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Database: PDB
Entry: 3EJ8
LinkDB: 3EJ8
Original site: 3EJ8 
HEADER    OXIDOREDUCTASE                          17-SEP-08   3EJ8              
TITLE     STRUCTURE OF DOUBLE MUTANT OF HUMAN INOS OXYGENASE DOMAIN             
TITLE    2 WITH BOUND IMMIDAZOLE                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NITRIC OXIDE SYNTHASE, INDUCIBLE;                          
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: NOS TYPE II, INDUCIBLE NOS, INOS, INDUCIBLE NO              
COMPND   5 SYNTHASE, HEPATOCYTE NOS, HEP-NOS;                                   
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 GENE: NOS2A, NOS2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PCWORI                                    
KEYWDS    NITRIC OXIDE SYNTHASE, NOS, HEME, TETRAHYDROBIOPTERIN,                
KEYWDS   2 OXIDOREDUCTASE CALMODULIN-BINDING, FAD, FMN, IRON, METAL-            
KEYWDS   3 BINDING, NADP, OXIDOREDUCTASE, 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,                      
AUTHOR   3 D.J.NICHOLLS,S.A.ST-GALLAY,A.C.TINKER,N.P.GENSMANTEL,                
AUTHOR   4 A.METE,D.R.CHESHIRE,S.CONNOLLY,D.J.STUEHR,A.ABERG,                   
AUTHOR   5 A.V.WALLACE,J.A.TAINER,E.D.GETZOFF                                   
REVDAT   4   09-JUN-09 3EJ8    1       REVDAT                                   
REVDAT   3   24-FEB-09 3EJ8    1       VERSN                                    
REVDAT   2   13-JAN-09 3EJ8    1       JRNL                                     
REVDAT   1   07-OCT-08 3EJ8    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.    2.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.85                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 3489997.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 77427                          
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) : 0.232                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3931                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.71                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 59.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 7961                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4540                       
REMARK   3   BIN FREE R VALUE                    : 0.4590                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 411                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.023                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13664                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 262                                     
REMARK   3   SOLVENT ATOMS            : 193                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 70.67                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -45.56000                                            
REMARK   3    B22 (A**2) : 49.01000                                             
REMARK   3    B33 (A**2) : -3.46000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.43                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.87                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.48                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.90                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.90                            
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) : 3.280 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 5.010 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 5.340 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 7.400 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.32                                                 
REMARK   3   BSOL        : 50.51                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : PARA_NEW.INP                                   
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : PARA_NEW.INP                                   
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 3EJ8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-SEP-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB049390.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.080                              
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 : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 77427                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.850                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: NULL                         
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.0, VAPOR DIFFUSION, HANGING         
REMARK 280  DROP, TEMPERATURE 298K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       44.94150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       95.52350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       75.35500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       95.52350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       44.94150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       75.35500            
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: 9850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -107.0 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: 9930 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -110.0 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     GLU C   504                                                      
REMARK 465     LYS C   505                                                      
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     ASP C 503    CG   OD1  OD2                                       
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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  5119     O    HOH A  5179              1.95            
REMARK 500   O    HOH C  5116     O    HOH C  5117              1.98            
REMARK 500   O    HOH C  5011     O    HOH C  5024              1.99            
REMARK 500   O    HOH A  5044     O    HOH A  5179              2.00            
REMARK 500   O    HOH B  5053     O    HOH B  5182              2.08            
REMARK 500   O    HOH B  5177     O    HOH B  5178              2.10            
REMARK 500   O    HOH A  5004     O    HOH A  5167              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU B 325   N   -  CA  -  C   ANGL. DEV. = -18.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 112       -8.12    -56.93                                   
REMARK 500    PRO A 133      166.69    -44.64                                   
REMARK 500    ALA A 157      154.88    -41.00                                   
REMARK 500    THR A 178      171.07    170.88                                   
REMARK 500    ARG A 203       -8.78    -47.35                                   
REMARK 500    TRP A 206      -19.98    -35.20                                   
REMARK 500    SER A 218       -5.16   -146.49                                   
REMARK 500    ASN A 236       33.51     37.56                                   
REMARK 500    SER A 251      -88.47   -110.55                                   
REMARK 500    CYS A 367       71.82   -155.47                                   
REMARK 500    ARG A 388     -126.44   -132.72                                   
REMARK 500    ASN A 390       72.23     30.01                                   
REMARK 500    THR A 403        6.36    -66.13                                   
REMARK 500    PRO A 467        6.27    -68.05                                   
REMARK 500    LEU A 485     -153.30   -121.05                                   
REMARK 500    GLU A 494      130.16    -39.52                                   
REMARK 500    HIS B  84      172.04    177.91                                   
REMARK 500    SER B 114      139.20   -172.63                                   
REMARK 500    ILE B 159      -60.87    -27.58                                   
REMARK 500    SER B 218        7.41   -152.57                                   
REMARK 500    SER B 251      -93.48   -109.29                                   
REMARK 500    TYR B 299       48.07     37.00                                   
REMARK 500    PHE B 302       57.81   -143.66                                   
REMARK 500    ASN B 354       31.51    -86.27                                   
REMARK 500    ARG B 388     -131.60   -119.57                                   
REMARK 500    GLU B 402       79.41    -69.07                                   
REMARK 500    THR B 403       21.28    -71.82                                   
REMARK 500    ALA B 407       -6.40    -56.48                                   
REMARK 500    SER B 453      -76.55    -65.74                                   
REMARK 500    CYS B 457       92.18   -173.73                                   
REMARK 500    SER B 471       -7.99    -52.68                                   
REMARK 500    LEU B 485     -162.85   -108.88                                   
REMARK 500    PRO B 487      172.93    -56.02                                   
REMARK 500    HIS C 101       -2.11    -59.77                                   
REMARK 500    TRP C 206      -39.73    -31.19                                   
REMARK 500    SER C 218       -4.29   -148.71                                   
REMARK 500    ASN C 236       27.79     40.95                                   
REMARK 500    SER C 251      -83.41   -108.24                                   
REMARK 500    GLN C 271       95.35    -65.68                                   
REMARK 500    SER C 276      174.04    -49.14                                   
REMARK 500    ASP C 292        3.62    -66.75                                   
REMARK 500    LYS C 335      -42.30   -139.04                                   
REMARK 500    CYS C 367       85.60   -157.48                                   
REMARK 500    ARG C 388     -140.52   -134.98                                   
REMARK 500    ALA C 407        2.85    -55.75                                   
REMARK 500    ILE C 433      148.52   -170.08                                   
REMARK 500    SER C 453      -73.49    -92.52                                   
REMARK 500    CYS C 457      107.69   -162.99                                   
REMARK 500    LEU C 485     -157.91   -118.39                                   
REMARK 500    GLU C 494      110.98    -34.69                                   
REMARK 500    HIS D 101       -3.86    -51.89                                   
REMARK 500    THR D 178      170.09    171.12                                   
REMARK 500    TRP D 206       -9.48    -53.67                                   
REMARK 500    SER D 218       -2.07   -147.27                                   
REMARK 500    ASN D 237       -0.52     66.03                                   
REMARK 500    ILE D 240      150.90    -41.77                                   
REMARK 500    SER D 251      -94.53   -113.49                                   
REMARK 500    SER D 276      158.69    -45.52                                   
REMARK 500    PRO D 281       -3.07    -56.89                                   
REMARK 500    PRO D 323      -35.40    -36.67                                   
REMARK 500    TYR D 336       98.66    -64.72                                   
REMARK 500    PRO D 365       -9.21    -57.74                                   
REMARK 500    ARG D 388     -135.85   -123.41                                   
REMARK 500    ASN D 390       68.10     29.57                                   
REMARK 500    THR D 403       14.06    -68.01                                   
REMARK 500    ALA D 407       -9.84    -52.21                                   
REMARK 500    LEU D 485     -164.16   -120.90                                   
REMARK 500    HIS D 499      152.99    -49.74                                   
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 C5020        DISTANCE =  5.78 ANGSTROMS                       
REMARK 525    HOH D5042        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH A5061        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH D5110        DISTANCE =  7.04 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 A1903  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 110   SG                                                     
REMARK 620 2 CYS A 115   SG  109.3                                              
REMARK 620 3 CYS B 110   SG  120.1 114.8                                        
REMARK 620 4 CYS B 115   SG  107.9 103.9  98.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C3903  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 110   SG                                                     
REMARK 620 2 CYS C 115   SG  109.1                                              
REMARK 620 3 CYS D 110   SG  123.8 102.2                                        
REMARK 620 4 CYS D 115   SG  115.9 100.6 102.2                                  
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 HEC A1901                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B A1902                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1903                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A1904                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B2901                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B B2902                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD B2904                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC C3901                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B C3902                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C3903                  
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD C3904                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC D4901                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B D4902                 
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD D4904                 
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                                   
REMARK 900 RELATED ID: 3E7G   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3E7I   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3E7M   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3E7S   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3E7T   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EAH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EAI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EBD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EBF   RELATED DB: PDB                                   
DBREF  3EJ8 A   82   505  UNP    P35228   NOS2A_HUMAN     82    505             
DBREF  3EJ8 B   82   505  UNP    P35228   NOS2A_HUMAN     82    505             
DBREF  3EJ8 C   82   505  UNP    P35228   NOS2A_HUMAN     82    505             
DBREF  3EJ8 D   82   505  UNP    P35228   NOS2A_HUMAN     82    505             
SEQADV 3EJ8 ILE A  286  UNP  P35228    PHE   286 ENGINEERED                     
SEQADV 3EJ8 LEU A  305  UNP  P35228    VAL   305 ENGINEERED                     
SEQADV 3EJ8 ILE B  286  UNP  P35228    PHE   286 ENGINEERED                     
SEQADV 3EJ8 LEU B  305  UNP  P35228    VAL   305 ENGINEERED                     
SEQADV 3EJ8 ILE C  286  UNP  P35228    PHE   286 ENGINEERED                     
SEQADV 3EJ8 LEU C  305  UNP  P35228    VAL   305 ENGINEERED                     
SEQADV 3EJ8 ILE D  286  UNP  P35228    PHE   286 ENGINEERED                     
SEQADV 3EJ8 LEU D  305  UNP  P35228    VAL   305 ENGINEERED                     
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 ILE 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 LEU 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 ILE 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 LEU 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 ILE 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 LEU 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 ILE 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 LEU 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    HEC  A1901      43                                                       
HET    H4B  A1902      17                                                       
HET     ZN  A1903       1                                                       
HET    IMD  A1904       5                                                       
HET    HEC  B2901      43                                                       
HET    H4B  B2902      17                                                       
HET    IMD  B2904       5                                                       
HET    HEC  C3901      43                                                       
HET    H4B  C3902      17                                                       
HET     ZN  C3903       1                                                       
HET    IMD  C3904       5                                                       
HET    HEC  D4901      43                                                       
HET    H4B  D4902      17                                                       
HET    IMD  D4904       5                                                       
HETNAM     HEC HEME C                                                           
HETNAM     H4B 5,6,7,8-TETRAHYDROBIOPTERIN                                      
HETNAM      ZN ZINC ION                                                         
HETNAM     IMD IMIDAZOLE                                                        
FORMUL   5  HEC    4(C34 H34 FE N4 O4)                                          
FORMUL   6  H4B    4(C9 H15 N5 O3)                                              
FORMUL   7   ZN    2(ZN 2+)                                                     
FORMUL   8  IMD    4(C3 H5 N2 1+)                                               
FORMUL  19  HOH   *193(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  GLY A  177  1                                  20    
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 TRP A  338  GLU A  343  5                                   6    
HELIX   12  12 GLY A  375  VAL A  380  1                                   6    
HELIX   13  13 ILE A  391  GLY A  400  1                                  10    
HELIX   14  14 LYS A  405  SER A  408  5                                   4    
HELIX   15  15 LEU A  409  GLN A  429  1                                  21    
HELIX   16  16 ASP A  435  GLY A  455  1                                  21    
HELIX   17  17 ASP A  460  VAL A  465  1                                   6    
HELIX   18  18 SER A  469  GLN A  478  5                                  10    
HELIX   19  19 GLU A  494  HIS A  499  1                                   6    
HELIX   20  20 THR B   99  ALA B  104  5                                   6    
HELIX   21  21 PRO B  135  GLY B  152  1                                  18    
HELIX   22  22 LYS B  158  GLY B  177  1                                  20    
HELIX   23  23 THR B  182  ASN B  196  1                                  15    
HELIX   24  24 GLY B  202  TRP B  206  5                                   5    
HELIX   25  25 THR B  219  ASN B  236  1                                  18    
HELIX   26  26 ASN B  237  ASN B  239  5                                   3    
HELIX   27  27 ASN B  283  LEU B  293  1                                  11    
HELIX   28  28 TRP B  338  GLU B  343  5                                   6    
HELIX   29  29 MET B  374  VAL B  380  1                                   7    
HELIX   30  30 VAL B  380  ASP B  385  1                                   6    
HELIX   31  31 ILE B  391  MET B  399  1                                   9    
HELIX   32  32 LYS B  405  SER B  408  5                                   4    
HELIX   33  33 LEU B  409  GLN B  429  1                                  21    
HELIX   34  34 ASP B  435  GLY B  455  1                                  21    
HELIX   35  35 ASP B  460  VAL B  465  1                                   6    
HELIX   36  36 SER B  469  GLN B  478  5                                  10    
HELIX   37  37 GLU B  494  HIS B  499  1                                   6    
HELIX   38  38 THR C   99  LYS C  103  5                                   5    
HELIX   39  39 PRO C  122  THR C  126  5                                   5    
HELIX   40  40 PRO C  135  GLY C  152  1                                  18    
HELIX   41  41 LYS C  158  GLY C  177  1                                  20    
HELIX   42  42 THR C  182  ASN C  196  1                                  15    
HELIX   43  43 GLY C  202  TRP C  206  5                                   5    
HELIX   44  44 THR C  219  ASN C  236  1                                  18    
HELIX   45  45 ASN C  237  ASN C  239  5                                   3    
HELIX   46  46 ASN C  283  ASP C  292  1                                  10    
HELIX   47  47 PRO C  322  VAL C  326  5                                   5    
HELIX   48  48 PHE C  339  GLU C  343  5                                   5    
HELIX   49  49 MET C  374  VAL C  380  1                                   7    
HELIX   50  50 ILE C  391  MET C  399  1                                   9    
HELIX   51  51 LYS C  405  SER C  408  5                                   4    
HELIX   52  52 LEU C  409  GLN C  429  1                                  21    
HELIX   53  53 ASP C  435  ARG C  454  1                                  20    
HELIX   54  54 ASP C  460  VAL C  465  1                                   6    
HELIX   55  55 THR C  473  GLN C  478  5                                   6    
HELIX   56  56 GLU C  494  HIS C  499  1                                   6    
HELIX   57  57 THR D   99  LYS D  103  5                                   5    
HELIX   58  58 PRO D  122  THR D  126  5                                   5    
HELIX   59  59 PRO D  135  GLY D  152  1                                  18    
HELIX   60  60 LYS D  158  GLY D  177  1                                  20    
HELIX   61  61 THR D  182  ASN D  196  1                                  15    
HELIX   62  62 GLY D  202  TRP D  206  5                                   5    
HELIX   63  63 THR D  219  ASN D  236  1                                  18    
HELIX   64  64 ASN D  237  ASN D  239  5                                   3    
HELIX   65  65 ASN D  283  LEU D  293  1                                  11    
HELIX   66  66 PRO D  322  VAL D  326  5                                   5    
HELIX   67  67 TRP D  338  GLU D  343  5                                   6    
HELIX   68  68 GLY D  375  VAL D  380  1                                   6    
HELIX   69  69 VAL D  380  ASP D  385  1                                   6    
HELIX   70  70 ILE D  391  MET D  399  1                                   9    
HELIX   71  71 LYS D  405  SER D  408  5                                   4    
HELIX   72  72 LEU D  409  GLN D  429  1                                  21    
HELIX   73  73 ASP D  435  GLY D  455  1                                  21    
HELIX   74  74 ASP D  460  VAL D  465  1                                   6    
HELIX   75  75 SER D  469  GLN D  478  5                                  10    
HELIX   76  76 GLU D  494  HIS D  499  1                                   6    
SHEET    1   A 2 VAL A  85  LYS A  88  0                                        
SHEET    2   A 2 THR A  95  ASP A  98 -1  O  ASP A  98   N  VAL A  85           
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 TYR A 373  MET A 374  0                                        
SHEET    2   G 2 ILE A 433  MET A 434  1  O  MET A 434   N  TYR A 373           
SHEET    1   H 2 VAL B  85  LYS B  88  0                                        
SHEET    2   H 2 THR B  95  ASP B  98 -1  O  ASP B  98   N  VAL B  85           
SHEET    1   I 4 GLN B 210  ASP B 213  0                                        
SHEET    2   I 4 ALA B 243  VAL B 246  1  O  ILE B 244   N  PHE B 212           
SHEET    3   I 4 PHE B 369  ASN B 370 -1  O  ASN B 370   N  ALA B 243           
SHEET    4   I 4 ALA B 351  VAL B 352 -1  N  VAL B 352   O  PHE B 369           
SHEET    1   J 3 ARG B 258  VAL B 259  0                                        
SHEET    2   J 3 LEU B 307  GLN B 310 -1  O  GLN B 310   N  ARG B 258           
SHEET    3   J 3 GLU B 317  PHE B 319 -1  O  PHE B 319   N  LEU B 307           
SHEET    1   K 2 GLY B 269  GLN B 271  0                                        
SHEET    2   K 2 ILE B 277  GLY B 279 -1  O  ARG B 278   N  TYR B 270           
SHEET    1   L 2 GLU B 328  ALA B 330  0                                        
SHEET    2   L 2 LYS B 345  TYR B 347 -1  O  TRP B 346   N  VAL B 329           
SHEET    1   M 3 LEU B 362  PHE B 364  0                                        
SHEET    2   M 3 LEU B 356  VAL B 359 -1  N  LEU B 357   O  PHE B 364           
SHEET    3   M 3 PHE B 488  TYR B 490 -1  O  TYR B 490   N  LEU B 356           
SHEET    1   N 2 VAL C  85  LYS C  88  0                                        
SHEET    2   N 2 THR C  95  ASP C  98 -1  O  PHE C  96   N  ILE C  87           
SHEET    1   O 2 GLN C 210  ASP C 213  0                                        
SHEET    2   O 2 ALA C 243  VAL C 246  1  O  ILE C 244   N  PHE C 212           
SHEET    1   P 3 ARG C 258  VAL C 259  0                                        
SHEET    2   P 3 LEU C 307  GLN C 310 -1  O  GLN C 310   N  ARG C 258           
SHEET    3   P 3 GLU C 317  PHE C 319 -1  O  PHE C 319   N  LEU C 307           
SHEET    1   Q 2 GLY C 269  GLN C 271  0                                        
SHEET    2   Q 2 ILE C 277  GLY C 279 -1  O  ARG C 278   N  TYR C 270           
SHEET    1   R 2 GLU C 328  ALA C 330  0                                        
SHEET    2   R 2 LYS C 345  TYR C 347 -1  O  TRP C 346   N  VAL C 329           
SHEET    1   S 2 ALA C 351  VAL C 352  0                                        
SHEET    2   S 2 PHE C 369  ASN C 370 -1  O  PHE C 369   N  VAL C 352           
SHEET    1   T 3 LEU C 362  PHE C 364  0                                        
SHEET    2   T 3 LEU C 356  VAL C 359 -1  N  LEU C 357   O  PHE C 364           
SHEET    3   T 3 PHE C 488  TYR C 490 -1  O  TYR C 490   N  LEU C 356           
SHEET    1   U 2 VAL D  85  LYS D  88  0                                        
SHEET    2   U 2 THR D  95  ASP D  98 -1  O  ASP D  98   N  VAL D  85           
SHEET    1   V 4 GLN D 210  ASP D 213  0                                        
SHEET    2   V 4 ALA D 243  VAL D 246  1  O  ILE D 244   N  PHE D 212           
SHEET    3   V 4 PHE D 369  ASN D 370 -1  O  ASN D 370   N  ALA D 243           
SHEET    4   V 4 ALA D 351  VAL D 352 -1  N  VAL D 352   O  PHE D 369           
SHEET    1   W 3 ARG D 258  VAL D 259  0                                        
SHEET    2   W 3 LEU D 307  GLN D 310 -1  O  GLN D 310   N  ARG D 258           
SHEET    3   W 3 GLU D 317  PHE D 319 -1  O  PHE D 319   N  LEU D 307           
SHEET    1   X 2 GLY D 269  GLN D 271  0                                        
SHEET    2   X 2 ILE D 277  GLY D 279 -1  O  ARG D 278   N  TYR D 270           
SHEET    1   Y 2 GLU D 328  ALA D 330  0                                        
SHEET    2   Y 2 LYS D 345  TYR D 347 -1  O  TRP D 346   N  VAL D 329           
SHEET    1   Z 3 LEU D 362  PHE D 364  0                                        
SHEET    2   Z 3 LEU D 356  VAL D 359 -1  N  VAL D 359   O  LEU D 362           
SHEET    3   Z 3 PHE D 488  TYR D 490 -1  O  TYR D 490   N  LEU D 356           
SHEET    1  AA 2 TYR D 373  MET D 374  0                                        
SHEET    2  AA 2 ILE D 433  MET D 434  1  O  MET D 434   N  TYR D 373           
LINK         SG  CYS A 110                ZN    ZN A1903     1555   1555  2.42  
LINK         SG  CYS A 115                ZN    ZN A1903     1555   1555  2.23  
LINK         SG  CYS A 200                FE   HEC A1901     1555   1555  2.53  
LINK         SG  CYS B 110                ZN    ZN A1903     1555   1555  2.32  
LINK         SG  CYS B 115                ZN    ZN A1903     1555   1555  2.38  
LINK         SG  CYS B 200                FE   HEC B2901     1555   1555  2.51  
LINK         SG  CYS C 110                ZN    ZN C3903     1555   1555  2.48  
LINK         SG  CYS C 115                ZN    ZN C3903     1555   1555  2.31  
LINK         SG  CYS C 200                FE   HEC C3901     1555   1555  2.53  
LINK         SG  CYS D 110                ZN    ZN C3903     1555   1555  2.31  
LINK         SG  CYS D 115                ZN    ZN C3903     1555   1555  2.25  
LINK         SG  CYS D 200                FE   HEC D4901     1555   1555  2.42  
CISPEP   1 SER A  486    PRO A  487          0         0.12                     
CISPEP   2 SER B  486    PRO B  487          0         0.00                     
CISPEP   3 SER C  486    PRO C  487          0         0.27                     
CISPEP   4 SER D  486    PRO D  487          0         0.14                     
SITE     1 AC1 15 TRP A 194  ARG A 199  CYS A 200  GLN A 205                    
SITE     2 AC1 15 SER A 242  PHE A 369  ASN A 370  GLY A 371                    
SITE     3 AC1 15 TRP A 372  GLU A 377  TRP A 463  TYR A 489                    
SITE     4 AC1 15 TYR A 491  H4B A1902  IMD A1904                               
SITE     1 AC2 11 SER A 118  MET A 120  ARG A 381  ILE A 462                    
SITE     2 AC2 11 TRP A 463  HEC A1901  HOH A5031  TRP B 461                    
SITE     3 AC2 11 PHE B 476  HIS B 477  GLN B 478                               
SITE     1 AC3  4 CYS A 110  CYS A 115  CYS B 110  CYS B 115                    
SITE     1 AC4  3 TRP A 372  GLU A 377  HEC A1901                               
SITE     1 AC5 13 TRP B 194  CYS B 200  GLN B 205  PHE B 369                    
SITE     2 AC5 13 GLY B 371  TRP B 372  GLU B 377  MET B 434                    
SITE     3 AC5 13 TRP B 463  TYR B 489  TYR B 491  H4B B2902                    
SITE     4 AC5 13 IMD B2904                                                     
SITE     1 AC6 10 TRP A 461  PHE A 476  HIS A 477  GLN A 478                    
SITE     2 AC6 10 SER B 118  MET B 120  ARG B 381  ILE B 462                    
SITE     3 AC6 10 TRP B 463  HEC B2901                                          
SITE     1 AC7  2 GLU B 377  HEC B2901                                          
SITE     1 AC8 16 TRP C 194  ARG C 199  CYS C 200  GLY C 202                    
SITE     2 AC8 16 GLN C 205  MET C 355  PHE C 369  ASN C 370                    
SITE     3 AC8 16 GLY C 371  TRP C 372  GLU C 377  TRP C 463                    
SITE     4 AC8 16 TYR C 489  TYR C 491  H4B C3902  IMD C3904                    
SITE     1 AC9  8 SER C 118  MET C 120  ARG C 381  ILE C 462                    
SITE     2 AC9  8 TRP C 463  HEC C3901  TRP D 461  PHE D 476                    
SITE     1 BC1  4 CYS C 110  CYS C 115  CYS D 110  CYS D 115                    
SITE     1 BC2  2 GLU C 377  HEC C3901                                          
SITE     1 BC3 12 TRP D 194  CYS D 200  GLN D 205  PHE D 369                    
SITE     2 BC3 12 GLY D 371  TRP D 372  GLU D 377  TRP D 463                    
SITE     3 BC3 12 TYR D 489  TYR D 491  H4B D4902  IMD D4904                    
SITE     1 BC4 12 TRP C  90  TRP C 461  PHE C 476  HIS C 477                    
SITE     2 BC4 12 GLN C 478  SER D 118  MET D 120  ARG D 381                    
SITE     3 BC4 12 ILE D 462  TRP D 463  HEC D4901  HOH D5166                    
SITE     1 BC5  3 GLU D 377  HEC D4901  HOH D5071                               
CRYST1   89.883  150.710  191.047  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      0.011126  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006635  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005234        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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