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Database: PDB
Entry: 1NSI
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Original site: 1NSI 
HEADER    OXIDOREDUCTASE                          10-JAN-99   1NSI              
TITLE     HUMAN INDUCIBLE NITRIC OXIDE SYNTHASE, ZN-BOUND, L-ARG COMPLEX        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (NITRIC OXIDE SYNTHASE);                           
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: HEME DOMAIN;                                               
COMPND   5 SYNONYM: INOS;                                                       
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 CELL: ADENOCARCINOMA DLD-1;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    NITRIC OXIDE SYNTHASE, HEME PROTEIN, TETRAHYDROBIOPTERIN,             
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.LI,C.S.RAMAN,C.B.GLASER,E.BLASKO,T.A.YOUNG,J.F.PARKINSON,M.WHITLOW, 
AUTHOR   2 T.L.POULOS                                                           
REVDAT   3   13-JUL-11 1NSI    1       VERSN                                    
REVDAT   2   24-FEB-09 1NSI    1       VERSN                                    
REVDAT   1   07-JAN-00 1NSI    0                                                
JRNL        AUTH   H.LI,C.S.RAMAN,C.B.GLASER,E.BLASKO,T.A.YOUNG,J.F.PARKINSON,  
JRNL        AUTH 2 M.WHITLOW,T.L.POULOS                                         
JRNL        TITL   CRYSTAL STRUCTURES OF ZINC-FREE AND -BOUND HEME DOMAIN OF    
JRNL        TITL 2 HUMAN INDUCIBLE NITRIC-OXIDE SYNTHASE. IMPLICATIONS FOR      
JRNL        TITL 3 DIMER STABILITY AND COMPARISON WITH ENDOTHELIAL NITRIC-OXIDE 
JRNL        TITL 4 SYNTHASE.                                                    
JRNL        REF    J.BIOL.CHEM.                  V. 274 21276 1999              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   10409685                                                     
JRNL        DOI    10.1074/JBC.274.30.21276                                     
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   B.R.CRANE,A.S.ARVAI,D.K.GHOSH,C.WU,E.D.GETZOFF,D.J.STUEHR,   
REMARK   1  AUTH 2 J.A.TAINER                                                   
REMARK   1  TITL   STRUCTURE OF NITRIC OXIDE SYNTHASE OXYGENASE DIMER WITH      
REMARK   1  TITL 2 PTERIN AND SUBSTRATE                                         
REMARK   1  REF    SCIENCE                       V. 279  2121 1998              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   B.R.CRANE,A.S.ARVAI,R.GACHHUI,C.WU,D.K.GHOSH,E.D.GETZOFF,    
REMARK   1  AUTH 2 D.J.STUEHR,J.A.TAINER                                        
REMARK   1  TITL   THE STRUCTURE OF NITRIC OXIDE SYNTHASE OXYGENASE DOMAIN AND  
REMARK   1  TITL 2 INHIBITOR COMPLEX                                            
REMARK   1  REF    SCIENCE                       V. 278   425 1997              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   C.S.RAMAN,H.LI,P.MARTASEK,V.KRAL,B.S.MASTERS,T.L.POULOS      
REMARK   1  TITL   CRYSTAL STRUCTURE OF CONSTITUTIVE ENDOTHELIAL NITRIC OXIDE   
REMARK   1  TITL 2 SYNTHASE: A PARADIGM FOR PTERIN FUNCTION INVOLVING A NOVEL   
REMARK   1  TITL 3 METAL CENTER                                                 
REMARK   1  REF    CELL(CAMBRIDGE,MASS.)         V.  95   939 1998              
REMARK   1  REFN                   ISSN 0092-8674                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.8                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 80.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 111401                         
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) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5651                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 46.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 7561                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3130                       
REMARK   3   BIN FREE R VALUE                    : 0.3340                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 415                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13676                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 359                                     
REMARK   3   SOLVENT ATOMS            : 295                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 63.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.32                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.49                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.20                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1NSI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB007219.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-AUG-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : YES                                
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 125717                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 71.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.48800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: ENOS HEME DOMAIN                                     
REMARK 200                                                                      
REMARK 200 REMARK: ONE DIMER AS THE SEARCH MODEL                                
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 78.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.0                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.74500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       93.67500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       93.67500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      170.61750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       93.67500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       93.67500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       56.87250            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       93.67500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       93.67500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      170.61750            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       93.67500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       93.67500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       56.87250            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      113.74500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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     LEU A    74                                                      
REMARK 465     ASP A    75                                                      
REMARK 465     ALA A    76                                                      
REMARK 465     THR A    77                                                      
REMARK 465     PRO A    78                                                      
REMARK 465     LEU A    79                                                      
REMARK 465     SER A    80                                                      
REMARK 465     SER A    81                                                      
REMARK 465     PRO A    82                                                      
REMARK 465     ASP A   503                                                      
REMARK 465     GLU A   504                                                      
REMARK 465     LEU B    74                                                      
REMARK 465     ASP B    75                                                      
REMARK 465     ALA B    76                                                      
REMARK 465     THR B    77                                                      
REMARK 465     PRO B    78                                                      
REMARK 465     LEU B    79                                                      
REMARK 465     SER B    80                                                      
REMARK 465     SER B    81                                                      
REMARK 465     PRO B    82                                                      
REMARK 465     ASP B   503                                                      
REMARK 465     GLU B   504                                                      
REMARK 465     LEU C    74                                                      
REMARK 465     ASP C    75                                                      
REMARK 465     ALA C    76                                                      
REMARK 465     THR C    77                                                      
REMARK 465     PRO C    78                                                      
REMARK 465     LEU C    79                                                      
REMARK 465     SER C    80                                                      
REMARK 465     SER C    81                                                      
REMARK 465     PRO C    82                                                      
REMARK 465     ASP C   503                                                      
REMARK 465     GLU C   504                                                      
REMARK 465     LEU D    74                                                      
REMARK 465     ASP D    75                                                      
REMARK 465     ALA D    76                                                      
REMARK 465     THR D    77                                                      
REMARK 465     PRO D    78                                                      
REMARK 465     LEU D    79                                                      
REMARK 465     SER D    80                                                      
REMARK 465     SER D    81                                                      
REMARK 465     PRO D    82                                                      
REMARK 465     ASP D   503                                                      
REMARK 465     GLU D   504                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A 110   CA  -  CB  -  SG  ANGL. DEV. =   6.8 DEGREES          
REMARK 500    CYS A 200   CA  -  CB  -  SG  ANGL. DEV. = -15.8 DEGREES          
REMARK 500    CYS D 110   CA  -  CB  -  SG  ANGL. DEV. =  11.0 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    GLU A 156     -154.37    -79.88                                   
REMARK 500    ILE A 159      -50.59     -6.82                                   
REMARK 500    ASN A 208       79.57   -107.41                                   
REMARK 500    SER A 218      -15.98   -147.93                                   
REMARK 500    SER A 251      -83.95   -102.16                                   
REMARK 500    ASN A 312       74.58     25.32                                   
REMARK 500    LYS A 335      -48.50   -130.46                                   
REMARK 500    CYS A 367       66.24   -154.08                                   
REMARK 500    ARG A 381      -72.33    -73.14                                   
REMARK 500    ARG A 388     -140.52   -128.10                                   
REMARK 500    THR A 403        1.61    -68.00                                   
REMARK 500    SER A 453      -69.09    -92.10                                   
REMARK 500    LEU A 485     -163.15   -121.21                                   
REMARK 500    ALA A 495      -60.39    -26.56                                   
REMARK 500    GLU B 156     -138.43    -78.46                                   
REMARK 500    ILE B 159      -59.17    -21.27                                   
REMARK 500    SER B 207       32.36    -82.85                                   
REMARK 500    CYS B 217      153.07    -44.51                                   
REMARK 500    SER B 218      -26.66   -142.31                                   
REMARK 500    SER B 251      -87.33   -120.12                                   
REMARK 500    TYR B 299       41.39     28.26                                   
REMARK 500    PHE B 302       56.06   -103.93                                   
REMARK 500    ARG B 314     -166.23    -70.62                                   
REMARK 500    ASN B 354        8.85    -67.24                                   
REMARK 500    CYS B 367       59.71   -170.53                                   
REMARK 500    ARG B 381      -71.58    -80.16                                   
REMARK 500    ARG B 388     -139.51   -123.55                                   
REMARK 500    SER B 453      -88.80    -72.92                                   
REMARK 500    CYS B 457       98.97   -162.54                                   
REMARK 500    LEU B 485     -158.54   -106.73                                   
REMARK 500    HIS B 499      137.45    -39.06                                   
REMARK 500    LEU C 116       51.22   -113.57                                   
REMARK 500    PRO C 133      158.90    -45.17                                   
REMARK 500    ILE C 159      -59.51    -19.55                                   
REMARK 500    THR C 178     -170.87   -174.91                                   
REMARK 500    SER C 218      -12.36   -141.81                                   
REMARK 500    ASN C 236       48.38     39.25                                   
REMARK 500    PRO C 248      134.72    -39.67                                   
REMARK 500    SER C 251      -82.61   -109.12                                   
REMARK 500    HIS C 255       63.36   -117.85                                   
REMARK 500    ASN C 312       73.98     15.57                                   
REMARK 500    LYS C 335      -58.38   -123.62                                   
REMARK 500    CYS C 367       62.60   -163.65                                   
REMARK 500    ARG C 381      -75.80    -70.50                                   
REMARK 500    ARG C 388     -144.19   -118.68                                   
REMARK 500    ASN C 390       67.39     36.41                                   
REMARK 500    THR C 403        2.57    -63.13                                   
REMARK 500    CYS C 457      100.32   -164.27                                   
REMARK 500    LEU C 485     -157.41   -118.36                                   
REMARK 500    ARG D 130     -166.69   -118.64                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      65 RAMACHANDRAN OUTLIERS.                        
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    ASN A 312        24.9      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 B 991        DISTANCE =  5.42 ANGSTROMS                       
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 A 901  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 115   SG                                                     
REMARK 620 2 CYS A 110   SG  100.5                                              
REMARK 620 3 CYS B 115   SG  110.8 103.8                                        
REMARK 620 4 CYS B 110   SG  101.0 125.3 114.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 902  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 115   SG                                                     
REMARK 620 2 CYS C 110   SG  106.4                                              
REMARK 620 3 CYS D 115   SG  113.8 104.0                                        
REMARK 620 4 CYS D 110   SG  105.0 122.7 105.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 550  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 200   SG                                                     
REMARK 620 2 HEM A 550   NA   87.7                                              
REMARK 620 3 HEM A 550   NB   94.4  90.5                                        
REMARK 620 4 HEM A 550   NC  104.9 167.0  91.4                                  
REMARK 620 5 HEM A 550   ND   91.4  87.7 173.9  89.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 550  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 200   SG                                                     
REMARK 620 2 HEM B 550   NA  102.5                                              
REMARK 620 3 HEM B 550   NB   89.2  85.8                                        
REMARK 620 4 HEM B 550   NC   99.6 157.6  90.5                                  
REMARK 620 5 HEM B 550   ND  104.8  89.5 165.9  88.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 550  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 200   SG                                                     
REMARK 620 2 HEM C 550   NA   92.9                                              
REMARK 620 3 HEM C 550   NB   92.9  89.6                                        
REMARK 620 4 HEM C 550   NC  101.9 165.2  89.5                                  
REMARK 620 5 HEM C 550   ND   97.1  90.2 170.0  88.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM D 550  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 200   SG                                                     
REMARK 620 2 HEM D 550   NA   95.4                                              
REMARK 620 3 HEM D 550   NB   88.5  91.0                                        
REMARK 620 4 HEM D 550   NC   95.1 169.5  89.3                                  
REMARK 620 5 HEM D 550   ND   93.3  89.0 178.2  90.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 910                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 920                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 930                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 911                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 921                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 912                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 922                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 913                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 923                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 902                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 550                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B A 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARG A 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 550                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARG B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 550                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B C 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARG C 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 550                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B D 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARG D 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 880                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 881                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 882                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 883                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2NSI   RELATED DB: PDB                                   
DBREF  1NSI A   74   504  UNP    P35228   NOS2A_HUMAN     74    504             
DBREF  1NSI B   74   504  UNP    P35228   NOS2A_HUMAN     74    504             
DBREF  1NSI C   74   504  UNP    P35228   NOS2A_HUMAN     74    504             
DBREF  1NSI D   74   504  UNP    P35228   NOS2A_HUMAN     74    504             
SEQRES   1 A  431  LEU ASP ALA THR PRO LEU SER SER PRO ARG HIS VAL ARG          
SEQRES   2 A  431  ILE LYS ASN TRP GLY SER GLY MET THR PHE GLN ASP THR          
SEQRES   3 A  431  LEU HIS HIS LYS ALA LYS GLY ILE LEU THR CYS ARG SER          
SEQRES   4 A  431  LYS SER CYS LEU GLY SER ILE MET THR PRO LYS SER LEU          
SEQRES   5 A  431  THR ARG GLY PRO ARG ASP LYS PRO THR PRO PRO ASP GLU          
SEQRES   6 A  431  LEU LEU PRO GLN ALA ILE GLU PHE VAL ASN GLN TYR TYR          
SEQRES   7 A  431  GLY SER PHE LYS GLU ALA LYS ILE GLU GLU HIS LEU ALA          
SEQRES   8 A  431  ARG VAL GLU ALA VAL THR LYS GLU ILE GLU THR THR GLY          
SEQRES   9 A  431  THR TYR GLN LEU THR GLY ASP GLU LEU ILE PHE ALA THR          
SEQRES  10 A  431  LYS GLN ALA TRP ARG ASN ALA PRO ARG CYS ILE GLY ARG          
SEQRES  11 A  431  ILE GLN TRP SER ASN LEU GLN VAL PHE ASP ALA ARG SER          
SEQRES  12 A  431  CYS SER THR ALA ARG GLU MET PHE GLU HIS ILE CYS ARG          
SEQRES  13 A  431  HIS VAL ARG TYR SER THR ASN ASN GLY ASN ILE ARG SER          
SEQRES  14 A  431  ALA ILE THR VAL PHE PRO GLN ARG SER ASP GLY LYS HIS          
SEQRES  15 A  431  ASP PHE ARG VAL TRP ASN ALA GLN LEU ILE ARG TYR ALA          
SEQRES  16 A  431  GLY TYR GLN MET PRO ASP GLY SER ILE ARG GLY ASP PRO          
SEQRES  17 A  431  ALA ASN VAL GLU PHE THR GLN LEU CYS ILE ASP LEU GLY          
SEQRES  18 A  431  TRP LYS PRO LYS TYR GLY ARG PHE ASP VAL VAL PRO LEU          
SEQRES  19 A  431  VAL LEU GLN ALA ASN GLY ARG ASP PRO GLU LEU PHE GLU          
SEQRES  20 A  431  ILE PRO PRO ASP LEU VAL LEU GLU VAL ALA MET GLU HIS          
SEQRES  21 A  431  PRO LYS TYR GLU TRP PHE ARG GLU LEU GLU LEU LYS TRP          
SEQRES  22 A  431  TYR ALA LEU PRO ALA VAL ALA ASN MET LEU LEU GLU VAL          
SEQRES  23 A  431  GLY GLY LEU GLU PHE PRO GLY CYS PRO PHE ASN GLY TRP          
SEQRES  24 A  431  TYR MET GLY THR GLU ILE GLY VAL ARG ASP PHE CYS ASP          
SEQRES  25 A  431  VAL GLN ARG TYR ASN ILE LEU GLU GLU VAL GLY ARG ARG          
SEQRES  26 A  431  MET GLY LEU GLU THR HIS LYS LEU ALA SER LEU TRP LYS          
SEQRES  27 A  431  ASP GLN ALA VAL VAL GLU ILE ASN ILE ALA VAL LEU HIS          
SEQRES  28 A  431  SER PHE GLN LYS GLN ASN VAL THR ILE MET ASP HIS HIS          
SEQRES  29 A  431  SER ALA ALA GLU SER PHE MET LYS TYR MET GLN ASN GLU          
SEQRES  30 A  431  TYR ARG SER ARG GLY GLY CYS PRO ALA ASP TRP ILE TRP          
SEQRES  31 A  431  LEU VAL PRO PRO MET SER GLY SER ILE THR PRO VAL PHE          
SEQRES  32 A  431  HIS GLN GLU MET LEU ASN TYR VAL LEU SER PRO PHE TYR          
SEQRES  33 A  431  TYR TYR GLN VAL GLU ALA TRP LYS THR HIS VAL TRP GLN          
SEQRES  34 A  431  ASP GLU                                                      
SEQRES   1 B  431  LEU ASP ALA THR PRO LEU SER SER PRO ARG HIS VAL ARG          
SEQRES   2 B  431  ILE LYS ASN TRP GLY SER GLY MET THR PHE GLN ASP THR          
SEQRES   3 B  431  LEU HIS HIS LYS ALA LYS GLY ILE LEU THR CYS ARG SER          
SEQRES   4 B  431  LYS SER CYS LEU GLY SER ILE MET THR PRO LYS SER LEU          
SEQRES   5 B  431  THR ARG GLY PRO ARG ASP LYS PRO THR PRO PRO ASP GLU          
SEQRES   6 B  431  LEU LEU PRO GLN ALA ILE GLU PHE VAL ASN GLN TYR TYR          
SEQRES   7 B  431  GLY SER PHE LYS GLU ALA LYS ILE GLU GLU HIS LEU ALA          
SEQRES   8 B  431  ARG VAL GLU ALA VAL THR LYS GLU ILE GLU THR THR GLY          
SEQRES   9 B  431  THR TYR GLN LEU THR GLY ASP GLU LEU ILE PHE ALA THR          
SEQRES  10 B  431  LYS GLN ALA TRP ARG ASN ALA PRO ARG CYS ILE GLY ARG          
SEQRES  11 B  431  ILE GLN TRP SER ASN LEU GLN VAL PHE ASP ALA ARG SER          
SEQRES  12 B  431  CYS SER THR ALA ARG GLU MET PHE GLU HIS ILE CYS ARG          
SEQRES  13 B  431  HIS VAL ARG TYR SER THR ASN ASN GLY ASN ILE ARG SER          
SEQRES  14 B  431  ALA ILE THR VAL PHE PRO GLN ARG SER ASP GLY LYS HIS          
SEQRES  15 B  431  ASP PHE ARG VAL TRP ASN ALA GLN LEU ILE ARG TYR ALA          
SEQRES  16 B  431  GLY TYR GLN MET PRO ASP GLY SER ILE ARG GLY ASP PRO          
SEQRES  17 B  431  ALA ASN VAL GLU PHE THR GLN LEU CYS ILE ASP LEU GLY          
SEQRES  18 B  431  TRP LYS PRO LYS TYR GLY ARG PHE ASP VAL VAL PRO LEU          
SEQRES  19 B  431  VAL LEU GLN ALA ASN GLY ARG ASP PRO GLU LEU PHE GLU          
SEQRES  20 B  431  ILE PRO PRO ASP LEU VAL LEU GLU VAL ALA MET GLU HIS          
SEQRES  21 B  431  PRO LYS TYR GLU TRP PHE ARG GLU LEU GLU LEU LYS TRP          
SEQRES  22 B  431  TYR ALA LEU PRO ALA VAL ALA ASN MET LEU LEU GLU VAL          
SEQRES  23 B  431  GLY GLY LEU GLU PHE PRO GLY CYS PRO PHE ASN GLY TRP          
SEQRES  24 B  431  TYR MET GLY THR GLU ILE GLY VAL ARG ASP PHE CYS ASP          
SEQRES  25 B  431  VAL GLN ARG TYR ASN ILE LEU GLU GLU VAL GLY ARG ARG          
SEQRES  26 B  431  MET GLY LEU GLU THR HIS LYS LEU ALA SER LEU TRP LYS          
SEQRES  27 B  431  ASP GLN ALA VAL VAL GLU ILE ASN ILE ALA VAL LEU HIS          
SEQRES  28 B  431  SER PHE GLN LYS GLN ASN VAL THR ILE MET ASP HIS HIS          
SEQRES  29 B  431  SER ALA ALA GLU SER PHE MET LYS TYR MET GLN ASN GLU          
SEQRES  30 B  431  TYR ARG SER ARG GLY GLY CYS PRO ALA ASP TRP ILE TRP          
SEQRES  31 B  431  LEU VAL PRO PRO MET SER GLY SER ILE THR PRO VAL PHE          
SEQRES  32 B  431  HIS GLN GLU MET LEU ASN TYR VAL LEU SER PRO PHE TYR          
SEQRES  33 B  431  TYR TYR GLN VAL GLU ALA TRP LYS THR HIS VAL TRP GLN          
SEQRES  34 B  431  ASP GLU                                                      
SEQRES   1 C  431  LEU ASP ALA THR PRO LEU SER SER PRO ARG HIS VAL ARG          
SEQRES   2 C  431  ILE LYS ASN TRP GLY SER GLY MET THR PHE GLN ASP THR          
SEQRES   3 C  431  LEU HIS HIS LYS ALA LYS GLY ILE LEU THR CYS ARG SER          
SEQRES   4 C  431  LYS SER CYS LEU GLY SER ILE MET THR PRO LYS SER LEU          
SEQRES   5 C  431  THR ARG GLY PRO ARG ASP LYS PRO THR PRO PRO ASP GLU          
SEQRES   6 C  431  LEU LEU PRO GLN ALA ILE GLU PHE VAL ASN GLN TYR TYR          
SEQRES   7 C  431  GLY SER PHE LYS GLU ALA LYS ILE GLU GLU HIS LEU ALA          
SEQRES   8 C  431  ARG VAL GLU ALA VAL THR LYS GLU ILE GLU THR THR GLY          
SEQRES   9 C  431  THR TYR GLN LEU THR GLY ASP GLU LEU ILE PHE ALA THR          
SEQRES  10 C  431  LYS GLN ALA TRP ARG ASN ALA PRO ARG CYS ILE GLY ARG          
SEQRES  11 C  431  ILE GLN TRP SER ASN LEU GLN VAL PHE ASP ALA ARG SER          
SEQRES  12 C  431  CYS SER THR ALA ARG GLU MET PHE GLU HIS ILE CYS ARG          
SEQRES  13 C  431  HIS VAL ARG TYR SER THR ASN ASN GLY ASN ILE ARG SER          
SEQRES  14 C  431  ALA ILE THR VAL PHE PRO GLN ARG SER ASP GLY LYS HIS          
SEQRES  15 C  431  ASP PHE ARG VAL TRP ASN ALA GLN LEU ILE ARG TYR ALA          
SEQRES  16 C  431  GLY TYR GLN MET PRO ASP GLY SER ILE ARG GLY ASP PRO          
SEQRES  17 C  431  ALA ASN VAL GLU PHE THR GLN LEU CYS ILE ASP LEU GLY          
SEQRES  18 C  431  TRP LYS PRO LYS TYR GLY ARG PHE ASP VAL VAL PRO LEU          
SEQRES  19 C  431  VAL LEU GLN ALA ASN GLY ARG ASP PRO GLU LEU PHE GLU          
SEQRES  20 C  431  ILE PRO PRO ASP LEU VAL LEU GLU VAL ALA MET GLU HIS          
SEQRES  21 C  431  PRO LYS TYR GLU TRP PHE ARG GLU LEU GLU LEU LYS TRP          
SEQRES  22 C  431  TYR ALA LEU PRO ALA VAL ALA ASN MET LEU LEU GLU VAL          
SEQRES  23 C  431  GLY GLY LEU GLU PHE PRO GLY CYS PRO PHE ASN GLY TRP          
SEQRES  24 C  431  TYR MET GLY THR GLU ILE GLY VAL ARG ASP PHE CYS ASP          
SEQRES  25 C  431  VAL GLN ARG TYR ASN ILE LEU GLU GLU VAL GLY ARG ARG          
SEQRES  26 C  431  MET GLY LEU GLU THR HIS LYS LEU ALA SER LEU TRP LYS          
SEQRES  27 C  431  ASP GLN ALA VAL VAL GLU ILE ASN ILE ALA VAL LEU HIS          
SEQRES  28 C  431  SER PHE GLN LYS GLN ASN VAL THR ILE MET ASP HIS HIS          
SEQRES  29 C  431  SER ALA ALA GLU SER PHE MET LYS TYR MET GLN ASN GLU          
SEQRES  30 C  431  TYR ARG SER ARG GLY GLY CYS PRO ALA ASP TRP ILE TRP          
SEQRES  31 C  431  LEU VAL PRO PRO MET SER GLY SER ILE THR PRO VAL PHE          
SEQRES  32 C  431  HIS GLN GLU MET LEU ASN TYR VAL LEU SER PRO PHE TYR          
SEQRES  33 C  431  TYR TYR GLN VAL GLU ALA TRP LYS THR HIS VAL TRP GLN          
SEQRES  34 C  431  ASP GLU                                                      
SEQRES   1 D  431  LEU ASP ALA THR PRO LEU SER SER PRO ARG HIS VAL ARG          
SEQRES   2 D  431  ILE LYS ASN TRP GLY SER GLY MET THR PHE GLN ASP THR          
SEQRES   3 D  431  LEU HIS HIS LYS ALA LYS GLY ILE LEU THR CYS ARG SER          
SEQRES   4 D  431  LYS SER CYS LEU GLY SER ILE MET THR PRO LYS SER LEU          
SEQRES   5 D  431  THR ARG GLY PRO ARG ASP LYS PRO THR PRO PRO ASP GLU          
SEQRES   6 D  431  LEU LEU PRO GLN ALA ILE GLU PHE VAL ASN GLN TYR TYR          
SEQRES   7 D  431  GLY SER PHE LYS GLU ALA LYS ILE GLU GLU HIS LEU ALA          
SEQRES   8 D  431  ARG VAL GLU ALA VAL THR LYS GLU ILE GLU THR THR GLY          
SEQRES   9 D  431  THR TYR GLN LEU THR GLY ASP GLU LEU ILE PHE ALA THR          
SEQRES  10 D  431  LYS GLN ALA TRP ARG ASN ALA PRO ARG CYS ILE GLY ARG          
SEQRES  11 D  431  ILE GLN TRP SER ASN LEU GLN VAL PHE ASP ALA ARG SER          
SEQRES  12 D  431  CYS SER THR ALA ARG GLU MET PHE GLU HIS ILE CYS ARG          
SEQRES  13 D  431  HIS VAL ARG TYR SER THR ASN ASN GLY ASN ILE ARG SER          
SEQRES  14 D  431  ALA ILE THR VAL PHE PRO GLN ARG SER ASP GLY LYS HIS          
SEQRES  15 D  431  ASP PHE ARG VAL TRP ASN ALA GLN LEU ILE ARG TYR ALA          
SEQRES  16 D  431  GLY TYR GLN MET PRO ASP GLY SER ILE ARG GLY ASP PRO          
SEQRES  17 D  431  ALA ASN VAL GLU PHE THR GLN LEU CYS ILE ASP LEU GLY          
SEQRES  18 D  431  TRP LYS PRO LYS TYR GLY ARG PHE ASP VAL VAL PRO LEU          
SEQRES  19 D  431  VAL LEU GLN ALA ASN GLY ARG ASP PRO GLU LEU PHE GLU          
SEQRES  20 D  431  ILE PRO PRO ASP LEU VAL LEU GLU VAL ALA MET GLU HIS          
SEQRES  21 D  431  PRO LYS TYR GLU TRP PHE ARG GLU LEU GLU LEU LYS TRP          
SEQRES  22 D  431  TYR ALA LEU PRO ALA VAL ALA ASN MET LEU LEU GLU VAL          
SEQRES  23 D  431  GLY GLY LEU GLU PHE PRO GLY CYS PRO PHE ASN GLY TRP          
SEQRES  24 D  431  TYR MET GLY THR GLU ILE GLY VAL ARG ASP PHE CYS ASP          
SEQRES  25 D  431  VAL GLN ARG TYR ASN ILE LEU GLU GLU VAL GLY ARG ARG          
SEQRES  26 D  431  MET GLY LEU GLU THR HIS LYS LEU ALA SER LEU TRP LYS          
SEQRES  27 D  431  ASP GLN ALA VAL VAL GLU ILE ASN ILE ALA VAL LEU HIS          
SEQRES  28 D  431  SER PHE GLN LYS GLN ASN VAL THR ILE MET ASP HIS HIS          
SEQRES  29 D  431  SER ALA ALA GLU SER PHE MET LYS TYR MET GLN ASN GLU          
SEQRES  30 D  431  TYR ARG SER ARG GLY GLY CYS PRO ALA ASP TRP ILE TRP          
SEQRES  31 D  431  LEU VAL PRO PRO MET SER GLY SER ILE THR PRO VAL PHE          
SEQRES  32 D  431  HIS GLN GLU MET LEU ASN TYR VAL LEU SER PRO PHE TYR          
SEQRES  33 D  431  TYR TYR GLN VAL GLU ALA TRP LYS THR HIS VAL TRP GLN          
SEQRES  34 D  431  ASP GLU                                                      
HET    SO4  A 910       5                                                       
HET    SO4  A 920       5                                                       
HET    SO4  A 930       5                                                       
HET    SO4  B 911       5                                                       
HET    SO4  B 921       5                                                       
HET    SO4  C 912       5                                                       
HET    SO4  C 922       5                                                       
HET    SO4  D 913       5                                                       
HET    SO4  D 923       5                                                       
HET     ZN  A 901       1                                                       
HET     ZN  C 902       1                                                       
HET    HEM  A 550      43                                                       
HET    H4B  A 600      17                                                       
HET    ARG  A 700      12                                                       
HET    HEM  B 550      43                                                       
HET    H4B  B 601      17                                                       
HET    ARG  B 701      12                                                       
HET    HEM  C 550      43                                                       
HET    H4B  C 602      17                                                       
HET    ARG  C 702      12                                                       
HET    HEM  D 550      43                                                       
HET    H4B  D 603      17                                                       
HET    ARG  D 703      12                                                       
HET    GOL  A 880       6                                                       
HET    GOL  B 881       6                                                       
HET    GOL  C 882       6                                                       
HET    GOL  D 883       6                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      ZN ZINC ION                                                         
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     H4B 5,6,7,8-TETRAHYDROBIOPTERIN                                      
HETNAM     ARG ARGININE                                                         
HETNAM     GOL GLYCEROL                                                         
HETSYN     HEM HEME                                                             
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  SO4    9(O4 S 2-)                                                   
FORMUL  14   ZN    2(ZN 2+)                                                     
FORMUL  16  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL  17  H4B    4(C9 H15 N5 O3)                                              
FORMUL  18  ARG    4(C6 H15 N4 O2 1+)                                           
FORMUL  28  GOL    4(C3 H8 O3)                                                  
FORMUL  32  HOH   *295(H2 O)                                                    
HELIX    1   1 LEU A  100  HIS A  102  5                                   3    
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  GLN A  205  5                                   3    
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 ARG A  381  CYS A  384  1                                   4    
HELIX   13  13 LEU A  392  ARG A  398  1                                   7    
HELIX   14  14 LEU A  406  SER A  408  5                                   3    
HELIX   15  15 TRP A  410  LYS A  428  1                                  19    
HELIX   16  16 HIS A  436  SER A  453  1                                  18    
HELIX   17  17 TRP A  461  LEU A  464  1                                   4    
HELIX   18  18 GLY A  470  ILE A  472  5                                   3    
HELIX   19  19 ALA A  495  THR A  498  1                                   4    
HELIX   20  20 LEU B  100  LYS B  103  5                                   4    
HELIX   21  21 LYS B  123  LEU B  125  5                                   3    
HELIX   22  22 PRO B  136  SER B  153  1                                  18    
HELIX   23  23 ILE B  159  THR B  176  1                                  18    
HELIX   24  24 GLY B  183  ARG B  195  1                                  13    
HELIX   25  25 ARG B  203  GLN B  205  5                                   3    
HELIX   26  26 ALA B  220  GLY B  238  1                                  19    
HELIX   27  27 PRO B  281  ASP B  292  5                                  12    
HELIX   28  28 PRO B  323  LEU B  325  5                                   3    
HELIX   29  29 GLU B  337  LEU B  342  5                                   6    
HELIX   30  30 GLY B  375  GLY B  379  1                                   5    
HELIX   31  31 ARG B  381  CYS B  384  1                                   4    
HELIX   32  32 LEU B  392  MET B  399  1                                   8    
HELIX   33  33 LEU B  406  SER B  408  5                                   3    
HELIX   34  34 TRP B  410  LYS B  428  1                                  19    
HELIX   35  35 HIS B  436  SER B  453  1                                  18    
HELIX   36  36 TRP B  461  LEU B  464  1                                   4    
HELIX   37  37 GLY B  470  ILE B  472  5                                   3    
HELIX   38  38 PRO B  474  HIS B  477  5                                   4    
HELIX   39  39 ALA B  495  LYS B  497  5                                   3    
HELIX   40  40 LEU C  100  LYS C  103  5                                   4    
HELIX   41  41 LYS C  123  LEU C  125  5                                   3    
HELIX   42  42 PRO C  136  SER C  153  1                                  18    
HELIX   43  43 ILE C  159  THR C  176  1                                  18    
HELIX   44  44 GLY C  183  ARG C  195  1                                  13    
HELIX   45  45 ARG C  203  GLN C  205  5                                   3    
HELIX   46  46 ALA C  220  GLY C  238  1                                  19    
HELIX   47  47 PRO C  281  ASP C  292  5                                  12    
HELIX   48  48 PRO C  323  LEU C  325  5                                   3    
HELIX   49  49 GLU C  337  LEU C  342  5                                   6    
HELIX   50  50 GLY C  375  GLY C  379  1                                   5    
HELIX   51  51 ARG C  381  CYS C  384  1                                   4    
HELIX   52  52 LEU C  392  ARG C  398  1                                   7    
HELIX   53  53 LEU C  406  SER C  408  5                                   3    
HELIX   54  54 TRP C  410  LYS C  428  1                                  19    
HELIX   55  55 HIS C  436  SER C  453  1                                  18    
HELIX   56  56 TRP C  461  LEU C  464  1                                   4    
HELIX   57  57 GLY C  470  ILE C  472  5                                   3    
HELIX   58  58 ALA C  495  LYS C  497  5                                   3    
HELIX   59  59 LEU D  100  LYS D  103  5                                   4    
HELIX   60  60 LYS D  123  LEU D  125  5                                   3    
HELIX   61  61 PRO D  136  GLY D  152  1                                  17    
HELIX   62  62 ILE D  159  THR D  175  1                                  17    
HELIX   63  63 GLY D  183  ARG D  195  1                                  13    
HELIX   64  64 ARG D  203  GLN D  205  5                                   3    
HELIX   65  65 ALA D  220  GLY D  238  1                                  19    
HELIX   66  66 PRO D  281  ASP D  292  5                                  12    
HELIX   67  67 GLU D  337  LEU D  342  5                                   6    
HELIX   68  68 GLY D  375  GLY D  379  1                                   5    
HELIX   69  69 ARG D  381  CYS D  384  1                                   4    
HELIX   70  70 LEU D  392  ARG D  398  1                                   7    
HELIX   71  71 LEU D  406  SER D  408  5                                   3    
HELIX   72  72 TRP D  410  LYS D  428  1                                  19    
HELIX   73  73 HIS D  436  SER D  453  1                                  18    
HELIX   74  74 TRP D  461  LEU D  464  1                                   4    
HELIX   75  75 GLY D  470  ILE D  472  5                                   3    
HELIX   76  76 PRO D  474  HIS D  477  1                                   4    
HELIX   77  77 ALA D  495  LYS D  497  5                                   3    
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 3 PHE A 488  TYR A 490  0                                        
SHEET    2   F 3 LEU A 356  VAL A 359 -1  N  GLU A 358   O  PHE A 488           
SHEET    3   F 3 LEU A 362  PHE A 364 -1  N  PHE A 364   O  LEU A 357           
SHEET    1   G 2 VAL B  85  LYS B  88  0                                        
SHEET    2   G 2 THR B  95  ASP B  98 -1  N  ASP B  98   O  VAL B  85           
SHEET    1   H 2 GLN B 210  ALA B 214  0                                        
SHEET    2   H 2 ALA B 243  PHE B 247  1  N  ILE B 244   O  GLN B 210           
SHEET    1   I 2 GLY B 269  GLN B 271  0                                        
SHEET    2   I 2 ILE B 277  GLY B 279 -1  N  ARG B 278   O  TYR B 270           
SHEET    1   J 2 LEU B 307  LEU B 309  0                                        
SHEET    2   J 2 GLU B 317  PHE B 319 -1  N  PHE B 319   O  LEU B 307           
SHEET    1   K 2 GLU B 328  ALA B 330  0                                        
SHEET    2   K 2 LYS B 345  TYR B 347 -1  N  TRP B 346   O  VAL B 329           
SHEET    1   L 3 PHE B 488  TYR B 490  0                                        
SHEET    2   L 3 LEU B 356  VAL B 359 -1  N  GLU B 358   O  PHE B 488           
SHEET    3   L 3 LEU B 362  PHE B 364 -1  N  PHE B 364   O  LEU B 357           
SHEET    1   M 2 VAL C  85  LYS C  88  0                                        
SHEET    2   M 2 THR C  95  ASP C  98 -1  N  ASP C  98   O  VAL C  85           
SHEET    1   N 2 GLN C 210  ALA C 214  0                                        
SHEET    2   N 2 ALA C 243  PHE C 247  1  N  ILE C 244   O  GLN C 210           
SHEET    1   O 2 GLY C 269  GLN C 271  0                                        
SHEET    2   O 2 ILE C 277  GLY C 279 -1  N  ARG C 278   O  TYR C 270           
SHEET    1   P 2 LEU C 307  LEU C 309  0                                        
SHEET    2   P 2 GLU C 317  PHE C 319 -1  N  PHE C 319   O  LEU C 307           
SHEET    1   Q 2 GLU C 328  ALA C 330  0                                        
SHEET    2   Q 2 LYS C 345  TYR C 347 -1  N  TRP C 346   O  VAL C 329           
SHEET    1   R 2 PRO C 350  VAL C 352  0                                        
SHEET    2   R 2 PHE C 369  GLY C 371 -1  N  GLY C 371   O  PRO C 350           
SHEET    1   S 3 PHE C 488  TYR C 490  0                                        
SHEET    2   S 3 LEU C 356  VAL C 359 -1  N  GLU C 358   O  PHE C 488           
SHEET    3   S 3 LEU C 362  PHE C 364 -1  N  PHE C 364   O  LEU C 357           
SHEET    1   T 2 VAL D  85  LYS D  88  0                                        
SHEET    2   T 2 THR D  95  ASP D  98 -1  N  ASP D  98   O  VAL D  85           
SHEET    1   U 4 GLN D 210  ALA D 214  0                                        
SHEET    2   U 4 ALA D 243  PHE D 247  1  N  ILE D 244   O  GLN D 210           
SHEET    3   U 4 CYS D 367  TRP D 372 -1  N  ASN D 370   O  ALA D 243           
SHEET    4   U 4 LEU D 349  VAL D 352 -1  N  VAL D 352   O  PHE D 369           
SHEET    1   V 2 GLY D 269  GLN D 271  0                                        
SHEET    2   V 2 ILE D 277  GLY D 279 -1  N  ARG D 278   O  TYR D 270           
SHEET    1   W 2 LEU D 307  LEU D 309  0                                        
SHEET    2   W 2 GLU D 317  PHE D 319 -1  N  PHE D 319   O  LEU D 307           
SHEET    1   X 2 GLU D 328  ALA D 330  0                                        
SHEET    2   X 2 LYS D 345  TYR D 347 -1  N  TRP D 346   O  VAL D 329           
SHEET    1   Y 2 LEU D 356  GLU D 358  0                                        
SHEET    2   Y 2 PHE D 488  TYR D 490 -1  N  TYR D 490   O  LEU D 356           
LINK         SG  CYS A 115                ZN    ZN A 901     1555   1555  2.29  
LINK         SG  CYS A 110                ZN    ZN A 901     1555   1555  2.32  
LINK         SG  CYS B 115                ZN    ZN A 901     1555   1555  2.32  
LINK         SG  CYS B 110                ZN    ZN A 901     1555   1555  2.28  
LINK         SG  CYS C 115                ZN    ZN C 902     1555   1555  2.32  
LINK         SG  CYS C 110                ZN    ZN C 902     1555   1555  2.33  
LINK         SG  CYS D 115                ZN    ZN C 902     1555   1555  2.32  
LINK         SG  CYS D 110                ZN    ZN C 902     1555   1555  2.36  
LINK        FE   HEM A 550                 SG  CYS A 200     1555   1555  2.21  
LINK        FE   HEM B 550                 SG  CYS B 200     1555   1555  2.20  
LINK        FE   HEM C 550                 SG  CYS C 200     1555   1555  2.22  
LINK        FE   HEM D 550                 SG  CYS D 200     1555   1555  2.24  
CISPEP   1 SER A  486    PRO A  487          0         1.13                     
CISPEP   2 SER B  486    PRO B  487          0        -0.43                     
CISPEP   3 SER C  486    PRO C  487          0         0.68                     
CISPEP   4 SER D  486    PRO D  487          0        -0.17                     
SITE     1 AC1  4 ARG A 301  HOH A1015  HOH A1016  HOH A1017                    
SITE     1 AC2  5 LYS A 335  TYR A 336  GLU A 337  TRP A 338                    
SITE     2 AC2  5 ARG D 340                                                     
SITE     1 AC3  4 ASN A 236  ASN A 239  ASN C 236  ASN C 239                    
SITE     1 AC4  3 GLY B 300  ARG B 301  HOH B 973                               
SITE     1 AC5  5 LYS B 335  GLU B 337  TRP B 338  TYR D 336                    
SITE     2 AC5  5 HOH D 960                                                     
SITE     1 AC6  1 ARG C 301                                                     
SITE     1 AC7  6 ARG B 340  LYS C 335  TYR C 336  GLU C 337                    
SITE     2 AC7  6 TRP C 338  HOH C 977                                          
SITE     1 AC8  2 ARG D 301  HOH D 961                                          
SITE     1 AC9  5 LYS D 335  TYR D 336  GLU D 337  TRP D 338                    
SITE     2 AC9  5 HOH D 925                                                     
SITE     1 BC1  4 CYS A 110  CYS A 115  CYS B 110  CYS B 115                    
SITE     1 BC2  4 CYS C 110  CYS C 115  CYS D 110  CYS D 115                    
SITE     1 BC3 15 TRP A 194  ALA A 197  ARG A 199  CYS A 200                    
SITE     2 BC3 15 SER A 242  PHE A 369  ASN A 370  GLY A 371                    
SITE     3 BC3 15 TRP A 372  TRP A 463  TYR A 491  H4B A 600                    
SITE     4 BC3 15 ARG A 700  HOH A 943  HOH A 953                               
SITE     1 BC4 12 SER A 118  ARG A 381  ILE A 462  TRP A 463                    
SITE     2 BC4 12 HEM A 550  HOH A 964  HOH A 999  TRP B 461                    
SITE     3 BC4 12 PHE B 476  HIS B 477  GLN B 478  GLU B 479                    
SITE     1 BC5  8 GLN A 263  TYR A 347  PRO A 350  TRP A 372                    
SITE     2 BC5  8 TYR A 373  GLU A 377  ASP A 382  HEM A 550                    
SITE     1 BC6 14 TRP B 194  ARG B 199  CYS B 200  PHE B 369                    
SITE     2 BC6 14 ASN B 370  TRP B 372  GLU B 377  TRP B 463                    
SITE     3 BC6 14 TYR B 489  TYR B 491  H4B B 601  ARG B 701                    
SITE     4 BC6 14 HOH B 932  HOH B 995                                          
SITE     1 BC7 14 TRP A 461  PHE A 476  HIS A 477  GLN A 478                    
SITE     2 BC7 14 SER B 118  ARG B 381  ILE B 462  TRP B 463                    
SITE     3 BC7 14 HEM B 550  HOH B 928  HOH B 932  HOH B 986                    
SITE     4 BC7 14 HOH B 987  HOH B 997                                          
SITE     1 BC8  8 GLN B 263  TYR B 347  PRO B 350  TRP B 372                    
SITE     2 BC8  8 TYR B 373  GLU B 377  ASP B 382  HEM B 550                    
SITE     1 BC9 14 TRP C 194  ARG C 199  CYS C 200  SER C 242                    
SITE     2 BC9 14 PHE C 369  ASN C 370  GLY C 371  TRP C 372                    
SITE     3 BC9 14 GLU C 377  TRP C 463  TYR C 491  H4B C 602                    
SITE     4 BC9 14 ARG C 702  HOH C 934                                          
SITE     1 CC1 13 SER C 118  ARG C 381  ILE C 462  TRP C 463                    
SITE     2 CC1 13 HEM C 550  HOH C 931  HOH C 934  HOH C 960                    
SITE     3 CC1 13 TRP D 461  PHE D 476  HIS D 477  GLN D 478                    
SITE     4 CC1 13 GLU D 479                                                     
SITE     1 CC2  7 GLN C 263  TYR C 347  TRP C 372  TYR C 373                    
SITE     2 CC2  7 GLU C 377  ASP C 382  HEM C 550                               
SITE     1 CC3 11 TRP D 194  ALA D 197  CYS D 200  PHE D 369                    
SITE     2 CC3 11 ASN D 370  TRP D 372  GLU D 377  TRP D 463                    
SITE     3 CC3 11 TYR D 491  H4B D 603  ARG D 703                               
SITE     1 CC4 12 TRP C 461  PHE C 476  HIS C 477  GLN C 478                    
SITE     2 CC4 12 GLU C 479  SER D 118  ARG D 381  ILE D 462                    
SITE     3 CC4 12 TRP D 463  HEM D 550  HOH D 936  HOH D 959                    
SITE     1 CC5  9 GLN D 263  TYR D 347  PRO D 350  TRP D 372                    
SITE     2 CC5  9 TYR D 373  GLU D 377  ASP D 382  HEM D 550                    
SITE     3 CC5  9 HOH D 944                                                     
SITE     1 CC6  5 ASP A 256  ARG A 258  GLN A 310  THR A 498                    
SITE     2 CC6  5 HIS A 499                                                     
SITE     1 CC7  5 ASP B 256  ARG B 258  GLN B 310  THR B 498                    
SITE     2 CC7  5 HIS B 499                                                     
SITE     1 CC8  6 ASP C 256  ARG C 258  GLN C 310  ALA C 495                    
SITE     2 CC8  6 THR C 498  HIS C 499                                          
SITE     1 CC9  5 ASP D 256  ARG D 258  GLN D 310  THR D 498                    
SITE     2 CC9  5 HIS D 499                                                     
CRYST1  187.350  187.350  227.490  90.00  90.00  90.00 P 43 21 2    32          
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      0.005338  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005338  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004396        0.00000                         
MTRIX1   1 -0.462454 -0.877798  0.124929       74.55360    1                    
MTRIX2   1 -0.880955  0.438969 -0.176704       55.41630    1                    
MTRIX3   1  0.100271 -0.191774 -0.976304       76.43760    1                    
MTRIX1   2 -0.873852  0.486131 -0.007712       47.98690    1                    
MTRIX2   2 -0.486179 -0.873599  0.021323       81.36220    1                    
MTRIX3   2  0.003629  0.022383  0.999743       40.33540    1                    
MTRIX1   3 -0.011838  0.983449 -0.180800        8.67220    1                    
MTRIX2   3  0.995748  0.028115  0.087728       -1.27190    1                    
MTRIX3   3  0.091359 -0.178993 -0.979599      117.70460    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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