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Database: PDB
Entry: 3E7G
LinkDB: 3E7G
Original site: 3E7G 
HEADER    OXIDOREDUCTASE                          18-AUG-08   3E7G              
TITLE     STRUCTURE OF HUMAN INOSOX WITH INHIBITOR AR-C95791                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NITRIC OXIDE SYNTHASE, INDUCIBLE;                          
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 82-505;                                       
COMPND   5 SYNONYM: INDUCIBLE NO SYNTHASE, INDUCIBLE NOS, INOS, NOS             
COMPND   6 TYPE II, HEPATOCYTE NOS, HEP-NOS;                                    
COMPND   7 EC: 1.14.13.39;                                                      
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI                                  
KEYWDS    NITRIC OXIDE, NOS, HEME, TETRAHYDROBIOPTERIN,                         
KEYWDS   2 OXIDOREDUCTASE, ALTERNATIVE SPLICING, CALCIUM, CALMODULIN-           
KEYWDS   3 BINDING, FAD, FMN, IRON, METAL-BINDING, NADP,                        
KEYWDS   4 PHOSPHOPROTEIN, POLYMORPHISM, ZINC                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.D.GARCIN,A.S.ARVAI,R.J.ROSENFELD,M.D.KROEGER,B.R.CRANE,             
AUTHOR   2 G.ANDERSSON,G.ANDREWS,P.J.HAMLEY,P.R.MALLINDER,D.J.NICHOLLS,         
AUTHOR   3 S.A.ST-GALLAY,A.C.TINKER,N.P.GENSMANTEL,A.METE,D.R.CHESHIRE,         
AUTHOR   4 S.CONNOLLY,D.J.STUEH,A.ABERG,A.V.WALLACE,J.A.TAINER,                 
AUTHOR   5 E.D.GETZOFF                                                          
REVDAT   2   20-JAN-09 3E7G    1       JRNL   VERSN                             
REVDAT   1   07-OCT-08 3E7G    0                                                
JRNL        AUTH   E.D.GARCIN,A.S.ARVAI,R.J.ROSENFELD,M.D.KROEGER,              
JRNL        AUTH 2 B.R.CRANE,G.ANDERSSON,G.ANDREWS,P.J.HAMLEY,                  
JRNL        AUTH 3 P.R.MALLINDER,D.J.NICHOLLS,S.A.ST-GALLAY,                    
JRNL        AUTH 4 A.C.TINKER,N.P.GENSMANTEL,A.METE,D.R.CHESHIRE,               
JRNL        AUTH 5 S.CONNOLLY,D.J.STUEHR,A.ABERG,A.V.WALLACE,                   
JRNL        AUTH 6 J.A.TAINER,E.D.GETZOFF                                       
JRNL        TITL   ANCHORED PLASTICITY OPENS DOORS FOR SELECTIVE                
JRNL        TITL 2 INHIBITOR DESIGN IN NITRIC OXIDE SYNTHASE.                   
JRNL        REF    NAT.CHEM.BIOL.                V.   4   700 2008              
JRNL        REFN                   ISSN 1552-4450                               
JRNL        PMID   18849972                                                     
JRNL        DOI    10.1038/NCHEMBIO.115                                         
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.9                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.51                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 262227.000                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 125869                         
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) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.213                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6396                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.34                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 69.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 15110                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580                       
REMARK   3   BIN FREE R VALUE                    : 0.2940                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 818                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.010                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13694                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 318                                     
REMARK   3   SOLVENT ATOMS            : 504                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.21                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -9.42000                                             
REMARK   3    B22 (A**2) : 10.94000                                             
REMARK   3    B33 (A**2) : -1.51000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 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) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.95                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.33                                                 
REMARK   3   BSOL        : 53.18                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.TOP                                
REMARK   3  PARAMETER FILE  2  : TOPH19X.HEME                                   
REMARK   3  PARAMETER FILE  3  : A1.TOP                                         
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN_REP.PARAM                              
REMARK   3  TOPOLOGY FILE  2   : PARAM19X.HEME                                  
REMARK   3  TOPOLOGY FILE  3   : A1.PAR                                         
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3E7G COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-AUG-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB048970.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-SEP-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 14-BM-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 141544                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 51.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MAGNESIUM SULFATE, HEPES, LITHIUM        
REMARK 280  ACETATE, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE         
REMARK 280  300K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       45.10300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       95.57050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       79.33550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       95.57050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       45.10300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       79.33550            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35540 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 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: 5340 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO A    82                                                      
REMARK 465     GLU A   504                                                      
REMARK 465     LYS A   505                                                      
REMARK 465     PRO B    82                                                      
REMARK 465     GLU B   504                                                      
REMARK 465     LYS B   505                                                      
REMARK 465     PRO C    82                                                      
REMARK 465     PRO D    82                                                      
REMARK 465     GLU D   504                                                      
REMARK 465     LYS D   505                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  83    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 503    CG   OD1  OD2                                       
REMARK 470     ARG B  83    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 503    CG   OD1  OD2                                       
REMARK 470     ARG C  83    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D  83    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP D 503    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A 157      150.60    -39.23                                   
REMARK 500    SER A 251      -91.33   -112.54                                   
REMARK 500    CYS A 367       64.05   -157.22                                   
REMARK 500    ARG A 388     -132.32   -114.64                                   
REMARK 500    CYS A 457       97.67   -169.77                                   
REMARK 500    LEU A 485     -160.72   -102.10                                   
REMARK 500    THR B 121       74.78   -117.79                                   
REMARK 500    ALA B 157      151.92    -48.26                                   
REMARK 500    SER B 251      -94.12   -104.76                                   
REMARK 500    LYS B 335      -60.27   -123.10                                   
REMARK 500    CYS B 367       63.58   -156.87                                   
REMARK 500    ARG B 388     -137.35   -118.47                                   
REMARK 500    ASN B 390       60.39     36.30                                   
REMARK 500    THR B 403       11.43    -67.50                                   
REMARK 500    ARG B 454       21.84   -145.20                                   
REMARK 500    CYS B 457       96.93   -160.43                                   
REMARK 500    LEU B 485     -163.40   -105.93                                   
REMARK 500    HIS C  84      149.36   -171.42                                   
REMARK 500    THR C 121       72.91   -115.85                                   
REMARK 500    SER C 251      -94.53   -100.66                                   
REMARK 500    TYR C 299       29.05     48.54                                   
REMARK 500    LYS C 335      -50.38   -125.12                                   
REMARK 500    CYS C 367       59.79   -156.05                                   
REMARK 500    ARG C 388     -133.56   -122.35                                   
REMARK 500    ASN C 390       63.70     32.48                                   
REMARK 500    CYS C 457       91.63   -164.21                                   
REMARK 500    LEU C 485     -166.32   -102.85                                   
REMARK 500    ASP C 503     -147.39   -138.22                                   
REMARK 500    GLU C 504       73.79   -110.47                                   
REMARK 500    HIS D  84      136.87    164.05                                   
REMARK 500    ALA D 104      165.40    -46.35                                   
REMARK 500    THR D 121       74.13   -119.55                                   
REMARK 500    ALA D 157      145.84    -35.34                                   
REMARK 500    ASN D 236       47.76     37.70                                   
REMARK 500    SER D 251      -90.58   -103.44                                   
REMARK 500    CYS D 367       65.94   -154.53                                   
REMARK 500    ARG D 388     -133.14   -121.23                                   
REMARK 500    ASN D 390       63.94     37.09                                   
REMARK 500    ARG D 454       15.10   -141.94                                   
REMARK 500    CYS D 457       93.52   -172.08                                   
REMARK 500    LEU D 485     -165.21   -103.44                                   
REMARK 500    GLN D 502       32.10    -99.83                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR D 451         0.07    SIDE_CHAIN                              
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 D7101        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH D7109        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH D7118        DISTANCE =  5.67 ANGSTROMS                       
REMARK 525    HOH A4124        DISTANCE =  5.29 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 A3001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 110   SG                                                     
REMARK 620 2 CYS A 115   SG  105.4                                              
REMARK 620 3 CYS B 110   SG  126.6 110.1                                        
REMARK 620 4 CYS B 115   SG   97.1 106.0 109.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C3002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 110   SG                                                     
REMARK 620 2 CYS C 115   SG  108.1                                              
REMARK 620 3 CYS D 110   SG  127.5 105.3                                        
REMARK 620 4 CYS D 115   SG  107.3 102.7 103.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A3001                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 901                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B A 902                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AT2 A 906                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B1901                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B B1902                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AT2 B1906                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C3002                  
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C2901                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B C2902                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AT2 C2906                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D3901                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B D3902                 
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AT2 D3906                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3E65   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3E67   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3E68   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3E6L   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3E6N   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3E6O   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3E6T   RELATED DB: PDB                                   
DBREF  3E7G A   82   505  UNP    P35228   NOS2A_HUMAN     82    505             
DBREF  3E7G B   82   505  UNP    P35228   NOS2A_HUMAN     82    505             
DBREF  3E7G C   82   505  UNP    P35228   NOS2A_HUMAN     82    505             
DBREF  3E7G D   82   505  UNP    P35228   NOS2A_HUMAN     82    505             
SEQRES   1 A  424  PRO ARG HIS VAL ARG ILE LYS ASN TRP GLY SER GLY MET          
SEQRES   2 A  424  THR PHE GLN ASP THR LEU HIS HIS LYS ALA LYS GLY ILE          
SEQRES   3 A  424  LEU THR CYS ARG SER LYS SER CYS LEU GLY SER ILE MET          
SEQRES   4 A  424  THR PRO LYS SER LEU THR ARG GLY PRO ARG ASP LYS PRO          
SEQRES   5 A  424  THR PRO PRO ASP GLU LEU LEU PRO GLN ALA ILE GLU PHE          
SEQRES   6 A  424  VAL ASN GLN TYR TYR GLY SER PHE LYS GLU ALA LYS ILE          
SEQRES   7 A  424  GLU GLU HIS LEU ALA ARG VAL GLU ALA VAL THR LYS GLU          
SEQRES   8 A  424  ILE GLU THR THR GLY THR TYR GLN LEU THR GLY ASP GLU          
SEQRES   9 A  424  LEU ILE PHE ALA THR LYS GLN ALA TRP ARG ASN ALA PRO          
SEQRES  10 A  424  ARG CYS ILE GLY ARG ILE GLN TRP SER ASN LEU GLN VAL          
SEQRES  11 A  424  PHE ASP ALA ARG SER CYS SER THR ALA ARG GLU MET PHE          
SEQRES  12 A  424  GLU HIS ILE CYS ARG HIS VAL ARG TYR SER THR ASN ASN          
SEQRES  13 A  424  GLY ASN ILE ARG SER ALA ILE THR VAL PHE PRO GLN ARG          
SEQRES  14 A  424  SER ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN ALA GLN          
SEQRES  15 A  424  LEU ILE ARG TYR ALA GLY TYR GLN MET PRO ASP GLY SER          
SEQRES  16 A  424  ILE ARG GLY ASP PRO ALA ASN VAL GLU PHE THR GLN LEU          
SEQRES  17 A  424  CYS ILE ASP LEU GLY TRP LYS PRO LYS TYR GLY ARG PHE          
SEQRES  18 A  424  ASP VAL VAL PRO LEU VAL LEU GLN ALA ASN GLY ARG ASP          
SEQRES  19 A  424  PRO GLU LEU PHE GLU ILE PRO PRO ASP LEU VAL LEU GLU          
SEQRES  20 A  424  VAL ALA MET GLU HIS PRO LYS TYR GLU TRP PHE ARG GLU          
SEQRES  21 A  424  LEU GLU LEU LYS TRP TYR ALA LEU PRO ALA VAL ALA ASN          
SEQRES  22 A  424  MET LEU LEU GLU VAL GLY GLY LEU GLU PHE PRO GLY CYS          
SEQRES  23 A  424  PRO PHE ASN GLY TRP TYR MET GLY THR GLU ILE GLY VAL          
SEQRES  24 A  424  ARG ASP PHE CYS ASP VAL GLN ARG TYR ASN ILE LEU GLU          
SEQRES  25 A  424  GLU VAL GLY ARG ARG MET GLY LEU GLU THR HIS LYS LEU          
SEQRES  26 A  424  ALA SER LEU TRP LYS ASP GLN ALA VAL VAL GLU ILE ASN          
SEQRES  27 A  424  ILE ALA VAL LEU HIS SER PHE GLN LYS GLN ASN VAL THR          
SEQRES  28 A  424  ILE MET ASP HIS HIS SER ALA ALA GLU SER PHE MET LYS          
SEQRES  29 A  424  TYR MET GLN ASN GLU TYR ARG SER ARG GLY GLY CYS PRO          
SEQRES  30 A  424  ALA ASP TRP ILE TRP LEU VAL PRO PRO MET SER GLY SER          
SEQRES  31 A  424  ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR VAL          
SEQRES  32 A  424  LEU SER PRO PHE TYR TYR TYR GLN VAL GLU ALA TRP LYS          
SEQRES  33 A  424  THR HIS VAL TRP GLN ASP GLU LYS                              
SEQRES   1 B  424  PRO ARG HIS VAL ARG ILE LYS ASN TRP GLY SER GLY MET          
SEQRES   2 B  424  THR PHE GLN ASP THR LEU HIS HIS LYS ALA LYS GLY ILE          
SEQRES   3 B  424  LEU THR CYS ARG SER LYS SER CYS LEU GLY SER ILE MET          
SEQRES   4 B  424  THR PRO LYS SER LEU THR ARG GLY PRO ARG ASP LYS PRO          
SEQRES   5 B  424  THR PRO PRO ASP GLU LEU LEU PRO GLN ALA ILE GLU PHE          
SEQRES   6 B  424  VAL ASN GLN TYR TYR GLY SER PHE LYS GLU ALA LYS ILE          
SEQRES   7 B  424  GLU GLU HIS LEU ALA ARG VAL GLU ALA VAL THR LYS GLU          
SEQRES   8 B  424  ILE GLU THR THR GLY THR TYR GLN LEU THR GLY ASP GLU          
SEQRES   9 B  424  LEU ILE PHE ALA THR LYS GLN ALA TRP ARG ASN ALA PRO          
SEQRES  10 B  424  ARG CYS ILE GLY ARG ILE GLN TRP SER ASN LEU GLN VAL          
SEQRES  11 B  424  PHE ASP ALA ARG SER CYS SER THR ALA ARG GLU MET PHE          
SEQRES  12 B  424  GLU HIS ILE CYS ARG HIS VAL ARG TYR SER THR ASN ASN          
SEQRES  13 B  424  GLY ASN ILE ARG SER ALA ILE THR VAL PHE PRO GLN ARG          
SEQRES  14 B  424  SER ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN ALA GLN          
SEQRES  15 B  424  LEU ILE ARG TYR ALA GLY TYR GLN MET PRO ASP GLY SER          
SEQRES  16 B  424  ILE ARG GLY ASP PRO ALA ASN VAL GLU PHE THR GLN LEU          
SEQRES  17 B  424  CYS ILE ASP LEU GLY TRP LYS PRO LYS TYR GLY ARG PHE          
SEQRES  18 B  424  ASP VAL VAL PRO LEU VAL LEU GLN ALA ASN GLY ARG ASP          
SEQRES  19 B  424  PRO GLU LEU PHE GLU ILE PRO PRO ASP LEU VAL LEU GLU          
SEQRES  20 B  424  VAL ALA MET GLU HIS PRO LYS TYR GLU TRP PHE ARG GLU          
SEQRES  21 B  424  LEU GLU LEU LYS TRP TYR ALA LEU PRO ALA VAL ALA ASN          
SEQRES  22 B  424  MET LEU LEU GLU VAL GLY GLY LEU GLU PHE PRO GLY CYS          
SEQRES  23 B  424  PRO PHE ASN GLY TRP TYR MET GLY THR GLU ILE GLY VAL          
SEQRES  24 B  424  ARG ASP PHE CYS ASP VAL GLN ARG TYR ASN ILE LEU GLU          
SEQRES  25 B  424  GLU VAL GLY ARG ARG MET GLY LEU GLU THR HIS LYS LEU          
SEQRES  26 B  424  ALA SER LEU TRP LYS ASP GLN ALA VAL VAL GLU ILE ASN          
SEQRES  27 B  424  ILE ALA VAL LEU HIS SER PHE GLN LYS GLN ASN VAL THR          
SEQRES  28 B  424  ILE MET ASP HIS HIS SER ALA ALA GLU SER PHE MET LYS          
SEQRES  29 B  424  TYR MET GLN ASN GLU TYR ARG SER ARG GLY GLY CYS PRO          
SEQRES  30 B  424  ALA ASP TRP ILE TRP LEU VAL PRO PRO MET SER GLY SER          
SEQRES  31 B  424  ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR VAL          
SEQRES  32 B  424  LEU SER PRO PHE TYR TYR TYR GLN VAL GLU ALA TRP LYS          
SEQRES  33 B  424  THR HIS VAL TRP GLN ASP GLU LYS                              
SEQRES   1 C  424  PRO ARG HIS VAL ARG ILE LYS ASN TRP GLY SER GLY MET          
SEQRES   2 C  424  THR PHE GLN ASP THR LEU HIS HIS LYS ALA LYS GLY ILE          
SEQRES   3 C  424  LEU THR CYS ARG SER LYS SER CYS LEU GLY SER ILE MET          
SEQRES   4 C  424  THR PRO LYS SER LEU THR ARG GLY PRO ARG ASP LYS PRO          
SEQRES   5 C  424  THR PRO PRO ASP GLU LEU LEU PRO GLN ALA ILE GLU PHE          
SEQRES   6 C  424  VAL ASN GLN TYR TYR GLY SER PHE LYS GLU ALA LYS ILE          
SEQRES   7 C  424  GLU GLU HIS LEU ALA ARG VAL GLU ALA VAL THR LYS GLU          
SEQRES   8 C  424  ILE GLU THR THR GLY THR TYR GLN LEU THR GLY ASP GLU          
SEQRES   9 C  424  LEU ILE PHE ALA THR LYS GLN ALA TRP ARG ASN ALA PRO          
SEQRES  10 C  424  ARG CYS ILE GLY ARG ILE GLN TRP SER ASN LEU GLN VAL          
SEQRES  11 C  424  PHE ASP ALA ARG SER CYS SER THR ALA ARG GLU MET PHE          
SEQRES  12 C  424  GLU HIS ILE CYS ARG HIS VAL ARG TYR SER THR ASN ASN          
SEQRES  13 C  424  GLY ASN ILE ARG SER ALA ILE THR VAL PHE PRO GLN ARG          
SEQRES  14 C  424  SER ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN ALA GLN          
SEQRES  15 C  424  LEU ILE ARG TYR ALA GLY TYR GLN MET PRO ASP GLY SER          
SEQRES  16 C  424  ILE ARG GLY ASP PRO ALA ASN VAL GLU PHE THR GLN LEU          
SEQRES  17 C  424  CYS ILE ASP LEU GLY TRP LYS PRO LYS TYR GLY ARG PHE          
SEQRES  18 C  424  ASP VAL VAL PRO LEU VAL LEU GLN ALA ASN GLY ARG ASP          
SEQRES  19 C  424  PRO GLU LEU PHE GLU ILE PRO PRO ASP LEU VAL LEU GLU          
SEQRES  20 C  424  VAL ALA MET GLU HIS PRO LYS TYR GLU TRP PHE ARG GLU          
SEQRES  21 C  424  LEU GLU LEU LYS TRP TYR ALA LEU PRO ALA VAL ALA ASN          
SEQRES  22 C  424  MET LEU LEU GLU VAL GLY GLY LEU GLU PHE PRO GLY CYS          
SEQRES  23 C  424  PRO PHE ASN GLY TRP TYR MET GLY THR GLU ILE GLY VAL          
SEQRES  24 C  424  ARG ASP PHE CYS ASP VAL GLN ARG TYR ASN ILE LEU GLU          
SEQRES  25 C  424  GLU VAL GLY ARG ARG MET GLY LEU GLU THR HIS LYS LEU          
SEQRES  26 C  424  ALA SER LEU TRP LYS ASP GLN ALA VAL VAL GLU ILE ASN          
SEQRES  27 C  424  ILE ALA VAL LEU HIS SER PHE GLN LYS GLN ASN VAL THR          
SEQRES  28 C  424  ILE MET ASP HIS HIS SER ALA ALA GLU SER PHE MET LYS          
SEQRES  29 C  424  TYR MET GLN ASN GLU TYR ARG SER ARG GLY GLY CYS PRO          
SEQRES  30 C  424  ALA ASP TRP ILE TRP LEU VAL PRO PRO MET SER GLY SER          
SEQRES  31 C  424  ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR VAL          
SEQRES  32 C  424  LEU SER PRO PHE TYR TYR TYR GLN VAL GLU ALA TRP LYS          
SEQRES  33 C  424  THR HIS VAL TRP GLN ASP GLU LYS                              
SEQRES   1 D  424  PRO ARG HIS VAL ARG ILE LYS ASN TRP GLY SER GLY MET          
SEQRES   2 D  424  THR PHE GLN ASP THR LEU HIS HIS LYS ALA LYS GLY ILE          
SEQRES   3 D  424  LEU THR CYS ARG SER LYS SER CYS LEU GLY SER ILE MET          
SEQRES   4 D  424  THR PRO LYS SER LEU THR ARG GLY PRO ARG ASP LYS PRO          
SEQRES   5 D  424  THR PRO PRO ASP GLU LEU LEU PRO GLN ALA ILE GLU PHE          
SEQRES   6 D  424  VAL ASN GLN TYR TYR GLY SER PHE LYS GLU ALA LYS ILE          
SEQRES   7 D  424  GLU GLU HIS LEU ALA ARG VAL GLU ALA VAL THR LYS GLU          
SEQRES   8 D  424  ILE GLU THR THR GLY THR TYR GLN LEU THR GLY ASP GLU          
SEQRES   9 D  424  LEU ILE PHE ALA THR LYS GLN ALA TRP ARG ASN ALA PRO          
SEQRES  10 D  424  ARG CYS ILE GLY ARG ILE GLN TRP SER ASN LEU GLN VAL          
SEQRES  11 D  424  PHE ASP ALA ARG SER CYS SER THR ALA ARG GLU MET PHE          
SEQRES  12 D  424  GLU HIS ILE CYS ARG HIS VAL ARG TYR SER THR ASN ASN          
SEQRES  13 D  424  GLY ASN ILE ARG SER ALA ILE THR VAL PHE PRO GLN ARG          
SEQRES  14 D  424  SER ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN ALA GLN          
SEQRES  15 D  424  LEU ILE ARG TYR ALA GLY TYR GLN MET PRO ASP GLY SER          
SEQRES  16 D  424  ILE ARG GLY ASP PRO ALA ASN VAL GLU PHE THR GLN LEU          
SEQRES  17 D  424  CYS ILE ASP LEU GLY TRP LYS PRO LYS TYR GLY ARG PHE          
SEQRES  18 D  424  ASP VAL VAL PRO LEU VAL LEU GLN ALA ASN GLY ARG ASP          
SEQRES  19 D  424  PRO GLU LEU PHE GLU ILE PRO PRO ASP LEU VAL LEU GLU          
SEQRES  20 D  424  VAL ALA MET GLU HIS PRO LYS TYR GLU TRP PHE ARG GLU          
SEQRES  21 D  424  LEU GLU LEU LYS TRP TYR ALA LEU PRO ALA VAL ALA ASN          
SEQRES  22 D  424  MET LEU LEU GLU VAL GLY GLY LEU GLU PHE PRO GLY CYS          
SEQRES  23 D  424  PRO PHE ASN GLY TRP TYR MET GLY THR GLU ILE GLY VAL          
SEQRES  24 D  424  ARG ASP PHE CYS ASP VAL GLN ARG TYR ASN ILE LEU GLU          
SEQRES  25 D  424  GLU VAL GLY ARG ARG MET GLY LEU GLU THR HIS LYS LEU          
SEQRES  26 D  424  ALA SER LEU TRP LYS ASP GLN ALA VAL VAL GLU ILE ASN          
SEQRES  27 D  424  ILE ALA VAL LEU HIS SER PHE GLN LYS GLN ASN VAL THR          
SEQRES  28 D  424  ILE MET ASP HIS HIS SER ALA ALA GLU SER PHE MET LYS          
SEQRES  29 D  424  TYR MET GLN ASN GLU TYR ARG SER ARG GLY GLY CYS PRO          
SEQRES  30 D  424  ALA ASP TRP ILE TRP LEU VAL PRO PRO MET SER GLY SER          
SEQRES  31 D  424  ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR VAL          
SEQRES  32 D  424  LEU SER PRO PHE TYR TYR TYR GLN VAL GLU ALA TRP LYS          
SEQRES  33 D  424  THR HIS VAL TRP GLN ASP GLU LYS                              
HET     ZN  A3001       1                                                       
HET    HEM  A 901      43                                                       
HET    H4B  A 902      17                                                       
HET    AT2  A 906      19                                                       
HET    HEM  B1901      43                                                       
HET    H4B  B1902      17                                                       
HET    AT2  B1906      19                                                       
HET     ZN  C3002       1                                                       
HET    HEM  C2901      43                                                       
HET    H4B  C2902      17                                                       
HET    AT2  C2906      19                                                       
HET    HEM  D3901      43                                                       
HET    H4B  D3902      17                                                       
HET    AT2  D3906      19                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     H4B 5,6,7,8-TETRAHYDROBIOPTERIN                                      
HETNAM     AT2 ETHYL 4-[(4-METHYLPYRIDIN-2-YL)AMINO]PIPERIDINE-1-               
HETNAM   2 AT2  CARBOXYLATE                                                     
HETSYN     HEM HEME                                                             
FORMUL   5   ZN    2(ZN 2+)                                                     
FORMUL   6  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL   7  H4B    4(C9 H15 N5 O3)                                              
FORMUL   8  AT2    4(C14 H21 N3 O2)                                             
FORMUL  19  HOH   *504(H2 O)                                                    
HELIX    1   1 THR A   99  ALA A  104  5                                   6    
HELIX    2   2 PRO A  122  THR A  126  5                                   5    
HELIX    3   3 PRO A  135  SER A  153  1                                  19    
HELIX    4   4 LYS A  158  THR A  176  1                                  19    
HELIX    5   5 THR A  182  ASN A  196  1                                  15    
HELIX    6   6 GLY A  202  TRP A  206  5                                   5    
HELIX    7   7 THR A  219  ASN A  236  1                                  18    
HELIX    8   8 ASN A  237  ASN A  239  5                                   3    
HELIX    9   9 ASN A  283  LEU A  293  1                                  11    
HELIX   10  10 PRO A  322  VAL A  326  5                                   5    
HELIX   11  11 TYR A  336  GLU A  343  5                                   8    
HELIX   12  12 MET A  374  VAL A  380  1                                   7    
HELIX   13  13 VAL A  380  ASP A  385  1                                   6    
HELIX   14  14 ILE A  391  GLY A  400  1                                  10    
HELIX   15  15 LYS A  405  SER A  408  5                                   4    
HELIX   16  16 LEU A  409  GLN A  429  1                                  21    
HELIX   17  17 ASP A  435  GLY A  455  1                                  21    
HELIX   18  18 ASP A  460  VAL A  465  1                                   6    
HELIX   19  19 SER A  469  GLN A  478  5                                  10    
HELIX   20  20 GLU A  494  HIS A  499  1                                   6    
HELIX   21  21 THR B   99  ALA B  104  5                                   6    
HELIX   22  22 PRO B  122  THR B  126  5                                   5    
HELIX   23  23 PRO B  135  SER B  153  1                                  19    
HELIX   24  24 LYS B  158  GLY B  177  1                                  20    
HELIX   25  25 THR B  182  ASN B  196  1                                  15    
HELIX   26  26 GLY B  202  TRP B  206  5                                   5    
HELIX   27  27 THR B  219  ASN B  236  1                                  18    
HELIX   28  28 ASN B  237  ASN B  239  5                                   3    
HELIX   29  29 ASN B  283  LEU B  293  1                                  11    
HELIX   30  30 PRO B  322  VAL B  326  5                                   5    
HELIX   31  31 TYR B  336  GLU B  343  5                                   8    
HELIX   32  32 MET B  374  VAL B  380  1                                   7    
HELIX   33  33 VAL B  380  ASP B  385  1                                   6    
HELIX   34  34 ILE B  391  MET B  399  1                                   9    
HELIX   35  35 LYS B  405  SER B  408  5                                   4    
HELIX   36  36 LEU B  409  GLN B  429  1                                  21    
HELIX   37  37 ASP B  435  GLY B  455  1                                  21    
HELIX   38  38 ASP B  460  VAL B  465  1                                   6    
HELIX   39  39 SER B  469  GLN B  478  5                                  10    
HELIX   40  40 GLU B  494  HIS B  499  1                                   6    
HELIX   41  41 THR C   99  ALA C  104  5                                   6    
HELIX   42  42 PRO C  122  THR C  126  5                                   5    
HELIX   43  43 PRO C  135  GLY C  152  1                                  18    
HELIX   44  44 LYS C  158  GLY C  177  1                                  20    
HELIX   45  45 THR C  182  ASN C  196  1                                  15    
HELIX   46  46 GLY C  202  TRP C  206  5                                   5    
HELIX   47  47 THR C  219  ASN C  236  1                                  18    
HELIX   48  48 ASN C  237  ASN C  239  5                                   3    
HELIX   49  49 ASN C  283  LEU C  293  1                                  11    
HELIX   50  50 PRO C  322  VAL C  326  5                                   5    
HELIX   51  51 TYR C  336  GLU C  343  5                                   8    
HELIX   52  52 MET C  374  VAL C  380  1                                   7    
HELIX   53  53 VAL C  380  ASP C  385  1                                   6    
HELIX   54  54 ILE C  391  MET C  399  1                                   9    
HELIX   55  55 LYS C  405  SER C  408  5                                   4    
HELIX   56  56 LEU C  409  GLN C  429  1                                  21    
HELIX   57  57 ASP C  435  GLY C  455  1                                  21    
HELIX   58  58 ASP C  460  VAL C  465  1                                   6    
HELIX   59  59 SER C  469  GLN C  478  5                                  10    
HELIX   60  60 GLU C  494  THR C  498  5                                   5    
HELIX   61  61 THR D   99  LYS D  103  5                                   5    
HELIX   62  62 PRO D  122  THR D  126  5                                   5    
HELIX   63  63 PRO D  135  GLY D  152  1                                  18    
HELIX   64  64 LYS D  158  GLY D  177  1                                  20    
HELIX   65  65 THR D  182  ASN D  196  1                                  15    
HELIX   66  66 GLY D  202  TRP D  206  5                                   5    
HELIX   67  67 THR D  219  ASN D  236  1                                  18    
HELIX   68  68 ASN D  237  ASN D  239  5                                   3    
HELIX   69  69 ASN D  283  LEU D  293  1                                  11    
HELIX   70  70 PRO D  322  VAL D  326  5                                   5    
HELIX   71  71 TYR D  336  GLU D  343  5                                   8    
HELIX   72  72 MET D  374  VAL D  380  1                                   7    
HELIX   73  73 VAL D  380  ASP D  385  1                                   6    
HELIX   74  74 ILE D  391  MET D  399  1                                   9    
HELIX   75  75 LYS D  405  SER D  408  5                                   4    
HELIX   76  76 LEU D  409  GLN D  429  1                                  21    
HELIX   77  77 ASP D  435  GLY D  455  1                                  21    
HELIX   78  78 ASP D  460  VAL D  465  1                                   6    
HELIX   79  79 SER D  469  GLN D  478  5                                  10    
HELIX   80  80 GLU D  494  THR D  498  5                                   5    
SHEET    1   A 2 VAL A  85  LYS A  88  0                                        
SHEET    2   A 2 THR A  95  ASP A  98 -1  O  PHE A  96   N  ILE A  87           
SHEET    1   B 4 GLN A 210  ASP A 213  0                                        
SHEET    2   B 4 ALA A 243  VAL A 246  1  O  ILE A 244   N  PHE A 212           
SHEET    3   B 4 PHE A 369  ASN A 370 -1  O  ASN A 370   N  ALA A 243           
SHEET    4   B 4 ALA A 351  VAL A 352 -1  N  VAL A 352   O  PHE A 369           
SHEET    1   C 3 ARG A 258  VAL A 259  0                                        
SHEET    2   C 3 LEU A 307  GLN A 310 -1  O  GLN A 310   N  ARG A 258           
SHEET    3   C 3 GLU A 317  PHE A 319 -1  O  PHE A 319   N  LEU A 307           
SHEET    1   D 2 GLY A 269  GLN A 271  0                                        
SHEET    2   D 2 ILE A 277  GLY A 279 -1  O  ARG A 278   N  TYR A 270           
SHEET    1   E 2 GLU A 328  ALA A 330  0                                        
SHEET    2   E 2 LYS A 345  TYR A 347 -1  O  TRP A 346   N  VAL A 329           
SHEET    1   F 3 LEU A 362  PHE A 364  0                                        
SHEET    2   F 3 LEU A 356  VAL A 359 -1  N  LEU A 357   O  PHE A 364           
SHEET    3   F 3 PHE A 488  TYR A 490 -1  O  TYR A 490   N  LEU A 356           
SHEET    1   G 2 VAL B  85  LYS B  88  0                                        
SHEET    2   G 2 THR B  95  ASP B  98 -1  O  PHE B  96   N  ILE B  87           
SHEET    1   H 4 GLN B 210  ASP B 213  0                                        
SHEET    2   H 4 ALA B 243  VAL B 246  1  O  ILE B 244   N  PHE B 212           
SHEET    3   H 4 PHE B 369  ASN B 370 -1  O  ASN B 370   N  ALA B 243           
SHEET    4   H 4 ALA B 351  VAL B 352 -1  N  VAL B 352   O  PHE B 369           
SHEET    1   I 3 ARG B 258  VAL B 259  0                                        
SHEET    2   I 3 LEU B 307  GLN B 310 -1  O  GLN B 310   N  ARG B 258           
SHEET    3   I 3 GLU B 317  PHE B 319 -1  O  PHE B 319   N  LEU B 307           
SHEET    1   J 2 GLY B 269  GLN B 271  0                                        
SHEET    2   J 2 ILE B 277  GLY B 279 -1  O  ARG B 278   N  TYR B 270           
SHEET    1   K 2 GLU B 328  ALA B 330  0                                        
SHEET    2   K 2 LYS B 345  TYR B 347 -1  O  TRP B 346   N  VAL B 329           
SHEET    1   L 3 LEU B 362  PHE B 364  0                                        
SHEET    2   L 3 LEU B 356  VAL B 359 -1  N  VAL B 359   O  LEU B 362           
SHEET    3   L 3 PHE B 488  TYR B 490 -1  O  TYR B 490   N  LEU B 356           
SHEET    1   M 2 VAL C  85  LYS C  88  0                                        
SHEET    2   M 2 THR C  95  ASP C  98 -1  O  ASP C  98   N  VAL C  85           
SHEET    1   N 4 GLN C 210  ASP C 213  0                                        
SHEET    2   N 4 ALA C 243  VAL C 246  1  O  ILE C 244   N  PHE C 212           
SHEET    3   N 4 PHE C 369  ASN C 370 -1  O  ASN C 370   N  ALA C 243           
SHEET    4   N 4 ALA C 351  VAL C 352 -1  N  VAL C 352   O  PHE C 369           
SHEET    1   O 3 ARG C 258  VAL C 259  0                                        
SHEET    2   O 3 LEU C 307  GLN C 310 -1  O  GLN C 310   N  ARG C 258           
SHEET    3   O 3 GLU C 317  PHE C 319 -1  O  PHE C 319   N  LEU C 307           
SHEET    1   P 2 GLY C 269  GLN C 271  0                                        
SHEET    2   P 2 ILE C 277  GLY C 279 -1  O  ARG C 278   N  TYR C 270           
SHEET    1   Q 2 GLU C 328  ALA C 330  0                                        
SHEET    2   Q 2 LYS C 345  TYR C 347 -1  O  TRP C 346   N  VAL C 329           
SHEET    1   R 3 LEU C 362  PHE C 364  0                                        
SHEET    2   R 3 LEU C 356  VAL C 359 -1  N  LEU C 357   O  PHE C 364           
SHEET    3   R 3 PHE C 488  TYR C 490 -1  O  TYR C 490   N  LEU C 356           
SHEET    1   S 2 VAL D  85  LYS D  88  0                                        
SHEET    2   S 2 THR D  95  ASP D  98 -1  O  ASP D  98   N  VAL D  85           
SHEET    1   T 4 GLN D 210  ASP D 213  0                                        
SHEET    2   T 4 ALA D 243  VAL D 246  1  O  ILE D 244   N  PHE D 212           
SHEET    3   T 4 PHE D 369  ASN D 370 -1  O  ASN D 370   N  ALA D 243           
SHEET    4   T 4 ALA D 351  VAL D 352 -1  N  VAL D 352   O  PHE D 369           
SHEET    1   U 3 ARG D 258  VAL D 259  0                                        
SHEET    2   U 3 LEU D 307  GLN D 310 -1  O  GLN D 310   N  ARG D 258           
SHEET    3   U 3 GLU D 317  PHE D 319 -1  O  PHE D 319   N  LEU D 307           
SHEET    1   V 2 GLY D 269  GLN D 271  0                                        
SHEET    2   V 2 ILE D 277  GLY D 279 -1  O  ARG D 278   N  TYR D 270           
SHEET    1   W 2 GLU D 328  ALA D 330  0                                        
SHEET    2   W 2 LYS D 345  TYR D 347 -1  O  TRP D 346   N  VAL D 329           
SHEET    1   X 3 LEU D 362  PHE D 364  0                                        
SHEET    2   X 3 LEU D 356  VAL D 359 -1  N  LEU D 357   O  PHE D 364           
SHEET    3   X 3 PHE D 488  TYR D 490 -1  O  TYR D 490   N  LEU D 356           
LINK         SG  CYS A 110                ZN    ZN A3001     1555   1555  2.76  
LINK         SG  CYS A 115                ZN    ZN A3001     1555   1555  2.69  
LINK         SG  CYS A 200                FE   HEM A 901     1555   1555  2.58  
LINK         SG  CYS B 110                ZN    ZN A3001     1555   1555  2.65  
LINK         SG  CYS B 115                ZN    ZN A3001     1555   1555  2.70  
LINK         SG  CYS B 200                FE   HEM B1901     1555   1555  2.52  
LINK         SG  CYS C 110                ZN    ZN C3002     1555   1555  2.80  
LINK         SG  CYS C 115                ZN    ZN C3002     1555   1555  2.63  
LINK         SG  CYS C 200                FE   HEM C2901     1555   1555  2.53  
LINK         SG  CYS D 110                ZN    ZN C3002     1555   1555  2.73  
LINK         SG  CYS D 115                ZN    ZN C3002     1555   1555  2.66  
LINK         SG  CYS D 200                FE   HEM D3901     1555   1555  2.58  
CISPEP   1 SER A  486    PRO A  487          0         0.12                     
CISPEP   2 SER B  486    PRO B  487          0         0.02                     
CISPEP   3 SER C  486    PRO C  487          0        -0.14                     
CISPEP   4 SER D  486    PRO D  487          0         0.08                     
SITE     1 AC1  4 CYS A 110  CYS A 115  CYS B 110  CYS B 115                    
SITE     1 AC2 18 TRP A 194  ARG A 199  CYS A 200  SER A 242                    
SITE     2 AC2 18 PHE A 369  ASN A 370  TRP A 372  GLU A 377                    
SITE     3 AC2 18 TRP A 463  TYR A 489  TYR A 491  H4B A 902                    
SITE     4 AC2 18 AT2 A 906  HOH A4015  HOH A4023  HOH A4048                    
SITE     5 AC2 18 HOH A4116  HOH A4121                                          
SITE     1 AC3 10 SER A 118  MET A 120  ARG A 381  ILE A 462                    
SITE     2 AC3 10 TRP A 463  HEM A 901  HOH A4072  HOH A4123                    
SITE     3 AC3 10 PHE B 476  HIS B 477                                          
SITE     1 AC4 12 GLN A 263  ARG A 266  TYR A 347  PRO A 350                    
SITE     2 AC4 12 PHE A 369  GLY A 371  TRP A 372  TYR A 373                    
SITE     3 AC4 12 GLU A 377  ASP A 382  ARG A 388  HEM A 901                    
SITE     1 AC5 19 TRP B 194  ARG B 199  CYS B 200  SER B 242                    
SITE     2 AC5 19 PHE B 369  ASN B 370  TRP B 372  GLU B 377                    
SITE     3 AC5 19 TRP B 463  TYR B 489  TYR B 491  H4B B1902                    
SITE     4 AC5 19 AT2 B1906  HOH B5026  HOH B5051  HOH B5061                    
SITE     5 AC5 19 HOH B5075  HOH B5093  HOH B5110                               
SITE     1 AC6 10 PHE A 476  HIS A 477  GLN A 478  SER B 118                    
SITE     2 AC6 10 MET B 120  ARG B 381  ILE B 462  TRP B 463                    
SITE     3 AC6 10 HEM B1901  HOH B5093                                          
SITE     1 AC7 11 GLN B 263  ARG B 266  TYR B 347  PRO B 350                    
SITE     2 AC7 11 GLY B 371  TRP B 372  TYR B 373  GLU B 377                    
SITE     3 AC7 11 ASP B 382  ARG B 388  HEM B1901                               
SITE     1 AC8  4 CYS C 110  CYS C 115  CYS D 110  CYS D 115                    
SITE     1 AC9 19 TRP C 194  ARG C 199  CYS C 200  SER C 242                    
SITE     2 AC9 19 PHE C 369  ASN C 370  TRP C 372  GLU C 377                    
SITE     3 AC9 19 TRP C 463  TYR C 489  TYR C 491  H4B C2902                    
SITE     4 AC9 19 AT2 C2906  HOH C6014  HOH C6047  HOH C6050                    
SITE     5 AC9 19 HOH C6079  HOH C6080  HOH C6131                               
SITE     1 BC1 11 SER C 118  MET C 120  ARG C 381  ILE C 462                    
SITE     2 BC1 11 TRP C 463  HEM C2901  HOH C6033  HOH C6087                    
SITE     3 BC1 11 HOH C6131  PHE D 476  GLN D 478                               
SITE     1 BC2 11 GLN C 263  ARG C 266  TYR C 347  PHE C 369                    
SITE     2 BC2 11 GLY C 371  TRP C 372  TYR C 373  GLU C 377                    
SITE     3 BC2 11 ASP C 382  ARG C 388  HEM C2901                               
SITE     1 BC3 18 TRP D 194  ARG D 199  CYS D 200  SER D 242                    
SITE     2 BC3 18 PHE D 369  ASN D 370  TRP D 372  GLU D 377                    
SITE     3 BC3 18 TRP D 463  TYR D 489  TYR D 491  H4B D3902                    
SITE     4 BC3 18 AT2 D3906  HOH D7024  HOH D7044  HOH D7048                    
SITE     5 BC3 18 HOH D7088  HOH D7091                                          
SITE     1 BC4 12 PHE C 476  HIS C 477  GLU C 479  SER D 118                    
SITE     2 BC4 12 MET D 120  ARG D 381  ILE D 462  TRP D 463                    
SITE     3 BC4 12 HEM D3901  HOH D7035  HOH D7092  HOH D7106                    
SITE     1 BC5 11 GLN D 263  ARG D 266  TYR D 347  PRO D 350                    
SITE     2 BC5 11 GLY D 371  TRP D 372  TYR D 373  GLU D 377                    
SITE     3 BC5 11 ASP D 382  ARG D 388  HEM D3901                               
CRYST1   90.206  158.671  191.141  90.00  90.00  90.00 P 21 21 21   16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011086  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006302  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005232        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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