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Database: PDB
Entry: 2NSI
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Original site: 2NSI 
HEADER    OXIDOREDUCTASE                          11-JAN-99   2NSI              
TITLE     HUMAN INDUCIBLE NITRIC OXIDE SYNTHASE, ZN-FREE, SEITU                 
TITLE    2 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,           
AUTHOR   2 M.WHITLOW,T.L.POULOS                                                 
REVDAT   3   24-FEB-09 2NSI    1       VERSN                                    
REVDAT   2   01-APR-03 2NSI    1       JRNL                                     
REVDAT   1   07-JAN-00 2NSI    0                                                
JRNL        AUTH   H.LI,C.S.RAMAN,C.B.GLASER,E.BLASKO,T.A.YOUNG,                
JRNL        AUTH 2 J.F.PARKINSON,M.WHITLOW,T.L.POULOS                           
JRNL        TITL   CRYSTAL STRUCTURES OF ZINC-FREE AND -BOUND HEME              
JRNL        TITL 2 DOMAIN OF HUMAN INDUCIBLE NITRIC-OXIDE SYNTHASE.             
JRNL        TITL 3 IMPLICATIONS FOR DIMER STABILITY AND COMPARISON              
JRNL        TITL 4 WITH ENDOTHELIAL NITRIC-OXIDE 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,              
REMARK   1  AUTH 2 D.J.STUEHR,J.A.TAINER                                        
REMARK   1  TITL   STRUCTURE OF NITRIC OXIDE SYNTHASE OXYGENASE DIMER           
REMARK   1  TITL 2 WITH 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,                
REMARK   1  AUTH 2 E.D.GETZOFF,D.J.STUEHR,J.A.TAINER                            
REMARK   1  TITL   THE STRUCTURE OF NITRIC OXIDE SYNTHASE OXYGENASE             
REMARK   1  TITL 2 DOMAIN AND 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,                
REMARK   1  AUTH 2 T.L.POULOS                                                   
REMARK   1  TITL   CRYSTAL STRUCTURE OF CONSTITUTIVE ENDOTHELIAL                
REMARK   1  TITL 2 NITRIC OXIDE SYNTHASE: A PARADIGM FOR PTERIN                 
REMARK   1  TITL 3 FUNCTION INVOLVING A NOVEL METAL CENTER                      
REMARK   1  REF    CELL(CAMBRIDGE,MASS.)         V.  95   939 1998              
REMARK   1  REFN                   ISSN 0092-8674                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 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) : 3.00                           
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)   (%) : 80.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 70704                          
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) : 0.214                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3614                            
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) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.14                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 57.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5920                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2990                       
REMARK   3   BIN FREE R VALUE                    : 0.3190                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 346                          
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          : 309                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 66.80                          
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) : 1.18                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.23                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.24                            
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 : RESIDUES 83-502 OF EACH SUBUNIT                         
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 2NSI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUL-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB007220.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUN-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               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08                               
REMARK 200  MONOCHROMATOR                  : YES                                
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 82161                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
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     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.69900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
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      115.08000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       94.18500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       94.18500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      172.62000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       94.18500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       94.18500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       57.54000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       94.18500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       94.18500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      172.62000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       94.18500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       94.18500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       57.54000            
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      115.08000            
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                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10270 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 32730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -115.0 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                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10440 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 32760 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -120.0 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     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: 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    ARG A 111     -169.42   -162.78                                   
REMARK 500    SER A 112       41.47    -90.90                                   
REMARK 500    LYS A 113       -8.75   -163.12                                   
REMARK 500    SER A 114       95.77    178.82                                   
REMARK 500    LEU A 116       42.11    -77.02                                   
REMARK 500    SER A 118        4.17    125.83                                   
REMARK 500    LYS A 155      -70.49    -60.55                                   
REMARK 500    LYS A 158       66.71   -103.35                                   
REMARK 500    GLU A 160      -71.08    -57.79                                   
REMARK 500    ARG A 203       -7.25    -59.46                                   
REMARK 500    SER A 218      -18.56   -142.76                                   
REMARK 500    SER A 251      -89.32   -103.44                                   
REMARK 500    HIS A 255       51.44   -109.58                                   
REMARK 500    ASN A 354       11.61    -68.40                                   
REMARK 500    CYS A 367       81.76   -158.56                                   
REMARK 500    ARG A 388     -138.45   -112.85                                   
REMARK 500    ASN A 390       81.73     38.52                                   
REMARK 500    THR A 403        5.80    -63.12                                   
REMARK 500    CYS A 457      103.32   -164.26                                   
REMARK 500    LEU A 485     -159.49   -114.79                                   
REMARK 500    ARG B 111     -169.36   -163.55                                   
REMARK 500    SER B 112       41.57    -90.66                                   
REMARK 500    LYS B 113       -8.17   -163.47                                   
REMARK 500    SER B 114       95.70    177.83                                   
REMARK 500    LEU B 116       41.86    -77.44                                   
REMARK 500    SER B 118        4.33    126.33                                   
REMARK 500    LYS B 158       67.08   -104.74                                   
REMARK 500    GLU B 160      -70.21    -57.95                                   
REMARK 500    ARG B 203       -6.70    -58.67                                   
REMARK 500    SER B 218      -17.87   -143.83                                   
REMARK 500    SER B 251      -89.77   -103.70                                   
REMARK 500    HIS B 255       51.89   -110.34                                   
REMARK 500    ASN B 354       12.09    -67.86                                   
REMARK 500    CYS B 367       80.39   -159.06                                   
REMARK 500    ARG B 388     -138.36   -111.99                                   
REMARK 500    ASN B 390       82.31     37.52                                   
REMARK 500    THR B 403        6.95    -63.62                                   
REMARK 500    CYS B 457      102.49   -165.37                                   
REMARK 500    LEU B 485     -158.78   -114.65                                   
REMARK 500    ARG C 111     -168.40   -163.07                                   
REMARK 500    SER C 112       41.74    -91.59                                   
REMARK 500    LYS C 113       -9.48   -162.98                                   
REMARK 500    SER C 114       96.16    179.51                                   
REMARK 500    LEU C 116       41.89    -76.08                                   
REMARK 500    SER C 118        3.19    126.41                                   
REMARK 500    LYS C 155      -70.89    -61.20                                   
REMARK 500    LYS C 158       66.45   -103.66                                   
REMARK 500    ARG C 203       -6.09    -58.71                                   
REMARK 500    SER C 218      -18.29   -142.69                                   
REMARK 500    SER C 251      -89.85   -103.99                                   
REMARK 500    HIS C 255       51.58   -109.32                                   
REMARK 500    ASN C 354       14.23    -68.69                                   
REMARK 500    CYS C 367       82.85   -157.61                                   
REMARK 500    ARG C 388     -136.58   -113.59                                   
REMARK 500    ASN C 390       80.41     39.03                                   
REMARK 500    THR C 403        5.87    -63.96                                   
REMARK 500    CYS C 457      103.74   -164.90                                   
REMARK 500    LEU C 485     -158.36   -115.16                                   
REMARK 500    ARG D 111     -169.19   -162.27                                   
REMARK 500    SER D 112       41.19    -91.29                                   
REMARK 500    LYS D 113       -8.92   -162.17                                   
REMARK 500    SER D 114       95.21    178.86                                   
REMARK 500    LEU D 116       42.34    -76.84                                   
REMARK 500    SER D 118        3.97    126.28                                   
REMARK 500    LYS D 155      -70.66    -59.86                                   
REMARK 500    LYS D 158       66.31   -101.85                                   
REMARK 500    GLU D 160      -71.09    -58.04                                   
REMARK 500    SER D 218      -18.87   -142.72                                   
REMARK 500    SER D 251      -89.57   -102.56                                   
REMARK 500    HIS D 255       52.06   -109.34                                   
REMARK 500    ASN D 354        9.75    -67.73                                   
REMARK 500    CYS D 367       80.28   -159.83                                   
REMARK 500    ARG D 388     -139.31   -113.43                                   
REMARK 500    ASN D 390       82.54     38.73                                   
REMARK 500    THR D 403        5.58    -63.75                                   
REMARK 500    CYS D 457      102.87   -164.69                                   
REMARK 500    LEU D 485     -160.38   -114.01                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 910                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 920                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 930                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 911                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 921                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 912                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 922                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 913                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 923                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 550                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B A 600                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ITU A 800                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 550                 
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B B 601                 
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ITU B 801                 
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 550                 
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B C 602                 
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ITU C 802                 
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 550                 
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B D 603                 
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ITU D 803                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1NSI   RELATED DB: PDB                                   
DBREF  2NSI A   74   504  UNP    P35228   NOS2A_HUMAN     74    504             
DBREF  2NSI B   74   504  UNP    P35228   NOS2A_HUMAN     74    504             
DBREF  2NSI C   74   504  UNP    P35228   NOS2A_HUMAN     74    504             
DBREF  2NSI 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    HEM  A 550      43                                                       
HET    H4B  A 600      17                                                       
HET    ITU  A 800       6                                                       
HET    HEM  B 550      43                                                       
HET    H4B  B 601      17                                                       
HET    ITU  B 801       6                                                       
HET    HEM  C 550      43                                                       
HET    H4B  C 602      17                                                       
HET    ITU  C 802       6                                                       
HET    HEM  D 550      43                                                       
HET    H4B  D 603      17                                                       
HET    ITU  D 803       6                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     H4B 5,6,7,8-TETRAHYDROBIOPTERIN                                      
HETNAM     ITU ETHYLISOTHIOUREA                                                 
HETSYN     HEM HEME                                                             
FORMUL   5  SO4    9(O4 S 2-)                                                   
FORMUL  14  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL  15  H4B    4(C9 H15 N5 O3)                                              
FORMUL  16  ITU    4(C3 H8 N2 S)                                                
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 PRO A  474  HIS A  477  1                                   4    
HELIX   20  20 ALA A  495  THR A  498  1                                   4    
HELIX   21  21 LEU B  100  HIS B  102  5                                   3    
HELIX   22  22 LYS B  123  LEU B  125  5                                   3    
HELIX   23  23 PRO B  136  SER B  153  1                                  18    
HELIX   24  24 ILE B  159  THR B  176  1                                  18    
HELIX   25  25 GLY B  183  ARG B  195  1                                  13    
HELIX   26  26 ARG B  203  GLN B  205  5                                   3    
HELIX   27  27 ALA B  220  GLY B  238  1                                  19    
HELIX   28  28 PRO B  281  ASP B  292  5                                  12    
HELIX   29  29 PRO B  323  LEU B  325  5                                   3    
HELIX   30  30 GLU B  337  LEU B  342  5                                   6    
HELIX   31  31 GLY B  375  GLY B  379  1                                   5    
HELIX   32  32 ARG B  381  CYS B  384  1                                   4    
HELIX   33  33 LEU B  392  ARG B  398  1                                   7    
HELIX   34  34 LEU B  406  SER B  408  5                                   3    
HELIX   35  35 TRP B  410  LYS B  428  1                                  19    
HELIX   36  36 HIS B  436  SER B  453  1                                  18    
HELIX   37  37 TRP B  461  LEU B  464  1                                   4    
HELIX   38  38 GLY B  470  ILE B  472  5                                   3    
HELIX   39  39 PRO B  474  HIS B  477  1                                   4    
HELIX   40  40 ALA B  495  THR B  498  1                                   4    
HELIX   41  41 LEU C  100  HIS C  102  5                                   3    
HELIX   42  42 LYS C  123  LEU C  125  5                                   3    
HELIX   43  43 PRO C  136  SER C  153  1                                  18    
HELIX   44  44 ILE C  159  THR C  176  1                                  18    
HELIX   45  45 GLY C  183  ARG C  195  1                                  13    
HELIX   46  46 ARG C  203  GLN C  205  5                                   3    
HELIX   47  47 ALA C  220  GLY C  238  1                                  19    
HELIX   48  48 PRO C  281  ASP C  292  5                                  12    
HELIX   49  49 PRO C  323  LEU C  325  5                                   3    
HELIX   50  50 GLU C  337  LEU C  342  5                                   6    
HELIX   51  51 GLY C  375  GLY C  379  1                                   5    
HELIX   52  52 ARG C  381  CYS C  384  1                                   4    
HELIX   53  53 LEU C  392  ARG C  398  1                                   7    
HELIX   54  54 LEU C  406  SER C  408  5                                   3    
HELIX   55  55 TRP C  410  LYS C  428  1                                  19    
HELIX   56  56 HIS C  436  SER C  453  1                                  18    
HELIX   57  57 TRP C  461  LEU C  464  1                                   4    
HELIX   58  58 GLY C  470  ILE C  472  5                                   3    
HELIX   59  59 PRO C  474  HIS C  477  1                                   4    
HELIX   60  60 ALA C  495  THR C  498  1                                   4    
HELIX   61  61 LEU D  100  HIS D  102  5                                   3    
HELIX   62  62 LYS D  123  LEU D  125  5                                   3    
HELIX   63  63 PRO D  136  SER D  153  1                                  18    
HELIX   64  64 ILE D  159  THR D  176  1                                  18    
HELIX   65  65 GLY D  183  ARG D  195  1                                  13    
HELIX   66  66 ARG D  203  GLN D  205  5                                   3    
HELIX   67  67 ALA D  220  GLY D  238  1                                  19    
HELIX   68  68 PRO D  281  ASP D  292  5                                  12    
HELIX   69  69 PRO D  323  LEU D  325  5                                   3    
HELIX   70  70 GLU D  337  LEU D  342  5                                   6    
HELIX   71  71 GLY D  375  GLY D  379  1                                   5    
HELIX   72  72 ARG D  381  CYS D  384  1                                   4    
HELIX   73  73 LEU D  392  ARG D  398  1                                   7    
HELIX   74  74 LEU D  406  SER D  408  5                                   3    
HELIX   75  75 TRP D  410  LYS D  428  1                                  19    
HELIX   76  76 HIS D  436  SER D  453  1                                  18    
HELIX   77  77 TRP D  461  LEU D  464  1                                   4    
HELIX   78  78 GLY D  470  ILE D  472  5                                   3    
HELIX   79  79 PRO D  474  HIS D  477  1                                   4    
HELIX   80  80 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 4 GLN A 210  ALA A 214  0                                        
SHEET    2   B 4 ALA A 243  PHE A 247  1  N  ILE A 244   O  GLN A 210           
SHEET    3   B 4 CYS A 367  TRP A 372 -1  N  ASN A 370   O  ALA A 243           
SHEET    4   B 4 LEU A 349  VAL A 352 -1  N  VAL A 352   O  PHE A 369           
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  MET A 331  0                                        
SHEET    2   E 2 LEU A 344  TYR A 347 -1  N  TRP A 346   O  VAL A 329           
SHEET    1   F 3 PHE A 488  TYR A 491  0                                        
SHEET    2   F 3 MET A 355  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 4 GLN B 210  ALA B 214  0                                        
SHEET    2   H 4 ALA B 243  PHE B 247  1  N  ILE B 244   O  GLN B 210           
SHEET    3   H 4 CYS B 367  TRP B 372 -1  N  ASN B 370   O  ALA B 243           
SHEET    4   H 4 LEU B 349  VAL B 352 -1  N  VAL B 352   O  PHE B 369           
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  MET B 331  0                                        
SHEET    2   K 2 LEU B 344  TYR B 347 -1  N  TRP B 346   O  VAL B 329           
SHEET    1   L 3 PHE B 488  TYR B 491  0                                        
SHEET    2   L 3 MET B 355  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 4 GLN C 210  ALA C 214  0                                        
SHEET    2   N 4 ALA C 243  PHE C 247  1  N  ILE C 244   O  GLN C 210           
SHEET    3   N 4 CYS C 367  TRP C 372 -1  N  ASN C 370   O  ALA C 243           
SHEET    4   N 4 LEU C 349  VAL C 352 -1  N  VAL C 352   O  PHE C 369           
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 3 PHE C 488  TYR C 491  0                                        
SHEET    2   R 3 MET C 355  VAL C 359 -1  N  GLU C 358   O  PHE C 488           
SHEET    3   R 3 LEU C 362  PHE C 364 -1  N  PHE C 364   O  LEU C 357           
SHEET    1   S 2 VAL D  85  LYS D  88  0                                        
SHEET    2   S 2 THR D  95  ASP D  98 -1  N  ASP D  98   O  VAL D  85           
SHEET    1   T 4 GLN D 210  ALA D 214  0                                        
SHEET    2   T 4 ALA D 243  PHE D 247  1  N  ILE D 244   O  GLN D 210           
SHEET    3   T 4 CYS D 367  TRP D 372 -1  N  ASN D 370   O  ALA D 243           
SHEET    4   T 4 LEU D 349  VAL D 352 -1  N  VAL D 352   O  PHE D 369           
SHEET    1   U 2 GLY D 269  GLN D 271  0                                        
SHEET    2   U 2 ILE D 277  GLY D 279 -1  N  ARG D 278   O  TYR D 270           
SHEET    1   V 2 LEU D 307  LEU D 309  0                                        
SHEET    2   V 2 GLU D 317  PHE D 319 -1  N  PHE D 319   O  LEU D 307           
SHEET    1   W 2 GLU D 328  MET D 331  0                                        
SHEET    2   W 2 LEU D 344  TYR D 347 -1  N  TRP D 346   O  VAL D 329           
SHEET    1   X 3 PHE D 488  TYR D 490  0                                        
SHEET    2   X 3 LEU D 356  VAL D 359 -1  N  GLU D 358   O  PHE D 488           
SHEET    3   X 3 LEU D 362  PHE D 364 -1  N  PHE D 364   O  LEU D 357           
SSBOND   1 CYS A  115    CYS B  115                          1555   1555  2.07  
SSBOND   2 CYS C  115    CYS D  115                          1555   1555  2.09  
LINK         SG  CYS C 200                FE   HEM C 550     1555   1555  2.19  
LINK        FE   HEM A 550                 SG  CYS A 200     1555   1555  2.20  
LINK        FE   HEM B 550                 SG  CYS B 200     1555   1555  2.24  
LINK        FE   HEM D 550                 SG  CYS D 200     1555   1555  2.26  
CISPEP   1 SER A  486    PRO A  487          0        -0.17                     
CISPEP   2 SER B  486    PRO B  487          0         0.02                     
CISPEP   3 SER C  486    PRO C  487          0         0.16                     
CISPEP   4 SER D  486    PRO D  487          0         0.09                     
SITE     1 AC1  4 ARG A 278  GLY A 300  ARG A 301  PHE A 302                    
SITE     1 AC2  4 TYR A 336  GLU A 337  TRP A 338  ARG D 340                    
SITE     1 AC3  4 ASN A 236  ASN A 239  ASN C 236  ASN C 239                    
SITE     1 AC4  3 ARG B 278  GLY B 300  ARG B 301                               
SITE     1 AC5  2 LYS B 335  GLU B 337                                          
SITE     1 AC6  2 GLY C 300  ARG C 301                                          
SITE     1 AC7  3 ARG B 340  GLU C 337  TRP C 338                               
SITE     1 AC8  2 ARG D 278  ARG D 301                                          
SITE     1 AC9  4 LYS D 335  TYR D 336  GLU D 337  TRP D 338                    
SITE     1 BC1 12 TRP A 194  CYS A 200  ILE A 201  PHE A 369                    
SITE     2 BC1 12 ASN A 370  GLY A 371  TRP A 372  GLU A 377                    
SITE     3 BC1 12 TRP A 463  TYR A 491  H4B A 600  ITU A 800                    
SITE     1 BC2  9 SER A 118  MET A 120  ARG A 381  ILE A 462                    
SITE     2 BC2  9 TRP A 463  HEM A 550  TRP B 461  PHE B 476                    
SITE     3 BC2  9 HIS B 477                                                     
SITE     1 BC3  6 PRO A 350  VAL A 352  GLY A 371  TRP A 372                    
SITE     2 BC3  6 GLU A 377  HEM A 550                                          
SITE     1 BC4 12 TRP B 194  CYS B 200  ILE B 201  PHE B 369                    
SITE     2 BC4 12 ASN B 370  GLY B 371  TRP B 372  GLU B 377                    
SITE     3 BC4 12 TRP B 463  TYR B 491  H4B B 601  ITU B 801                    
SITE     1 BC5 10 TRP A 461  PHE A 476  HIS A 477  GLN A 478                    
SITE     2 BC5 10 SER B 118  MET B 120  ARG B 381  ILE B 462                    
SITE     3 BC5 10 TRP B 463  HEM B 550                                          
SITE     1 BC6  6 PRO B 350  VAL B 352  GLY B 371  TRP B 372                    
SITE     2 BC6  6 GLU B 377  HEM B 550                                          
SITE     1 BC7 11 TRP C 194  CYS C 200  PHE C 369  ASN C 370                    
SITE     2 BC7 11 GLY C 371  TRP C 372  GLU C 377  TRP C 463                    
SITE     3 BC7 11 TYR C 491  H4B C 602  ITU C 802                               
SITE     1 BC8 10 SER C 118  MET C 120  ARG C 381  ILE C 462                    
SITE     2 BC8 10 TRP C 463  HEM C 550  TRP D 461  PHE D 476                    
SITE     3 BC8 10 HIS D 477  GLN D 478                                          
SITE     1 BC9  6 PRO C 350  VAL C 352  GLY C 371  TRP C 372                    
SITE     2 BC9  6 GLU C 377  HEM C 550                                          
SITE     1 CC1 11 TRP D 194  CYS D 200  PHE D 369  ASN D 370                    
SITE     2 CC1 11 GLY D 371  TRP D 372  GLU D 377  TRP D 463                    
SITE     3 CC1 11 TYR D 491  H4B D 603  ITU D 803                               
SITE     1 CC2 10 TRP C 461  PHE C 476  HIS C 477  GLN C 478                    
SITE     2 CC2 10 SER D 118  MET D 120  ARG D 381  ILE D 462                    
SITE     3 CC2 10 TRP D 463  HEM D 550                                          
SITE     1 CC3  6 PRO D 350  VAL D 352  GLY D 371  TRP D 372                    
SITE     2 CC3  6 GLU D 377  HEM D 550                                          
CRYST1  188.370  188.370  230.160  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      0.005309  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005309  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004345        0.00000                         
MTRIX1   1 -0.489109 -0.866926  0.095976       75.54540    1                    
MTRIX2   1 -0.869369  0.475655 -0.133977       51.67290    1                    
MTRIX3   1  0.070496 -0.148968 -0.986326       74.39810    1                    
MTRIX1   2 -0.855992  0.516839 -0.012429       45.43100    1                    
MTRIX2   2 -0.516982 -0.855621  0.025329       80.09170    1                    
MTRIX3   2  0.002457  0.028107  0.999602       40.27170    1                    
MTRIX1   3 -0.016854  0.990534 -0.136231        6.15530    1                    
MTRIX2   3  0.998232  0.024436  0.054174       -0.78440    1                    
MTRIX3   3  0.056990 -0.135077 -0.989195      115.96600    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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