   
REMARK 500    SER D 251      -85.66   -108.28                                   
REMARK 500    LYS D 335      -33.66   -132.61                                   
REMARK 500    TRP D 338       -9.72    -58.77                                   
REMARK 500    CYS D 367       61.66   -160.11                                   
REMARK 500    ARG D 388     -133.09   -118.59                                   
REMARK 500    CYS D 457       88.01   -177.69                                   
REMARK 500    GLN D 502      -73.77    -69.58                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ARG A 203        24.6      L          L   OUTSIDE RANGE           
REMARK 500    TRP D 206        24.5      L          L   OUTSIDE RANGE           
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 A3229        DISTANCE =  7.19 ANGSTROMS                       
REMARK 525    HOH B1314        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH C2287        DISTANCE =  7.87 ANGSTROMS                       
REMARK 525    HOH C2324        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH C2335        DISTANCE =  6.51 ANGSTROMS                       
REMARK 525    HOH C2337        DISTANCE =  5.73 ANGSTROMS                       
REMARK 525    HOH C2342        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH D3309        DISTANCE =  5.59 ANGSTROMS                       
REMARK 525    HOH D3332        DISTANCE =  5.61 ANGSTROMS                       
REMARK 525    HOH D3359        DISTANCE =  5.80 ANGSTROMS                       
REMARK 525    HOH D3362        DISTANCE =  5.83 ANGSTROMS                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 HIGH-SPIN STATE                                                      
REMARK 600                                                                      
REMARK 600 ZNS4 CLUSTER LOCATED AT THE DIMER INTERFACE                          
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 A3000  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 110   SG                                                     
REMARK 620 2 CYS A 115   SG  108.8                                              
REMARK 620 3 CYS B 110   SG  110.5 116.4                                        
REMARK 620 4 CYS B 115   SG  106.6 106.3 107.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 510  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 200   SG                                                     
REMARK 620 2 HEM A 510   NA  111.8                                              
REMARK 620 3 HEM A 510   NB  106.3  86.7                                        
REMARK 620 4 HEM A 510   NC   94.6 153.4  89.1                                  
REMARK 620 5 HEM A 510   ND   99.3  88.1 153.9  84.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B1010  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 200   SG                                                     
REMARK 620 2 HEM B1010   NA  105.2                                              
REMARK 620 3 HEM B1010   NB  101.5  91.6                                        
REMARK 620 4 HEM B1010   NC   98.1 156.7  85.7                                  
REMARK 620 5 HEM B1010   ND  100.6  87.2 157.4  86.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C2000  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 110   SG                                                     
REMARK 620 2 CYS C 115   SG  108.5                                              
REMARK 620 3 CYS D 110   SG  115.8 115.7                                        
REMARK 620 4 CYS D 115   SG  101.6 106.5 107.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C2010  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 200   SG                                                     
REMARK 620 2 HEM C2010   NA  110.5                                              
REMARK 620 3 HEM C2010   NB   99.7  86.6                                        
REMARK 620 4 HEM C2010   NC   95.7 153.7  86.3                                  
REMARK 620 5 HEM C2010   ND  104.4  88.8 155.5  87.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM D3010  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 200   SG                                                     
REMARK 620 2 HEM D3010   NA  100.9                                              
REMARK 620 3 HEM D3010   NB   99.4  86.0                                        
REMARK 620 4 HEM D3010   NC  100.7 158.1  86.8                                  
REMARK 620 5 HEM D3010   ND  101.3  89.9 159.3  89.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: COF                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: COFACTORS                                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SUB                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: INHIBITOR                                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ZNB                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: ZN BINDING SITE AT THE DIMERIZATION INTERFACE 2    
REMARK 800  MOTIFS CX4C                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 3000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 2000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H2B A 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ITU A 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 1010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B B 1011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ITU B 1012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 2010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B C 2011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ITU C 2012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 3010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B D 3011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ITU D 3012                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3NOS   RELATED DB: PDB                                   
DBREF  4NOS A   82   508  UNP    P35228   NOS2A_HUMAN     82    508             
DBREF  4NOS B   82   508  UNP    P35228   NOS2A_HUMAN     82    508             
DBREF  4NOS C   82   508  UNP    P35228   NOS2A_HUMAN     82    508             
DBREF  4NOS D   82   508  UNP    P35228   NOS2A_HUMAN     82    508             
SEQADV 4NOS ILE A  423  UNP  P35228    LEU   423 CONFLICT                       
SEQADV 4NOS ILE B  423  UNP  P35228    LEU   423 CONFLICT                       
SEQADV 4NOS ILE C  423  UNP  P35228    LEU   423 CONFLICT                       
SEQADV 4NOS ILE D  423  UNP  P35228    LEU   423 CONFLICT                       
SEQRES   1 A  427  PRO ARG HIS VAL ARG ILE LYS ASN TRP GLY SER GLY MET          
SEQRES   2 A  427  THR PHE GLN ASP THR LEU HIS HIS LYS ALA LYS GLY ILE          
SEQRES   3 A  427  LEU THR CYS ARG SER LYS SER CYS LEU GLY SER ILE MET          
SEQRES   4 A  427  THR PRO LYS SER LEU THR ARG GLY PRO ARG ASP LYS PRO          
SEQRES   5 A  427  THR PRO PRO ASP GLU LEU LEU PRO GLN ALA ILE GLU PHE          
SEQRES   6 A  427  VAL ASN GLN TYR TYR GLY SER PHE LYS GLU ALA LYS ILE          
SEQRES   7 A  427  GLU GLU HIS LEU ALA ARG VAL GLU ALA VAL THR LYS GLU          
SEQRES   8 A  427  ILE GLU THR THR GLY THR TYR GLN LEU THR GLY ASP GLU          
SEQRES   9 A  427  LEU ILE PHE ALA THR LYS GLN ALA TRP ARG ASN ALA PRO          
SEQRES  10 A  427  ARG CYS ILE GLY ARG ILE GLN TRP SER ASN LEU GLN VAL          
SEQRES  11 A  427  PHE ASP ALA ARG SER CYS SER THR ALA ARG GLU MET PHE          
SEQRES  12 A  427  GLU HIS ILE CYS ARG HIS VAL ARG TYR SER THR ASN ASN          
SEQRES  13 A  427  GLY ASN ILE ARG SER ALA ILE THR VAL PHE PRO GLN ARG          
SEQRES  14 A  427  SER ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN ALA GLN          
SEQRES  15 A  427  LEU ILE ARG TYR ALA GLY TYR GLN MET PRO ASP GLY SER          
SEQRES  16 A  427  ILE ARG GLY ASP PRO ALA ASN VAL GLU PHE THR GLN LEU          
SEQRES  17 A  427  CYS ILE ASP LEU GLY TRP LYS PRO LYS TYR GLY ARG PHE          
SEQRES  18 A  427  ASP VAL VAL PRO LEU VAL LEU GLN ALA ASN GLY ARG ASP          
SEQRES  19 A  427  PRO GLU LEU PHE GLU ILE PRO PRO ASP LEU VAL LEU GLU          
SEQRES  20 A  427  VAL ALA MET GLU HIS PRO LYS TYR GLU TRP PHE ARG GLU          
SEQRES  21 A  427  LEU GLU LEU LYS TRP TYR ALA LEU PRO ALA VAL ALA ASN          
SEQRES  22 A  427  MET LEU LEU GLU VAL GLY GLY LEU GLU PHE PRO GLY CYS          
SEQRES  23 A  427  PRO PHE ASN GLY TRP TYR MET GLY THR GLU ILE GLY VAL          
SEQRES  24 A  427  ARG ASP PHE CYS ASP VAL GLN ARG TYR ASN ILE LEU GLU          
SEQRES  25 A  427  GLU VAL GLY ARG ARG MET GLY LEU GLU THR HIS LYS LEU          
SEQRES  26 A  427  ALA SER LEU TRP LYS ASP GLN ALA VAL VAL GLU ILE ASN          
SEQRES  27 A  427  ILE ALA VAL ILE HIS SER PHE GLN LYS GLN ASN VAL THR          
SEQRES  28 A  427  ILE MET ASP HIS HIS SER ALA ALA GLU SER PHE MET LYS          
SEQRES  29 A  427  TYR MET GLN ASN GLU TYR ARG SER ARG GLY GLY CYS PRO          
SEQRES  30 A  427  ALA ASP TRP ILE TRP LEU VAL PRO PRO MET SER GLY SER          
SEQRES  31 A  427  ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR VAL          
SEQRES  32 A  427  LEU SER PRO PHE TYR TYR TYR GLN VAL GLU ALA TRP LYS          
SEQRES  33 A  427  THR HIS VAL TRP GLN ASP GLU LYS ARG ARG PRO                  
SEQRES   1 B  427  PRO ARG HIS VAL ARG ILE LYS ASN TRP GLY SER GLY MET          
SEQRES   2 B  427  THR PHE GLN ASP THR LEU HIS HIS LYS ALA LYS GLY ILE          
SEQRES   3 B  427  LEU THR CYS ARG SER LYS SER CYS LEU GLY SER ILE MET          
SEQRES   4 B  427  THR PRO LYS SER LEU THR ARG GLY PRO ARG ASP LYS PRO          
SEQRES   5 B  427  THR PRO PRO ASP GLU LEU LEU PRO GLN ALA ILE GLU PHE          
SEQRES   6 B  427  VAL ASN GLN TYR TYR GLY SER PHE LYS GLU ALA LYS ILE          
SEQRES   7 B  427  GLU GLU HIS LEU ALA ARG VAL GLU ALA VAL THR LYS GLU          
SEQRES   8 B  427  ILE GLU THR THR GLY THR TYR GLN LEU THR GLY ASP GLU          
SEQRES   9 B  427  LEU ILE PHE ALA THR LYS GLN ALA TRP ARG ASN ALA PRO          
SEQRES  10 B  427  ARG CYS ILE GLY ARG ILE GLN TRP SER ASN LEU GLN VAL          
SEQRES  11 B  427  PHE ASP ALA ARG SER CYS SER THR ALA ARG GLU MET PHE          
SEQRES  12 B  427  GLU HIS ILE CYS ARG HIS VAL ARG TYR SER THR ASN ASN          
SEQRES  13 B  427  GLY ASN ILE ARG SER ALA ILE THR VAL PHE PRO GLN ARG          
SEQRES  14 B  427  SER ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN ALA GLN          
SEQRES  15 B  427  LEU ILE ARG TYR ALA GLY TYR GLN MET PRO ASP GLY SER          
SEQRES  16 B  427  ILE ARG GLY ASP PRO ALA ASN VAL GLU PHE THR GLN LEU          
SEQRES  17 B  427  CYS ILE ASP LEU GLY TRP LYS PRO LYS TYR GLY ARG PHE          
SEQRES  18 B  427  ASP VAL VAL PRO LEU VAL LEU GLN ALA ASN GLY ARG ASP          
SEQRES  19 B  427  PRO GLU LEU PHE GLU ILE PRO PRO ASP LEU VAL LEU GLU          
SEQRES  20 B  427  VAL ALA MET GLU HIS PRO LYS TYR GLU TRP PHE ARG GLU          
SEQRES  21 B  427  LEU GLU LEU LYS TRP TYR ALA LEU PRO ALA VAL ALA ASN          
SEQRES  22 B  427  MET LEU LEU GLU VAL GLY GLY LEU GLU PHE PRO GLY CYS          
SEQRES  23 B  427  PRO PHE ASN GLY TRP TYR MET GLY THR GLU ILE GLY VAL          
SEQRES  24 B  427  ARG ASP PHE CYS ASP VAL GLN ARG TYR ASN ILE LEU GLU          
SEQRES  25 B  427  GLU VAL GLY ARG ARG MET GLY LEU GLU THR HIS LYS LEU          
SEQRES  26 B  427  ALA SER LEU TRP LYS ASP GLN ALA VAL VAL GLU ILE ASN          
SEQRES  27 B  427  ILE ALA VAL ILE HIS SER PHE GLN LYS GLN ASN VAL THR          
SEQRES  28 B  427  ILE MET ASP HIS HIS SER ALA ALA GLU SER PHE MET LYS          
SEQRES  29 B  427  TYR MET GLN ASN GLU TYR ARG SER ARG GLY GLY CYS PRO          
SEQRES  30 B  427  ALA ASP TRP ILE TRP LEU VAL PRO PRO MET SER GLY SER          
SEQRES  31 B  427  ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR VAL          
SEQRES  32 B  427  LEU SER PRO PHE TYR TYR TYR GLN VAL GLU ALA TRP LYS          
SEQRES  33 B  427  THR HIS VAL TRP GLN ASP GLU LYS ARG ARG PRO                  
SEQRES   1 C  427  PRO ARG HIS VAL ARG ILE LYS ASN TRP GLY SER GLY MET          
SEQRES   2 C  427  THR PHE GLN ASP THR LEU HIS HIS LYS ALA LYS GLY ILE          
SEQRES   3 C  427  LEU THR CYS ARG SER LYS SER CYS LEU GLY SER ILE MET          
SEQRES   4 C  427  THR PRO LYS SER LEU THR ARG GLY PRO ARG ASP LYS PRO          
SEQRES   5 C  427  THR PRO PRO ASP GLU LEU LEU PRO GLN ALA ILE GLU PHE          
SEQRES   6 C  427  VAL ASN GLN TYR TYR GLY SER PHE LYS GLU ALA LYS ILE          
SEQRES   7 C  427  GLU GLU HIS LEU ALA ARG VAL GLU ALA VAL THR LYS GLU          
SEQRES   8 C  427  ILE GLU THR THR GLY THR TYR GLN LEU THR GLY ASP GLU          
SEQRES   9 C  427  LEU ILE PHE ALA THR LYS GLN ALA TRP ARG ASN ALA PRO          
SEQRES  10 C  427  ARG CYS ILE GLY ARG ILE GLN TRP SER ASN LEU GLN VAL          
SEQRES  11 C  427  PHE ASP ALA ARG SER CYS SER THR ALA ARG GLU MET PHE          
SEQRES  12 C  427  GLU HIS ILE CYS ARG HIS VAL ARG TYR SER THR ASN ASN          
SEQRES  13 C  427  GLY ASN ILE ARG SER ALA ILE THR VAL PHE PRO GLN ARG          
SEQRES  14 C  427  SER ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN ALA GLN          
SEQRES  15 C  427  LEU ILE ARG TYR ALA GLY TYR GLN MET PRO ASP GLY SER          
SEQRES  16 C  427  ILE ARG GLY ASP PRO ALA ASN VAL GLU PHE THR GLN LEU          
SEQRES  17 C  427  CYS ILE ASP LEU GLY TRP LYS PRO LYS TYR GLY ARG PHE          
SEQRES  18 C  427  ASP VAL VAL PRO LEU VAL LEU GLN ALA ASN GLY ARG ASP          
SEQRES  19 C  427  PRO GLU LEU PHE GLU ILE PRO PRO ASP LEU VAL LEU GLU          
SEQRES  20 C  427  VAL ALA MET GLU HIS PRO LYS TYR GLU TRP PHE ARG GLU          
SEQRES  21 C  427  LEU GLU LEU LYS TRP TYR ALA LEU PRO ALA VAL ALA ASN          
SEQRES  22 C  427  MET LEU LEU GLU VAL GLY GLY LEU GLU PHE PRO GLY CYS          
SEQRES  23 C  427  PRO PHE ASN GLY TRP TYR MET GLY THR GLU ILE GLY VAL          
SEQRES  24 C  427  ARG ASP PHE CYS ASP VAL GLN ARG TYR ASN ILE LEU GLU          
SEQRES  25 C  427  GLU VAL GLY ARG ARG MET GLY LEU GLU THR HIS LYS LEU          
SEQRES  26 C  427  ALA SER LEU TRP LYS ASP GLN ALA VAL VAL GLU ILE ASN          
SEQRES  27 C  427  ILE ALA VAL ILE HIS SER PHE GLN LYS GLN ASN VAL THR          
SEQRES  28 C  427  ILE MET ASP HIS HIS SER ALA ALA GLU SER PHE MET LYS          
SEQRES  29 C  427  TYR MET GLN ASN GLU TYR ARG SER ARG GLY GLY CYS PRO          
SEQRES  30 C  427  ALA ASP TRP ILE TRP LEU VAL PRO PRO MET SER GLY SER          
SEQRES  31 C  427  ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR VAL          
SEQRES  32 C  427  LEU SER PRO PHE TYR TYR TYR GLN VAL GLU ALA TRP LYS          
SEQRES  33 C  427  THR HIS VAL TRP GLN ASP GLU LYS ARG ARG PRO                  
SEQRES   1 D  427  PRO ARG HIS VAL ARG ILE LYS ASN TRP GLY SER GLY MET          
SEQRES   2 D  427  THR PHE GLN ASP THR LEU HIS HIS LYS ALA LYS GLY ILE          
SEQRES   3 D  427  LEU THR CYS ARG SER LYS SER CYS LEU GLY SER ILE MET          
SEQRES   4 D  427  THR PRO LYS SER LEU THR ARG GLY PRO ARG ASP LYS PRO          
SEQRES   5 D  427  THR PRO PRO ASP GLU LEU LEU PRO GLN ALA ILE GLU PHE          
SEQRES   6 D  427  VAL ASN GLN TYR TYR GLY SER PHE LYS GLU ALA LYS ILE          
SEQRES   7 D  427  GLU GLU HIS LEU ALA ARG VAL GLU ALA VAL THR LYS GLU          
SEQRES   8 D  427  ILE GLU THR THR GLY THR TYR GLN LEU THR GLY ASP GLU          
SEQRES   9 D  427  LEU ILE PHE ALA THR LYS GLN ALA TRP ARG ASN ALA PRO          
SEQRES  10 D  427  ARG CYS ILE GLY ARG ILE GLN TRP SER ASN LEU GLN VAL          
SEQRES  11 D  427  PHE ASP ALA ARG SER CYS SER THR ALA ARG GLU MET PHE          
SEQRES  12 D  427  GLU HIS ILE CYS ARG HIS VAL ARG TYR SER THR ASN ASN          
SEQRES  13 D  427  GLY ASN ILE ARG SER ALA ILE THR VAL PHE PRO GLN ARG          
SEQRES  14 D  427  SER ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN ALA GLN          
SEQRES  15 D  427  LEU ILE ARG TYR ALA GLY TYR GLN MET PRO ASP GLY SER          
SEQRES  16 D  427  ILE ARG GLY ASP PRO ALA ASN VAL GLU PHE THR GLN LEU          
SEQRES  17 D  427  CYS ILE ASP LEU GLY TRP LYS PRO LYS TYR GLY ARG PHE          
SEQRES  18 D  427  ASP VAL VAL PRO LEU VAL LEU GLN ALA ASN GLY ARG ASP          
SEQRES  19 D  427  PRO GLU LEU PHE GLU ILE PRO PRO ASP LEU VAL LEU GLU          
SEQRES  20 D  427  VAL ALA MET GLU HIS PRO LYS TYR GLU TRP PHE ARG GLU          
SEQRES  21 D  427  LEU GLU LEU LYS TRP TYR ALA LEU PRO ALA VAL ALA ASN          
SEQRES  22 D  427  MET LEU LEU GLU VAL GLY GLY LEU GLU PHE PRO GLY CYS          
SEQRES  23 D  427  PRO PHE ASN GLY TRP TYR MET GLY THR GLU ILE GLY VAL          
SEQRES  24 D  427  ARG ASP PHE CYS ASP VAL GLN ARG TYR ASN ILE LEU GLU          
SEQRES  25 D  427  GLU VAL GLY ARG ARG MET GLY LEU GLU THR HIS LYS LEU          
SEQRES  26 D  427  ALA SER LEU TRP LYS ASP GLN ALA VAL VAL GLU ILE ASN          
SEQRES  27 D  427  ILE ALA VAL ILE HIS SER PHE GLN LYS GLN ASN VAL THR          
SEQRES  28 D  427  ILE MET ASP HIS HIS SER ALA ALA GLU SER PHE MET LYS          
SEQRES  29 D  427  TYR MET GLN ASN GLU TYR ARG SER ARG GLY GLY CYS PRO          
SEQRES  30 D  427  ALA ASP TRP ILE TRP LEU VAL PRO PRO MET SER GLY SER          
SEQRES  31 D  427  ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR VAL          
SEQRES  32 D  427  LEU SER PRO PHE TYR TYR TYR GLN VAL GLU ALA TRP LYS          
SEQRES  33 D  427  THR HIS VAL TRP GLN ASP GLU LYS ARG ARG PRO                  
HET     ZN  A3000       1                                                       
HET     ZN  C2000       1                                                       
HET    HEM  A 510      43                                                       
HET    H2B  A 511      17                                                       
HET    ITU  A 512       6                                                       
HET    HEM  B1010      43                                                       
HET    H4B  B1011      17                                                       
HET    ITU  B1012       6                                                       
HET    HEM  C2010      43                                                       
HET    H4B  C2011      17                                                       
HET    ITU  C2012       6                                                       
HET    HEM  D3010      43                                                       
HET    H4B  D3011      17                                                       
HET    ITU  D3012       6                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     H2B 2-AMINO-6-(1,2-DIHYDROXY-PROPYL)-7,8-DIHYDRO-6H-                 
HETNAM   2 H2B  PTERIDIN-4-ONE                                                  
HETNAM     ITU ETHYLISOTHIOUREA                                                 
HETNAM     H4B 5,6,7,8-TETRAHYDROBIOPTERIN                                      
HETSYN     HEM HEME                                                             
HETSYN     H2B QUINONOID 7,8-TETRAHYDROBIOPTERIN                                
FORMUL   5   ZN    2(ZN 2+)                                                     
FORMUL   7  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL   8  H2B    C9 H13 N5 O3                                                 
FORMUL   9  ITU    4(C3 H8 N2 S)                                                
FORMUL  11  H4B    3(C9 H15 N5 O3)                                              
FORMUL  19  HOH   *1371(H2 O)                                                   
HELIX    1   1 LEU A  100  LYS A  103  5                                   4    
HELIX    2   2 LYS A  123  LEU A  125  5                                   3    
HELIX    3   3 PRO A  136  SER A  153  1                                  18    
HELIX    4   4 ILE A  159  THR A  176  1                                  18    
HELIX    5   5 GLY A  183  ARG A  195  1                                  13    
HELIX    6   6 ARG A  203  SER A  207  5                                   5    
HELIX    7   7 ALA A  220  GLY A  238  1                                  19    
HELIX    8   8 PRO A  281  ASP A  292  5                                  12    
HELIX    9   9 PRO A  323  LEU A  325  5                                   3    
HELIX   10  10 GLU A  337  LEU A  342  5                                   6    
HELIX   11  11 GLY A  375  GLY A  379  1                                   5    
HELIX   12  12 LEU A  392  ARG A  398  1                                   7    
HELIX   13  13 LEU A  406  SER A  408  5                                   3    
HELIX   14  14 TRP A  410  LYS A  428  1                                  19    
HELIX   15  15 HIS A  436  ARG A  454  1                                  19    
HELIX   16  16 TRP A  461  LEU A  464  1                                   4    
HELIX   17  17 GLY A  470  ILE A  472  5                                   3    
HELIX   18  18 ALA A  495  THR A  498  1                                   4    
HELIX   19  19 LEU B  100  LYS B  103  5                                   4    
HELIX   20  20 PRO B  136  SER B  153  1                                  18    
HELIX   21  21 ILE B  159  THR B  176  1                                  18    
HELIX   22  22 GLY B  183  ARG B  195  1                                  13    
HELIX   23  23 ARG B  203  GLN B  205  5                                   3    
HELIX   24  24 ALA B  220  GLY B  238  1                                  19    
HELIX   25  25 PRO B  281  LEU B  293  5                                  13    
HELIX   26  26 PRO B  323  LEU B  325  5                                   3    
HELIX   27  27 GLU B  337  LEU B  342  5                                   6    
HELIX   28  28 GLY B  375  GLY B  379  1                                   5    
HELIX   29  29 LEU B  392  MET B  399  1                                   8    
HELIX   30  30 LEU B  406  SER B  408  5                                   3    
HELIX   31  31 TRP B  410  LYS B  428  1                                  19    
HELIX   32  32 HIS B  436  ARG B  454  1                                  19    
HELIX   33  33 TRP B  461  LEU B  464  1                                   4    
HELIX   34  34 GLY B  470  ILE B  472  5                                   3    
HELIX   35  35 ALA B  495  THR B  498  1                                   4    
HELIX   36  36 LEU C  100  LYS C  103  5                                   4    
HELIX   37  37 LYS C  123  LEU C  125  5                                   3    
HELIX   38  38 PRO C  136  SER C  153  1                                  18    
HELIX   39  39 ILE C  159  THR C  176  1                                  18    
HELIX   40  40 GLY C  183  ARG C  195  1                                  13    
HELIX   41  41 ARG C  203  SER C  207  5                                   5    
HELIX   42  42 ALA C  220  GLY C  238  1                                  19    
HELIX   43  43 PRO C  281  ASP C  292  5                                  12    
HELIX   44  44 PRO C  323  LEU C  325  5                                   3    
HELIX   45  45 GLU C  337  LEU C  342  5                                   6    
HELIX   46  46 GLY C  375  GLY C  379  1                                   5    
HELIX   47  47 ARG C  381  CYS C  384  1                                   4    
HELIX   48  48 LEU C  392  MET C  399  1                                   8    
HELIX   49  49 LEU C  406  SER C  408  5                                   3    
HELIX   50  50 TRP C  410  LYS C  428  1                                  19    
HELIX   51  51 HIS C  436  ARG C  454  1                                  19    
HELIX   52  52 TRP C  461  LEU C  464  1                                   4    
HELIX   53  53 GLY C  470  ILE C  472  5                                   3    
HELIX   54  54 PRO C  474  HIS C  477  5                                   4    
HELIX   55  55 ALA C  495  LYS C  497  5                                   3    
HELIX   56  56 LEU D  100  LYS D  103  5                                   4    
HELIX   57  57 LYS D  123  LEU D  125  5                                   3    
HELIX   58  58 PRO D  136  SER D  153  1                                  18    
HELIX   59  59 ILE D  159  THR D  176  1                                  18    
HELIX   60  60 GLY D  183  ARG D  195  1                                  13    
HELIX   61  61 ARG D  203  GLN D  205  5                                   3    
HELIX   62  62 ALA D  220  GLY D  238  1                                  19    
HELIX   63  63 PRO D  281  ASP D  292  5                                  12    
HELIX   64  64 PRO D  323  LEU D  325  5                                   3    
HELIX   65  65 GLU D  337  LEU D  342  5                                   6    
HELIX   66  66 GLY D  375  GLY D  379  1                                   5    
HELIX   67  67 ARG D  381  CYS D  384  1                                   4    
HELIX   68  68 LEU D  392  MET D  399  1                                   8    
HELIX   69  69 LEU D  406  SER D  408  5                                   3    
HELIX   70  70 TRP D  410  LYS D  428  1                                  19    
HELIX   71  71 HIS D  436  ARG D  454  1                                  19    
HELIX   72  72 TRP D  461  LEU D  464  1                                   4    
HELIX   73  73 GLY D  470  ILE D  472  5                                   3    
HELIX   74  74 PRO D  474  HIS D  477  5                                   4    
HELIX   75  75 ALA D  495  THR D  498  1                                   4    
SHEET    1   A 2 VAL A  85  LYS A  88  0                                        
SHEET    2   A 2 THR A  95  ASP A  98 -1  N  ASP A  98   O  VAL A  85           
SHEET    1   B 2 GLN A 210  ALA A 214  0                                        
SHEET    2   B 2 ALA A 243  PHE A 247  1  N  ILE A 244   O  GLN A 210           
SHEET    1   C 2 GLY A 269  GLN A 271  0                                        
SHEET    2   C 2 ILE A 277  GLY A 279 -1  N  ARG A 278   O  TYR A 270           
SHEET    1   D 2 LEU A 307  LEU A 309  0                                        
SHEET    2   D 2 GLU A 317  PHE A 319 -1  N  PHE A 319   O  LEU A 307           
SHEET    1   E 2 GLU A 328  ALA A 330  0                                        
SHEET    2   E 2 LYS A 345  TYR A 347 -1  N  TRP A 346   O  VAL A 329           
SHEET    1   F 2 PRO A 350  VAL A 352  0                                        
SHEET    2   F 2 PHE A 369  GLY A 371 -1  N  GLY A 371   O  PRO A 350           
SHEET    1   G 3 PHE A 488  TYR A 490  0                                        
SHEET    2   G 3 LEU A 356  VAL A 359 -1  N  GLU A 358   O  PHE A 488           
SHEET    3   G 3 LEU A 362  PHE A 364 -1  N  PHE A 364   O  LEU A 357           
SHEET    1   H 2 VAL B  85  LYS B  88  0                                        
SHEET    2   H 2 THR B  95  ASP B  98 -1  N  ASP B  98   O  VAL B  85           
SHEET    1   I 2 GLN B 210  ALA B 214  0                                        
SHEET    2   I 2 ALA B 243  PHE B 247  1  N  ILE B 244   O  GLN B 210           
SHEET    1   J 2 GLY B 269  GLN B 271  0                                        
SHEET    2   J 2 ILE B 277  GLY B 279 -1  N  ARG B 278   O  TYR B 270           
SHEET    1   K 2 LEU B 307  LEU B 309  0                                        
SHEET    2   K 2 GLU B 317  PHE B 319 -1  N  PHE B 319   O  LEU B 307           
SHEET    1   L 2 GLU B 328  ALA B 330  0                                        
SHEET    2   L 2 LYS B 345  TYR B 347 -1  N  TRP B 346   O  VAL B 329           
SHEET    1   M 3 PHE B 488  TYR B 490  0                                        
SHEET    2   M 3 LEU B 356  VAL B 359 -1  N  GLU B 358   O  PHE B 488           
SHEET    3   M 3 LEU B 362  PHE B 364 -1  N  PHE B 364   O  LEU B 357           
SHEET    1   N 2 VAL C  85  LYS C  88  0                                        
SHEET    2   N 2 THR C  95  ASP C  98 -1  N  ASP C  98   O  VAL C  85           
SHEET    1   O 2 GLN C 210  ASP C 213  0                                        
SHEET    2   O 2 ALA C 243  VAL C 246  1  N  ILE C 244   O  GLN C 210           
SHEET    1   P 2 GLY C 269  MET C 272  0                                        
SHEET    2   P 2 SER C 276  GLY C 279 -1  N  ARG C 278   O  TYR C 270           
SHEET    1   Q 2 LEU C 307  LEU C 309  0                                        
SHEET    2   Q 2 GLU C 317  PHE C 319 -1  N  PHE C 319   O  LEU C 307           
SHEET    1   R 2 GLU C 328  ALA C 330  0                                        
SHEET    2   R 2 LYS C 345  TYR C 347 -1  N  TRP C 346   O  VAL C 329           
SHEET    1   S 2 PRO C 350  VAL C 352  0                                        
SHEET    2   S 2 PHE C 369  GLY C 371 -1  N  GLY C 371   O  PRO C 350           
SHEET    1   T 3 PHE C 488  TYR C 490  0                                        
SHEET    2   T 3 LEU C 356  VAL C 359 -1  N  GLU C 358   O  PHE C 488           
SHEET    3   T 3 LEU C 362  PHE C 364 -1  N  PHE C 364   O  LEU C 357           
SHEET    1   U 2 VAL D  85  LYS D  88  0                                        
SHEET    2   U 2 THR D  95  ASP D  98 -1  N  ASP D  98   O  VAL D  85           
SHEET    1   V 2 GLN D 210  ASP D 213  0                                        
SHEET    2   V 2 ALA D 243  VAL D 246  1  N  ILE D 244   O  GLN D 210           
SHEET    1   W 2 GLY D 269  GLN D 271  0                                        
SHEET    2   W 2 ILE D 277  GLY D 279 -1  N  ARG D 278   O  TYR D 270           
SHEET    1   X 2 LEU D 307  LEU D 309  0                                        
SHEET    2   X 2 GLU D 317  PHE D 319 -1  N  PHE D 319   O  LEU D 307           
SHEET    1   Y 2 GLU D 328  ALA D 330  0                                        
SHEET    2   Y 2 LYS D 345  TYR D 347 -1  N  TRP D 346   O  VAL D 329           
SHEET    1   Z 3 PHE D 488  TYR D 490  0                                        
SHEET    2   Z 3 LEU D 356  VAL D 359 -1  N  GLU D 358   O  PHE D 488           
SHEET    3   Z 3 LEU D 362  PHE D 364 -1  N  PHE D 364   O  LEU D 357           
LINK         SG  CYS A 110                ZN    ZN A3000     1555   1555  2.45  
LINK         SG  CYS A 115                ZN    ZN A3000     1555   1555  2.24  
LINK         SG  CYS A 200                FE   HEM A 510     1555   1555  2.38  
LINK         SG  CYS B 110                ZN    ZN A3000     1555   1555  2.28  
LINK         SG  CYS B 115                ZN    ZN A3000     1555   1555  2.45  
LINK         SG  CYS B 200                FE   HEM B1010     1555   1555  2.43  
LINK         SG  CYS C 110                ZN    ZN C2000     1555   1555  2.46  
LINK         SG  CYS C 115                ZN    ZN C2000     1555   1555  2.22  
LINK         SG  CYS C 200                FE   HEM C2010     1555   1555  2.27  
LINK         SG  CYS D 110                ZN    ZN C2000     1555   1555  2.18  
LINK         SG  CYS D 115                ZN    ZN C2000     1555   1555  2.39  
LINK         SG  CYS D 200                FE   HEM D3010     1555   1555  2.54  
CISPEP   1 SER A  486    PRO A  487          0         5.65                     
CISPEP   2 SER B  486    PRO B  487          0        -0.70                     
CISPEP   3 SER C  486    PRO C  487          0         8.49                     
CISPEP   4 SER D  486    PRO D  487          0         3.13                     
SITE     1 COF  2 HEM A 510  H2B A 511                                          
SITE     1 SUB  1 ITU A 512                                                     
SITE     1 ZNB  2 CYS A 110  CYS A 115                                          
SITE     1 AC1  4 CYS A 110  CYS A 115  CYS B 110  CYS B 115                    
SITE     1 AC2  4 CYS C 110  CYS C 115  CYS D 110  CYS D 115                    
SITE     1 AC3 20 TRP A 194  ARG A 199  CYS A 200  GLN A 205                    
SITE     2 AC3 20 SER A 242  PHE A 369  ASN A 370  TRP A 372                    
SITE     3 AC3 20 GLU A 377  TRP A 463  TYR A 489  TYR A 491                    
SITE     4 AC3 20 H2B A 511  ITU A 512  HOH A3007  HOH A3103                    
SITE     5 AC3 20 HOH A3131  HOH A3133  HOH A3203  HOH A3219                    
SITE     1 AC4 15 SER A 118  ARG A 381  ILE A 462  TRP A 463                    
SITE     2 AC4 15 HEM A 510  HOH A3001  HOH A3013  HOH A3017                    
SITE     3 AC4 15 HOH A3131  HOH A3221  TRP B 461  PHE B 476                    
SITE     4 AC4 15 HIS B 477  GLN B 478  GLU B 479                               
SITE     1 AC5  4 PHE A 369  TRP A 372  GLU A 377  HEM A 510                    
SITE     1 AC6 20 TRP B 194  ARG B 199  CYS B 200  GLN B 205                    
SITE     2 AC6 20 LEU B 209  SER B 242  PHE B 369  ASN B 370                    
SITE     3 AC6 20 TRP B 372  MET B 374  GLU B 377  TRP B 463                    
SITE     4 AC6 20 TYR B 489  TYR B 491  H4B B1011  ITU B1012                    
SITE     5 AC6 20 HOH B1059  HOH B1074  HOH B1143  HOH B1144                    
SITE     1 AC7 16 TRP A 461  PHE A 476  HIS A 477  GLN A 478                    
SITE     2 AC7 16 GLU A 479  SER B 118  MET B 120  ARG B 381                    
SITE     3 AC7 16 ILE B 462  TRP B 463  HEM B1010  HOH B1018                    
SITE     4 AC7 16 HOH B1021  HOH B1056  HOH B1113  HOH B1144                    
SITE     1 AC8  5 VAL B 352  PHE B 369  TRP B 372  GLU B 377                    
SITE     2 AC8  5 HEM B1010                                                     
SITE     1 AC9 19 TRP C 194  ARG C 199  CYS C 200  GLN C 205                    
SITE     2 AC9 19 SER C 242  PHE C 369  ASN C 370  TRP C 372                    
SITE     3 AC9 19 GLU C 377  TRP C 463  TYR C 491  H4B C2011                    
SITE     4 AC9 19 ITU C2012  HOH C2041  HOH C2075  HOH C2142                    
SITE     5 AC9 19 HOH C2161  HOH C2164  HOH C2173                               
SITE     1 BC1 16 SER C 118  ARG C 381  ILE C 462  TRP C 463                    
SITE     2 BC1 16 HEM C2010  HOH C2015  HOH C2016  HOH C2044                    
SITE     3 BC1 16 HOH C2056  HOH C2115  HOH C2142  TRP D 461                    
SITE     4 BC1 16 PHE D 476  HIS D 477  GLN D 478  GLU D 479                    
SITE     1 BC2  6 PRO C 350  PHE C 369  TRP C 372  GLU C 377                    
SITE     2 BC2  6 HEM C2010  HOH C2214                                          
SITE     1 BC3 20 TRP D 194  ARG D 199  CYS D 200  GLN D 205                    
SITE     2 BC3 20 SER D 242  PHE D 369  ASN D 370  GLY D 371                    
SITE     3 BC3 20 TRP D 372  MET D 374  GLU D 377  TRP D 463                    
SITE     4 BC3 20 TYR D 489  TYR D 491  H4B D3011  ITU D3012                    
SITE     5 BC3 20 HOH D3056  HOH D3060  HOH D3137  HOH D3153                    
SITE     1 BC4 12 TRP C 461  PHE C 476  HIS C 477  GLN C 478                    
SITE     2 BC4 12 SER D 118  ARG D 381  ILE D 462  TRP D 463                    
SITE     3 BC4 12 HEM D3010  HOH D3014  HOH D3021  HOH D3052                    
SITE     1 BC5  5 VAL D 352  PHE D 369  TRP D 372  GLU D 377                    
SITE     2 BC5  5 HEM D3010                                                     
CRYST1   89.759  156.672  190.044  90.00  90.00  90.00 P 21 21 21   16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011141  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006383  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005262        0.00000                         
MTRIX1   1 -0.992700  0.102910  0.062930       22.00306    1                    
MTRIX2   1  0.113740  0.624880  0.772390       22.59963    1                    
MTRIX3   1  0.040160  0.773910 -0.632020      -50.29379    1                    
MTRIX1   2  0.999980  0.003580 -0.004510       -1.40336    1                    
MTRIX2   2 -0.000540  0.837660  0.546200       52.21081    1                    
MTRIX3   2  0.005730 -0.546190  0.837640        8.07962    1                    
MTRIX1   3 -0.991890  0.055680  0.114290       28.94339    1                    
MTRIX2   3  0.119100  0.092600  0.988550       61.45053    1                    
MTRIX3   3  0.044460  0.994150 -0.098480      -15.62112    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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