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Database: PDB
Entry: 6NG4
LinkDB: 6NG4
Original site: 6NG4 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 21-DEC-18   6NG4              
TITLE     STRUCTURE OF HUMAN NEURONAL NITRIC OXIDE SYNTHASE R354A/G357D MUTANT  
TITLE    2 HEME DOMAIN IN COMPLEX WITH (R)-6-(3-FLUORO-5-(2-(PYRROLIDIN-2-YL)   
TITLE    3 ETHYL)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                                                        
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 BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PCWORI                                    
KEYWDS    NITRIC OXIDE SYNTHASE, INHIBITOR COMPLEX, HEME ENZYME,                
KEYWDS   2 OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.LI,T.L.POULOS                                                       
REVDAT   3   04-DEC-19 6NG4    1       REMARK                                   
REVDAT   2   27-MAR-19 6NG4    1       JRNL                                     
REVDAT   1   13-MAR-19 6NG4    0                                                
JRNL        AUTH   H.T.DO,H.LI,G.CHREIFI,T.L.POULOS,R.B.SILVERMAN               
JRNL        TITL   OPTIMIZATION OF BLOOD-BRAIN BARRIER PERMEABILITY WITH POTENT 
JRNL        TITL 2 AND SELECTIVE HUMAN NEURONAL NITRIC OXIDE SYNTHASE           
JRNL        TITL 3 INHIBITORS HAVING A 2-AMINOPYRIDINE SCAFFOLD.                
JRNL        REF    J. MED. CHEM.                 V.  62  2690 2019              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   30802056                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.8B02032                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.78 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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) : 1.78                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.85                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.870                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 100431                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.910                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 9446                            
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 38.8628 -  5.5124    1.00     6223   280  0.1598 0.1849        
REMARK   3     2  5.5124 -  4.3772    1.00     6189   311  0.1296 0.1560        
REMARK   3     3  4.3772 -  3.8245    1.00     6195   326  0.1329 0.1654        
REMARK   3     4  3.8245 -  3.4750    1.00     6140   348  0.1399 0.1778        
REMARK   3     5  3.4750 -  3.2261    1.00     6241   312  0.1588 0.2265        
REMARK   3     6  3.2261 -  3.0360    1.00     6204   309  0.1738 0.2151        
REMARK   3     7  3.0360 -  2.8840    1.00     6163   310  0.1681 0.2257        
REMARK   3     8  2.8840 -  2.7585    1.00     6184   293  0.1678 0.2008        
REMARK   3     9  2.7585 -  2.6523    1.00     6257   308  0.1717 0.1966        
REMARK   3    10  2.6523 -  2.5608    1.00     6189   333  0.1665 0.2374        
REMARK   3    11  2.5608 -  2.4807    1.00     6136   327  0.1633 0.1897        
REMARK   3    12  2.4807 -  2.4098    1.00     6193   350  0.1734 0.2297        
REMARK   3    13  2.4098 -  2.3464    1.00     6121   352  0.1800 0.2240        
REMARK   3    14  2.3464 -  2.2892    1.00     6174   308  0.1848 0.2436        
REMARK   3    15  2.2892 -  2.2371    1.00     6254   308  0.1903 0.2331        
REMARK   3    16  2.2371 -  2.1895    1.00     6167   303  0.1942 0.2346        
REMARK   3    17  2.1895 -  2.1457    1.00     6192   291  0.2142 0.2558        
REMARK   3    18  2.1457 -  2.1052    1.00     6108   333  0.2418 0.2824        
REMARK   3    19  2.1052 -  2.0677    1.00     6224   336  0.2636 0.3096        
REMARK   3    20  2.0677 -  2.0326    1.00     6182   309  0.2732 0.3127        
REMARK   3    21  2.0326 -  1.9998    0.99     6127   308  0.2964 0.3161        
REMARK   3    22  1.9998 -  1.9691    0.99     6123   369  0.3095 0.3266        
REMARK   3    23  1.9691 -  1.9401    0.99     6102   348  0.3395 0.3743        
REMARK   3    24  1.9401 -  1.9128    0.99     6199   261  0.3696 0.3829        
REMARK   3    25  1.9128 -  1.8869    0.99     6199   302  0.3844 0.3728        
REMARK   3    26  1.8869 -  1.8624    0.99     6082   357  0.4096 0.4039        
REMARK   3    27  1.8624 -  1.8391    0.98     6125   327  0.4381 0.4744        
REMARK   3    28  1.8391 -  1.8170    0.97     5952   320  0.4859 0.4896        
REMARK   3    29  1.8170 -  1.7959    0.97     6060   286  0.4893 0.5383        
REMARK   3    30  1.7959 -  1.7757    0.66     4074   221  0.5146 0.5226        
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)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.210           
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           7146                                  
REMARK   3   ANGLE     :  1.134           9724                                  
REMARK   3   CHIRALITY :  0.042           1003                                  
REMARK   3   PLANARITY :  0.005           1226                                  
REMARK   3   DIHEDRAL  : 15.391           2615                                  
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 302:722)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 117.7342 248.3164 358.7407              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2502 T22:   0.3287                                     
REMARK   3      T33:   0.3247 T12:  -0.0076                                     
REMARK   3      T13:   0.0260 T23:   0.0310                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4325 L22:   0.6329                                     
REMARK   3      L33:   2.2013 L12:  -0.2075                                     
REMARK   3      L13:  -0.0750 L23:   0.2676                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0064 S12:  -0.0323 S13:   0.0382                       
REMARK   3      S21:  -0.0427 S22:  -0.0835 S23:   0.0041                       
REMARK   3      S31:   0.1144 S32:   0.1387 S33:  -0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 304:722)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 116.0960 246.8301 321.5555              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3332 T22:   0.3682                                     
REMARK   3      T33:   0.3501 T12:  -0.0049                                     
REMARK   3      T13:   0.0139 T23:  -0.0292                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1866 L22:   0.4100                                     
REMARK   3      L33:   3.2970 L12:  -0.2930                                     
REMARK   3      L13:  -0.2956 L23:   0.0924                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0281 S12:   0.0760 S13:  -0.0125                       
REMARK   3      S21:  -0.0498 S22:  -0.0795 S23:   0.0334                       
REMARK   3      S31:   0.0187 S32:  -0.1505 S33:  -0.0004                       
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 6NG4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000236879.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-MAR-17                          
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               : SSRL                               
REMARK 200  BEAMLINE                       : BL12-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 101601                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.776                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 8.900                              
REMARK 200  R MERGE                    (I) : 0.09900                            
REMARK 200  R SYM                      (I) : 0.09900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.82                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 4.25100                            
REMARK 200  R SYM FOR SHELL            (I) : 4.25100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1OM4                                       
REMARK 200                                                                      
REMARK 200 REMARK: PLATES                                                       
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG3350, 35 MM CITRIC ACID, 65 MM     
REMARK 280  BIS-TRIS PROPANE, 10% GLYCEROL, 5 MM TCEP, PH 7.2, VAPOR            
REMARK 280  DIFFUSION, 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       26.19650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       82.00350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       60.81450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       82.00350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.19650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       60.81450            
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: 9990 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33860 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 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     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 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  1081     O    HOH B  1132              2.13            
REMARK 500   O    HOH A  1218     O    HOH A  1233              2.17            
REMARK 500   O    HOH A  1021     O    HOH A  1178              2.18            
REMARK 500   O    HOH A  1006     O    HOH A  1215              2.18            
REMARK 500   O    HOH B   982     O    HOH B  1041              2.18            
REMARK 500   O    HOH A  1057     O    HOH A  1148              2.19            
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    THR A 326      -88.66   -117.80                                   
REMARK 500    VAL A 353      117.15     39.26                                   
REMARK 500    LYS A 428       73.65   -105.56                                   
REMARK 500    THR A 471      -86.44   -111.75                                   
REMARK 500    CYS A 587       56.95   -149.88                                   
REMARK 500    ARG A 608     -134.86   -117.19                                   
REMARK 500    CYS A 677       99.46   -160.83                                   
REMARK 500    THR B 326      -74.89   -134.39                                   
REMARK 500    THR B 471      -76.77   -114.51                                   
REMARK 500    LYS B 555      -38.93   -133.22                                   
REMARK 500    CYS B 587       59.95   -149.08                                   
REMARK 500    ARG B 608     -131.71   -117.13                                   
REMARK 500    CYS B 677      104.55   -160.41                                   
REMARK 500    TRP B 721      174.28    -59.68                                   
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 B1156        DISTANCE =  6.30 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 803  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 331   SG                                                     
REMARK 620 2 CYS A 336   SG  108.9                                              
REMARK 620 3 CYS B 331   SG  125.1 103.7                                        
REMARK 620 4 CYS B 336   SG  101.4 100.7 114.5                                  
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  101.2                                              
REMARK 620 3 HEM A 801   NB  100.9  88.4                                        
REMARK 620 4 HEM A 801   NC   97.8 161.0  88.6                                  
REMARK 620 5 HEM A 801   ND  100.6  87.8 158.5  88.1                            
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   99.6                                              
REMARK 620 3 HEM B 801   NB   98.5  84.8                                        
REMARK 620 4 HEM B 801   NC   97.9 162.4  90.9                                  
REMARK 620 5 HEM B 801   ND  102.1  92.2 159.4  85.8                            
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 ZN A 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue KMA A 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 805                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 806                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B B 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue KMA B 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 804                 
DBREF  6NG4 A  302   722  UNP    P29475   NOS1_HUMAN     302    722             
DBREF  6NG4 B  302   722  UNP    P29475   NOS1_HUMAN     302    722             
SEQADV 6NG4 ALA A  354  UNP  P29475    ARG   354 ENGINEERED MUTATION            
SEQADV 6NG4 ASP A  357  UNP  P29475    GLY   357 ENGINEERED MUTATION            
SEQADV 6NG4 ALA B  354  UNP  P29475    ARG   354 ENGINEERED MUTATION            
SEQADV 6NG4 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     ZN  A 803       1                                                       
HET    KMA  A 804      24                                                       
HET    GOL  A 805       6                                                       
HET    GOL  A 806       6                                                       
HET    HEM  B 801      43                                                       
HET    H4B  B 802      17                                                       
HET    KMA  B 803      24                                                       
HET    GOL  B 804       6                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     H4B 5,6,7,8-TETRAHYDROBIOPTERIN                                      
HETNAM      ZN ZINC ION                                                         
HETNAM     KMA 6-[2-(3-FLUORO-5-{2-[(2R)-PYRROLIDIN-2-                          
HETNAM   2 KMA  YL]ETHYL}PHENYL)ETHYL]-4-METHYLPYRIDIN-2-AMINE                  
HETNAM     GOL GLYCEROL                                                         
HETSYN     HEM HEME                                                             
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  HEM    2(C34 H32 FE N4 O4)                                          
FORMUL   4  H4B    2(C9 H15 N5 O3)                                              
FORMUL   5   ZN    ZN 2+                                                        
FORMUL   6  KMA    2(C20 H26 F N3)                                              
FORMUL   7  GOL    3(C3 H8 O3)                                                  
FORMUL  13  HOH   *612(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  GLY A  675  1                                  21    
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 PHE B  556  GLY B  563  5                                   8    
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  HIS B  719  1                                   6    
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  GLU A 710   N  LEU A 576           
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  SER B 708   N  GLU B 578           
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 803     1555   1555  2.36  
LINK         SG  CYS A 336                ZN    ZN A 803     1555   1555  2.37  
LINK         SG  CYS A 420                FE   HEM A 801     1555   1555  2.38  
LINK         SG  CYS B 331                ZN    ZN A 803     1555   1555  2.34  
LINK         SG  CYS B 336                ZN    ZN A 803     1555   1555  2.34  
LINK         SG  CYS B 420                FE   HEM B 801     1555   1555  2.35  
CISPEP   1 THR A  706    PRO A  707          0         0.68                     
CISPEP   2 THR B  706    PRO B  707          0         2.07                     
SITE     1 AC1 15 TRP A 414  CYS A 420  PHE A 589  SER A 590                    
SITE     2 AC1 15 TRP A 592  GLU A 597  TRP A 683  PHE A 709                    
SITE     3 AC1 15 TYR A 711  H4B A 802  KMA A 804  HOH A 929                    
SITE     4 AC1 15 HOH A 972  HOH A 975  HOH A1000                               
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 929  HOH A 936  HOH A1003                    
SITE     3 AC2 15 HOH A1012  HOH A1073  TRP B 681  PHE B 696                    
SITE     4 AC2 15 HIS B 697  GLN B 698  GLU B 699                               
SITE     1 AC3  4 CYS A 331  CYS A 336  CYS B 331  CYS B 336                    
SITE     1 AC4  9 GLN A 483  ARG A 486  TYR A 567  GLY A 591                    
SITE     2 AC4  9 TRP A 592  TYR A 593  GLU A 597  HEM A 801                    
SITE     3 AC4  9 HOH A 929                                                     
SITE     1 AC5  4 LYS A 324  GLN A 369  ARG A 674  HOH A1076                    
SITE     1 AC6  1 ARG A 415                                                     
SITE     1 AC7 18 TRP B 414  ARG B 419  CYS B 420  SER B 462                    
SITE     2 AC7 18 PHE B 589  SER B 590  GLY B 591  TRP B 592                    
SITE     3 AC7 18 GLU B 597  TRP B 683  PHE B 709  TYR B 711                    
SITE     4 AC7 18 H4B B 802  KMA B 803  HOH B 902  HOH B 903                    
SITE     5 AC7 18 HOH B1070  HOH B1090                                          
SITE     1 AC8 16 TRP A 681  PHE A 696  HIS A 697  GLN A 698                    
SITE     2 AC8 16 GLU A 699  SER B 339  ARG B 601  VAL B 682                    
SITE     3 AC8 16 TRP B 683  HEM B 801  KMA B 803  HOH B 902                    
SITE     4 AC8 16 HOH B 961  HOH B 965  HOH B 995  HOH B1027                    
SITE     1 AC9 12 GLN B 483  ARG B 486  TYR B 567  VAL B 572                    
SITE     2 AC9 12 PHE B 589  GLY B 591  TRP B 592  GLU B 597                    
SITE     3 AC9 12 TRP B 683  HEM B 801  H4B B 802  HOH B 902                    
SITE     1 AD1  2 GLN B 369  ARG B 674                                          
CRYST1   52.393  121.629  164.007  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      0.019087  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008222  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006097        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system