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Database: PDB
Entry: 6AV2
LinkDB: 6AV2
Original site: 6AV2 
HEADER    OXIDOREDUCTASE                          01-SEP-17   6AV2              
TITLE     STRUCTURE OF HUMAN NEURONAL NITRIC OXIDE SYNTHASE R354A/G357D MUTANT  
TITLE    2 HEME DOMAIN IN COMPLEX WITH 6-(3-(3-(DIMETHYLAMINO)PROPYL)-5-        
TITLE    3 (TRIFLUOROMETHYL)PHENETHYL)-4-METHYLPYRIDIN-2-AMINE                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NITRIC OXIDE SYNTHASE, BRAIN;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 302-722;                                      
COMPND   5 SYNONYM: CONSTITUTIVE NOS,NC-NOS,NOS TYPE I,NEURONAL NOS,NNOS,       
COMPND   6 PEPTIDYL-CYSTEINE S-NITROSYLASE NOS1,BNOS;                           
COMPND   7 EC: 1.14.13.39;                                                      
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 OTHER_DETAILS: RESIDUES 344 TO 351 ARE DISORDERED                    
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ORGAN: BRAIN;                                                        
SOURCE   6 GENE: NOS1;                                                          
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PCWORI                                    
KEYWDS    NITRIC OXIDE SYNTHASE INHIBITOR COMPLEX HEME ENZYME, OXIDOREDUCTASE   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.LI,T.L.POULOS                                                       
REVDAT   3   25-DEC-19 6AV2    1       REMARK                                   
REVDAT   2   20-FEB-19 6AV2    1       REMARK                                   
REVDAT   1   11-JUL-18 6AV2    0                                                
JRNL        AUTH   H.T.DO,H.Y.WANG,H.LI,G.CHREIFI,T.L.POULOS,R.B.SILVERMAN      
JRNL        TITL   IMPROVEMENT OF CELL PERMEABILITY OF HUMAN NEURONAL NITRIC    
JRNL        TITL 2 OXIDE SYNTHASE INHIBITORS USING POTENT AND SELECTIVE         
JRNL        TITL 3 2-AMINOPYRIDINE-BASED SCAFFOLDS WITH A FLUOROBENZENE LINKER. 
JRNL        REF    J. MED. CHEM.                 V.  60  9360 2017              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   29091437                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.7B01356                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.2_1309                                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.17                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.260                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 60724                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.860                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2955                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 50.1870 -  6.5206    0.99     3730   161  0.1470 0.1644        
REMARK   3     2  6.5206 -  5.1773    0.99     3731   179  0.1552 0.1904        
REMARK   3     3  5.1773 -  4.5233    0.99     3728   189  0.1225 0.1673        
REMARK   3     4  4.5233 -  4.1100    0.99     3712   186  0.1247 0.1496        
REMARK   3     5  4.1100 -  3.8155    0.99     3705   191  0.1348 0.1884        
REMARK   3     6  3.8155 -  3.5906    0.99     3689   216  0.1454 0.2017        
REMARK   3     7  3.5906 -  3.4108    0.98     3691   189  0.1546 0.1876        
REMARK   3     8  3.4108 -  3.2624    0.98     3642   206  0.1586 0.2187        
REMARK   3     9  3.2624 -  3.1368    0.98     3745   169  0.1721 0.2226        
REMARK   3    10  3.1368 -  3.0286    0.98     3686   184  0.1832 0.2777        
REMARK   3    11  3.0286 -  2.9339    0.98     3698   187  0.1758 0.2373        
REMARK   3    12  2.9339 -  2.8500    0.98     3732   188  0.1890 0.2229        
REMARK   3    13  2.8500 -  2.7750    0.98     3652   160  0.1832 0.2365        
REMARK   3    14  2.7750 -  2.7073    0.98     3708   167  0.1883 0.2306        
REMARK   3    15  2.7073 -  2.6458    0.97     3636   204  0.2110 0.2450        
REMARK   3    16  2.6458 -  2.5895    0.98     3656   200  0.2026 0.2581        
REMARK   3    17  2.5895 -  2.5377    0.98     3720   195  0.2040 0.2391        
REMARK   3    18  2.5377 -  2.4898    0.97     3588   206  0.2119 0.2721        
REMARK   3    19  2.4898 -  2.4453    0.98     3705   203  0.2381 0.2957        
REMARK   3    20  2.4453 -  2.4039    0.98     3651   197  0.2445 0.3194        
REMARK   3    21  2.4039 -  2.3651    0.97     3634   211  0.2406 0.2897        
REMARK   3    22  2.3651 -  2.3287    0.97     3638   212  0.2529 0.2663        
REMARK   3    23  2.3287 -  2.2945    0.97     3686   174  0.2610 0.2943        
REMARK   3    24  2.2945 -  2.2621    0.97     3664   175  0.2898 0.3411        
REMARK   3    25  2.2621 -  2.2316    0.95     3623   182  0.3789 0.4110        
REMARK   3    26  2.2316 -  2.2026    0.97     3593   166  0.3163 0.3790        
REMARK   3    27  2.2026 -  2.1751    0.97     3613   191  0.3105 0.3414        
REMARK   3    28  2.1751 -  2.1489    0.97     3724   165  0.3050 0.3152        
REMARK   3    29  2.1489 -  2.1239    0.97     3665   186  0.3243 0.3408        
REMARK   3    30  2.1239 -  2.1000    0.97     3584   187  0.3462 0.3937        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.080           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           7116                                  
REMARK   3   ANGLE     :  1.161           9694                                  
REMARK   3   CHIRALITY :  0.071           1003                                  
REMARK   3   PLANARITY :  0.004           1224                                  
REMARK   3   DIHEDRAL  : 15.445           2594                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 302:721)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 117.1539 247.8534 361.1810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1547 T22:   0.2224                                     
REMARK   3      T33:   0.2392 T12:  -0.0121                                     
REMARK   3      T13:   0.0360 T23:   0.0526                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7269 L22:   1.0117                                     
REMARK   3      L33:   2.4615 L12:  -0.1386                                     
REMARK   3      L13:  -0.0695 L23:   0.2289                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0056 S12:  -0.0322 S13:  -0.0018                       
REMARK   3      S21:  -0.0458 S22:  -0.0810 S23:  -0.0221                       
REMARK   3      S31:   0.1238 S32:   0.0957 S33:   0.0756                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 304:721)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 115.8342 246.7210 323.9429              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2287 T22:   0.2915                                     
REMARK   3      T33:   0.2713 T12:   0.0048                                     
REMARK   3      T13:   0.0274 T23:  -0.0377                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6128 L22:   0.7953                                     
REMARK   3      L33:   3.5957 L12:  -0.2961                                     
REMARK   3      L13:  -0.3009 L23:   0.3751                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0606 S12:   0.1166 S13:  -0.0194                       
REMARK   3      S21:  -0.0388 S22:  -0.1369 S23:   0.0926                       
REMARK   3      S31:   0.0111 S32:  -0.3236 S33:   0.0541                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6AV2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-SEP-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000223180.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-OCT-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM 7.1.0                      
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.3.11                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60809                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 51.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.14800                            
REMARK 200  R SYM                      (I) : 0.14800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.5000                             
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     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.68900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: REFMAC 5.8.0049                                       
REMARK 200 STARTING MODEL: 4UH5                                                 
REMARK 200                                                                      
REMARK 200 REMARK: PLATE                                                        
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG3350 35MM CITRIC ACID 65MM BIS     
REMARK 280  -TRIS-PROPANE 10% GLYCEROL 5MM TCEP, PH 7.2, VAPOR DIFFUSION,       
REMARK 280  SITTING DROP, TEMPERATURE 277K                                      
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       26.10500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       82.63500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       60.74500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       82.63500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.10500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       60.74500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9340 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.0 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 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     SER A   344                                                      
REMARK 465     GLN A   345                                                      
REMARK 465     HIS A   346                                                      
REMARK 465     ALA A   347                                                      
REMARK 465     ARG A   348                                                      
REMARK 465     ARG A   349                                                      
REMARK 465     PRO A   350                                                      
REMARK 465     GLU A   351                                                      
REMARK 465     CYS B   302                                                      
REMARK 465     PRO B   303                                                      
REMARK 465     GLN B   345                                                      
REMARK 465     HIS B   346                                                      
REMARK 465     ALA B   347                                                      
REMARK 465     ARG B   348                                                      
REMARK 465     ARG B   349                                                      
REMARK 465     PRO B   350                                                      
REMARK 465     GLU B   351                                                      
REMARK 465     ASP B   352                                                      
REMARK 465     VAL B   353                                                      
REMARK 465     LYS B   722                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A 314       -6.61     66.57                                   
REMARK 500    THR A 471      -84.55   -110.70                                   
REMARK 500    ARG A 608     -134.63   -119.10                                   
REMARK 500    CYS A 677      101.00   -162.46                                   
REMARK 500    THR B 471      -78.96   -113.33                                   
REMARK 500    LYS B 555      -30.82   -130.94                                   
REMARK 500    CYS B 587       59.57   -146.85                                   
REMARK 500    ARG B 608     -133.51   -122.18                                   
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 B1084        DISTANCE =  6.14 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 804  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 331   SG                                                     
REMARK 620 2 CYS A 336   SG  108.2                                              
REMARK 620 3 CYS B 331   SG  123.1 104.4                                        
REMARK 620 4 CYS B 336   SG  103.2  98.8 116.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 801  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 420   SG                                                     
REMARK 620 2 HEM A 801   NA   98.5                                              
REMARK 620 3 HEM A 801   NB  101.3  85.5                                        
REMARK 620 4 HEM A 801   NC  102.3 159.1  90.6                                  
REMARK 620 5 HEM A 801   ND  100.2  90.2 158.5  86.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 801  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 420   SG                                                     
REMARK 620 2 HEM B 801   NA  100.2                                              
REMARK 620 3 HEM B 801   NB  100.4  84.8                                        
REMARK 620 4 HEM B 801   NC   97.7 162.1  90.6                                  
REMARK 620 5 HEM B 801   ND  100.2  92.5 159.5  85.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BY7 A 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 804                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B B 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BY7 B 803                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6AUR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6AUT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6AUQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6AUS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6AUZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6AV1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6AUY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6AV0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6AV6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6AV7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6AUU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6AUV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6AUW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6AUX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6AV3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6AV4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6AV5   RELATED DB: PDB                                   
DBREF  6AV2 A  302   722  UNP    P29475   NOS1_HUMAN     302    722             
DBREF  6AV2 B  302   722  UNP    P29475   NOS1_HUMAN     302    722             
SEQADV 6AV2 ALA A  354  UNP  P29475    ARG   354 ENGINEERED MUTATION            
SEQADV 6AV2 ASP A  357  UNP  P29475    GLY   357 ENGINEERED MUTATION            
SEQADV 6AV2 ALA B  354  UNP  P29475    ARG   354 ENGINEERED MUTATION            
SEQADV 6AV2 ASP B  357  UNP  P29475    GLY   357 ENGINEERED MUTATION            
SEQRES   1 A  421  CYS PRO ARG PHE LEU LYS VAL LYS ASN TRP GLU THR GLU          
SEQRES   2 A  421  VAL VAL LEU THR ASP THR LEU HIS LEU LYS SER THR LEU          
SEQRES   3 A  421  GLU THR GLY CYS THR GLU TYR ILE CYS MET GLY SER ILE          
SEQRES   4 A  421  MET HIS PRO SER GLN HIS ALA ARG ARG PRO GLU ASP VAL          
SEQRES   5 A  421  ALA THR LYS ASP GLN LEU PHE PRO LEU ALA LYS GLU PHE          
SEQRES   6 A  421  ILE ASP GLN TYR TYR SER SER ILE LYS ARG PHE GLY SER          
SEQRES   7 A  421  LYS ALA HIS MET GLU ARG LEU GLU GLU VAL ASN LYS GLU          
SEQRES   8 A  421  ILE ASP THR THR SER THR TYR GLN LEU LYS ASP THR GLU          
SEQRES   9 A  421  LEU ILE TYR GLY ALA LYS HIS ALA TRP ARG ASN ALA SER          
SEQRES  10 A  421  ARG CYS VAL GLY ARG ILE GLN TRP SER LYS LEU GLN VAL          
SEQRES  11 A  421  PHE ASP ALA ARG ASP CYS THR THR ALA HIS GLY MET PHE          
SEQRES  12 A  421  ASN TYR ILE CYS ASN HIS VAL LYS TYR ALA THR ASN LYS          
SEQRES  13 A  421  GLY ASN LEU ARG SER ALA ILE THR ILE PHE PRO GLN ARG          
SEQRES  14 A  421  THR ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN SER GLN          
SEQRES  15 A  421  LEU ILE ARG TYR ALA GLY TYR LYS GLN PRO ASP GLY SER          
SEQRES  16 A  421  THR LEU GLY ASP PRO ALA ASN VAL GLN PHE THR GLU ILE          
SEQRES  17 A  421  CYS ILE GLN GLN GLY TRP LYS PRO PRO ARG GLY ARG PHE          
SEQRES  18 A  421  ASP VAL LEU PRO LEU LEU LEU GLN ALA ASN GLY ASN ASP          
SEQRES  19 A  421  PRO GLU LEU PHE GLN ILE PRO PRO GLU LEU VAL LEU GLU          
SEQRES  20 A  421  VAL PRO ILE ARG HIS PRO LYS PHE GLU TRP PHE LYS ASP          
SEQRES  21 A  421  LEU GLY LEU LYS TRP TYR GLY LEU PRO ALA VAL SER ASN          
SEQRES  22 A  421  MET LEU LEU GLU ILE GLY GLY LEU GLU PHE SER ALA CYS          
SEQRES  23 A  421  PRO PHE SER GLY TRP TYR MET GLY THR GLU ILE GLY VAL          
SEQRES  24 A  421  ARG ASP TYR CYS ASP ASN SER ARG TYR ASN ILE LEU GLU          
SEQRES  25 A  421  GLU VAL ALA LYS LYS MET ASN LEU ASP MET ARG LYS THR          
SEQRES  26 A  421  SER SER LEU TRP LYS ASP GLN ALA LEU VAL GLU ILE ASN          
SEQRES  27 A  421  ILE ALA VAL LEU TYR SER PHE GLN SER ASP LYS VAL THR          
SEQRES  28 A  421  ILE VAL ASP HIS HIS SER ALA THR GLU SER PHE ILE LYS          
SEQRES  29 A  421  HIS MET GLU ASN GLU TYR ARG CYS ARG GLY GLY CYS PRO          
SEQRES  30 A  421  ALA ASP TRP VAL TRP ILE VAL PRO PRO MET SER GLY SER          
SEQRES  31 A  421  ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR ARG          
SEQRES  32 A  421  LEU THR PRO SER PHE GLU TYR GLN PRO ASP PRO TRP ASN          
SEQRES  33 A  421  THR HIS VAL TRP LYS                                          
SEQRES   1 B  421  CYS PRO ARG PHE LEU LYS VAL LYS ASN TRP GLU THR GLU          
SEQRES   2 B  421  VAL VAL LEU THR ASP THR LEU HIS LEU LYS SER THR LEU          
SEQRES   3 B  421  GLU THR GLY CYS THR GLU TYR ILE CYS MET GLY SER ILE          
SEQRES   4 B  421  MET HIS PRO SER GLN HIS ALA ARG ARG PRO GLU ASP VAL          
SEQRES   5 B  421  ALA THR LYS ASP GLN LEU PHE PRO LEU ALA LYS GLU PHE          
SEQRES   6 B  421  ILE ASP GLN TYR TYR SER SER ILE LYS ARG PHE GLY SER          
SEQRES   7 B  421  LYS ALA HIS MET GLU ARG LEU GLU GLU VAL ASN LYS GLU          
SEQRES   8 B  421  ILE ASP THR THR SER THR TYR GLN LEU LYS ASP THR GLU          
SEQRES   9 B  421  LEU ILE TYR GLY ALA LYS HIS ALA TRP ARG ASN ALA SER          
SEQRES  10 B  421  ARG CYS VAL GLY ARG ILE GLN TRP SER LYS LEU GLN VAL          
SEQRES  11 B  421  PHE ASP ALA ARG ASP CYS THR THR ALA HIS GLY MET PHE          
SEQRES  12 B  421  ASN TYR ILE CYS ASN HIS VAL LYS TYR ALA THR ASN LYS          
SEQRES  13 B  421  GLY ASN LEU ARG SER ALA ILE THR ILE PHE PRO GLN ARG          
SEQRES  14 B  421  THR ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN SER GLN          
SEQRES  15 B  421  LEU ILE ARG TYR ALA GLY TYR LYS GLN PRO ASP GLY SER          
SEQRES  16 B  421  THR LEU GLY ASP PRO ALA ASN VAL GLN PHE THR GLU ILE          
SEQRES  17 B  421  CYS ILE GLN GLN GLY TRP LYS PRO PRO ARG GLY ARG PHE          
SEQRES  18 B  421  ASP VAL LEU PRO LEU LEU LEU GLN ALA ASN GLY ASN ASP          
SEQRES  19 B  421  PRO GLU LEU PHE GLN ILE PRO PRO GLU LEU VAL LEU GLU          
SEQRES  20 B  421  VAL PRO ILE ARG HIS PRO LYS PHE GLU TRP PHE LYS ASP          
SEQRES  21 B  421  LEU GLY LEU LYS TRP TYR GLY LEU PRO ALA VAL SER ASN          
SEQRES  22 B  421  MET LEU LEU GLU ILE GLY GLY LEU GLU PHE SER ALA CYS          
SEQRES  23 B  421  PRO PHE SER GLY TRP TYR MET GLY THR GLU ILE GLY VAL          
SEQRES  24 B  421  ARG ASP TYR CYS ASP ASN SER ARG TYR ASN ILE LEU GLU          
SEQRES  25 B  421  GLU VAL ALA LYS LYS MET ASN LEU ASP MET ARG LYS THR          
SEQRES  26 B  421  SER SER LEU TRP LYS ASP GLN ALA LEU VAL GLU ILE ASN          
SEQRES  27 B  421  ILE ALA VAL LEU TYR SER PHE GLN SER ASP LYS VAL THR          
SEQRES  28 B  421  ILE VAL ASP HIS HIS SER ALA THR GLU SER PHE ILE LYS          
SEQRES  29 B  421  HIS MET GLU ASN GLU TYR ARG CYS ARG GLY GLY CYS PRO          
SEQRES  30 B  421  ALA ASP TRP VAL TRP ILE VAL PRO PRO MET SER GLY SER          
SEQRES  31 B  421  ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR ARG          
SEQRES  32 B  421  LEU THR PRO SER PHE GLU TYR GLN PRO ASP PRO TRP ASN          
SEQRES  33 B  421  THR HIS VAL TRP LYS                                          
HET    HEM  A 801      43                                                       
HET    H4B  A 802      17                                                       
HET    BY7  A 803      26                                                       
HET     ZN  A 804       1                                                       
HET    HEM  B 801      43                                                       
HET    H4B  B 802      17                                                       
HET    BY7  B 803      26                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     H4B 5,6,7,8-TETRAHYDROBIOPTERIN                                      
HETNAM     BY7 6-(2-{3-[3-(DIMETHYLAMINO)PROPYL]-5-(TRIFLUOROMETHYL)            
HETNAM   2 BY7  PHENYL}ETHYL)-4-METHYLPYRIDIN-2-AMINE                           
HETNAM      ZN ZINC ION                                                         
HETSYN     HEM HEME                                                             
FORMUL   3  HEM    2(C34 H32 FE N4 O4)                                          
FORMUL   4  H4B    2(C9 H15 N5 O3)                                              
FORMUL   5  BY7    2(C20 H26 F3 N3)                                             
FORMUL   6   ZN    ZN 2+                                                        
FORMUL  10  HOH   *407(H2 O)                                                    
HELIX    1 AA1 THR A  320  SER A  325  5                                   6    
HELIX    2 AA2 THR A  355  ILE A  374  1                                  20    
HELIX    3 AA3 SER A  379  SER A  397  1                                  19    
HELIX    4 AA4 LYS A  402  ASN A  416  1                                  15    
HELIX    5 AA5 GLY A  422  TRP A  426  5                                   5    
HELIX    6 AA6 THR A  439  ASN A  456  1                                  18    
HELIX    7 AA7 LYS A  457  ASN A  459  5                                   3    
HELIX    8 AA8 ASN A  503  GLN A  513  1                                  11    
HELIX    9 AA9 PRO A  542  VAL A  546  5                                   5    
HELIX   10 AB1 PHE A  556  GLY A  563  5                                   8    
HELIX   11 AB2 GLY A  595  VAL A  600  1                                   6    
HELIX   12 AB3 VAL A  600  ASP A  605  1                                   6    
HELIX   13 AB4 ILE A  611  MET A  619  1                                   9    
HELIX   14 AB5 LYS A  625  SER A  628  5                                   4    
HELIX   15 AB6 LEU A  629  ASP A  649  1                                  21    
HELIX   16 AB7 ASP A  655  ARG A  674  1                                  20    
HELIX   17 AB8 ASP A  680  VAL A  685  1                                   6    
HELIX   18 AB9 SER A  689  THR A  693  5                                   5    
HELIX   19 AC1 ASP A  714  HIS A  719  1                                   6    
HELIX   20 AC2 THR B  320  SER B  325  5                                   6    
HELIX   21 AC3 THR B  355  ILE B  374  1                                  20    
HELIX   22 AC4 SER B  379  SER B  397  1                                  19    
HELIX   23 AC5 LYS B  402  ASN B  416  1                                  15    
HELIX   24 AC6 GLY B  422  TRP B  426  5                                   5    
HELIX   25 AC7 THR B  439  ASN B  456  1                                  18    
HELIX   26 AC8 LYS B  457  ASN B  459  5                                   3    
HELIX   27 AC9 ASN B  503  GLN B  513  1                                  11    
HELIX   28 AD1 PRO B  542  VAL B  546  5                                   5    
HELIX   29 AD2 TRP B  558  GLY B  563  5                                   6    
HELIX   30 AD3 GLY B  595  VAL B  600  1                                   6    
HELIX   31 AD4 VAL B  600  ASP B  605  1                                   6    
HELIX   32 AD5 ILE B  611  MET B  619  1                                   9    
HELIX   33 AD6 LYS B  625  SER B  628  5                                   4    
HELIX   34 AD7 LEU B  629  ASP B  649  1                                  21    
HELIX   35 AD8 ASP B  655  GLY B  675  1                                  21    
HELIX   36 AD9 ASP B  680  VAL B  685  1                                   6    
HELIX   37 AE1 SER B  689  GLN B  698  5                                  10    
HELIX   38 AE2 ASP B  714  THR B  718  5                                   5    
SHEET    1 AA1 2 LEU A 306  LYS A 309  0                                        
SHEET    2 AA1 2 VAL A 316  ASP A 319 -1  O  ASP A 319   N  LEU A 306           
SHEET    1 AA2 4 GLN A 430  ASP A 433  0                                        
SHEET    2 AA2 4 ALA A 463  ILE A 466  1  O  ILE A 464   N  PHE A 432           
SHEET    3 AA2 4 PHE A 589  SER A 590 -1  O  SER A 590   N  ALA A 463           
SHEET    4 AA2 4 ALA A 571  VAL A 572 -1  N  VAL A 572   O  PHE A 589           
SHEET    1 AA3 3 ARG A 478  VAL A 479  0                                        
SHEET    2 AA3 3 LEU A 527  GLN A 530 -1  O  GLN A 530   N  ARG A 478           
SHEET    3 AA3 3 GLU A 537  PHE A 539 -1  O  PHE A 539   N  LEU A 527           
SHEET    1 AA4 2 GLY A 489  LYS A 491  0                                        
SHEET    2 AA4 2 THR A 497  GLY A 499 -1  O  LEU A 498   N  TYR A 490           
SHEET    1 AA5 2 GLU A 548  PRO A 550  0                                        
SHEET    2 AA5 2 LYS A 565  TYR A 567 -1  O  TRP A 566   N  VAL A 549           
SHEET    1 AA6 3 LEU A 582  PHE A 584  0                                        
SHEET    2 AA6 3 LEU A 576  ILE A 579 -1  N  LEU A 577   O  PHE A 584           
SHEET    3 AA6 3 SER A 708  GLU A 710 -1  O  SER A 708   N  GLU A 578           
SHEET    1 AA7 2 TYR A 593  MET A 594  0                                        
SHEET    2 AA7 2 ILE A 653  VAL A 654  1  O  VAL A 654   N  TYR A 593           
SHEET    1 AA8 2 LEU B 306  LYS B 309  0                                        
SHEET    2 AA8 2 VAL B 316  ASP B 319 -1  O  ASP B 319   N  LEU B 306           
SHEET    1 AA9 4 GLN B 430  ASP B 433  0                                        
SHEET    2 AA9 4 ALA B 463  ILE B 466  1  O  ILE B 464   N  PHE B 432           
SHEET    3 AA9 4 PHE B 589  SER B 590 -1  O  SER B 590   N  ALA B 463           
SHEET    4 AA9 4 ALA B 571  VAL B 572 -1  N  VAL B 572   O  PHE B 589           
SHEET    1 AB1 3 ARG B 478  VAL B 479  0                                        
SHEET    2 AB1 3 LEU B 527  GLN B 530 -1  O  GLN B 530   N  ARG B 478           
SHEET    3 AB1 3 GLU B 537  PHE B 539 -1  O  PHE B 539   N  LEU B 527           
SHEET    1 AB2 2 GLY B 489  LYS B 491  0                                        
SHEET    2 AB2 2 THR B 497  GLY B 499 -1  O  LEU B 498   N  TYR B 490           
SHEET    1 AB3 2 GLU B 548  PRO B 550  0                                        
SHEET    2 AB3 2 LYS B 565  TYR B 567 -1  O  TRP B 566   N  VAL B 549           
SHEET    1 AB4 3 LEU B 582  PHE B 584  0                                        
SHEET    2 AB4 3 LEU B 576  ILE B 579 -1  N  LEU B 577   O  PHE B 584           
SHEET    3 AB4 3 SER B 708  GLU B 710 -1  O  GLU B 710   N  LEU B 576           
SHEET    1 AB5 2 TYR B 593  MET B 594  0                                        
SHEET    2 AB5 2 ILE B 653  VAL B 654  1  O  VAL B 654   N  TYR B 593           
LINK         SG  CYS A 331                ZN    ZN A 804     1555   1555  2.33  
LINK         SG  CYS A 336                ZN    ZN A 804     1555   1555  2.39  
LINK         SG  CYS A 420                FE   HEM A 801     1555   1555  2.37  
LINK         SG  CYS B 331                ZN    ZN A 804     1555   1555  2.38  
LINK         SG  CYS B 336                ZN    ZN A 804     1555   1555  2.31  
LINK         SG  CYS B 420                FE   HEM B 801     1555   1555  2.40  
CISPEP   1 THR A  706    PRO A  707          0         3.24                     
CISPEP   2 THR B  706    PRO B  707          0         5.03                     
SITE     1 AC1 14 TRP A 414  CYS A 420  PHE A 589  SER A 590                    
SITE     2 AC1 14 TRP A 592  GLU A 597  TRP A 683  PHE A 709                    
SITE     3 AC1 14 TYR A 711  H4B A 802  BY7 A 803  HOH A 912                    
SITE     4 AC1 14 HOH A 930  HOH A 978                                          
SITE     1 AC2 15 SER A 339  ARG A 601  VAL A 682  TRP A 683                    
SITE     2 AC2 15 HEM A 801  HOH A 930  HOH A 948  HOH A 950                    
SITE     3 AC2 15 HOH A 970  HOH A1017  TRP B 681  PHE B 696                    
SITE     4 AC2 15 HIS B 697  GLN B 698  GLU B 699                               
SITE     1 AC3 12 GLN A 483  ARG A 486  GLY A 591  TRP A 592                    
SITE     2 AC3 12 TYR A 593  GLU A 597  ARG A 601  ASP A 602                    
SITE     3 AC3 12 ARG A 608  HEM A 801  HOH A 912  HOH A1000                    
SITE     1 AC4  4 CYS A 331  CYS A 336  CYS B 331  CYS B 336                    
SITE     1 AC5 14 TRP B 414  CYS B 420  SER B 462  PHE B 589                    
SITE     2 AC5 14 SER B 590  GLY B 591  TRP B 592  GLU B 597                    
SITE     3 AC5 14 TRP B 683  PHE B 709  TYR B 711  H4B B 802                    
SITE     4 AC5 14 BY7 B 803  HOH B 907                                          
SITE     1 AC6 16 TRP A 681  PHE A 696  HIS A 697  GLN A 698                    
SITE     2 AC6 16 GLU A 699  HOH A 939  SER B 339  MET B 341                    
SITE     3 AC6 16 ARG B 601  VAL B 682  TRP B 683  HEM B 801                    
SITE     4 AC6 16 HOH B 936  HOH B 948  HOH B 996  HOH B1045                    
SITE     1 AC7 10 GLN B 483  ARG B 486  VAL B 572  PHE B 589                    
SITE     2 AC7 10 TRP B 592  TYR B 593  GLU B 597  ARG B 601                    
SITE     3 AC7 10 ASP B 602  HEM B 801                                          
CRYST1   52.210  121.490  165.270  90.00  90.00  90.00 P 21 21 21    8          
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      0.019153  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008231  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006051        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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