GenomeNet

Database: PDB
Entry: 6NGQ
LinkDB: 6NGQ
Original site: 6NGQ 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 21-DEC-18   6NGQ              
TITLE     STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME DOMAIN IN COMPLEX
TITLE    2 WITH 6-(3-FLUORO-5-(2-((2R,4S)-4-FLUOROPYRROLIDIN-2-YL)ETHYL)        
TITLE    3 PHENETHYL)-4-METHYLPYRIDIN-2-AMINE                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NITRIC OXIDE SYNTHASE, BRAIN;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: BNOS,CONSTITUTIVE NOS,NC-NOS,NOS TYPE I,NEURONAL NOS,NNOS,  
COMPND   5 PEPTIDYL-CYSTEINE S-NITROSYLASE NOS1;                                
COMPND   6 EC: 1.14.13.39;                                                      
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 ORGAN: BRAIN;                                                        
SOURCE   6 GENE: NOS1, BNOS;                                                    
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
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,  
KEYWDS   2 OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.LI,T.L.POULOS                                                       
REVDAT   3   04-DEC-19 6NGQ    1       REMARK                                   
REVDAT   2   27-MAR-19 6NGQ    1       JRNL                                     
REVDAT   1   13-MAR-19 6NGQ    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.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1-2575_1496: ???)                       
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) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 81.79                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.030                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 69548                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6554                            
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 81.8620 -  6.0583    0.98     4176   203  0.1663 0.1647        
REMARK   3     2  6.0583 -  4.8088    0.99     4138   248  0.1453 0.1998        
REMARK   3     3  4.8088 -  4.2010    0.99     4151   233  0.1211 0.1556        
REMARK   3     4  4.2010 -  3.8169    0.98     4113   206  0.1213 0.1604        
REMARK   3     5  3.8169 -  3.5433    0.98     4108   260  0.1361 0.2054        
REMARK   3     6  3.5433 -  3.3344    0.99     4193   194  0.1538 0.1892        
REMARK   3     7  3.3344 -  3.1674    0.99     4177   203  0.1668 0.1959        
REMARK   3     8  3.1674 -  3.0295    0.99     4114   236  0.1910 0.2445        
REMARK   3     9  3.0295 -  2.9129    0.99     4208   240  0.2014 0.2496        
REMARK   3    10  2.9129 -  2.8124    0.99     4209   216  0.1970 0.2593        
REMARK   3    11  2.8124 -  2.7244    0.99     4131   204  0.2046 0.2709        
REMARK   3    12  2.7244 -  2.6465    0.99     4230   225  0.2208 0.2732        
REMARK   3    13  2.6465 -  2.5769    0.99     4156   197  0.2196 0.2715        
REMARK   3    14  2.5769 -  2.5140    0.99     4213   236  0.2214 0.2927        
REMARK   3    15  2.5140 -  2.4568    0.99     4185   192  0.2373 0.3351        
REMARK   3    16  2.4568 -  2.4045    0.99     4231   216  0.2488 0.3232        
REMARK   3    17  2.4045 -  2.3564    0.99     4147   206  0.2419 0.2903        
REMARK   3    18  2.3564 -  2.3120    0.99     4220   245  0.2454 0.2762        
REMARK   3    19  2.3120 -  2.2707    0.99     4122   233  0.2618 0.3059        
REMARK   3    20  2.2707 -  2.2322    0.99     4114   255  0.3206 0.3762        
REMARK   3    21  2.2322 -  2.1962    0.99     4196   224  0.3023 0.3321        
REMARK   3    22  2.1962 -  2.1624    0.99     4207   190  0.3019 0.3833        
REMARK   3    23  2.1624 -  2.1306    0.99     4205   208  0.3128 0.3601        
REMARK   3    24  2.1306 -  2.1006    0.99     4248   178  0.3196 0.4156        
REMARK   3    25  2.1006 -  2.0722    0.99     4116   197  0.3479 0.4482        
REMARK   3    26  2.0722 -  2.0453    0.98     4148   228  0.3589 0.3937        
REMARK   3    27  2.0453 -  2.0197    0.99     4203   225  0.3495 0.3968        
REMARK   3    28  2.0197 -  1.9954    0.99     4115   183  0.3587 0.3730        
REMARK   3    29  1.9954 -  1.9722    0.99     4195   218  0.3716 0.4340        
REMARK   3    30  1.9722 -  1.9500    0.99     4211   255  0.3768 0.3981        
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)     : 0.310            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.290           
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           7077                                  
REMARK   3   ANGLE     :  0.966           9632                                  
REMARK   3   CHIRALITY :  0.050            998                                  
REMARK   3   PLANARITY :  0.005           1215                                  
REMARK   3   DIHEDRAL  : 17.284           4132                                  
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 299:716)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  11.3287   5.1096  22.3560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2709 T22:   0.3309                                     
REMARK   3      T33:   0.2846 T12:   0.0193                                     
REMARK   3      T13:   0.0135 T23:  -0.0203                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5285 L22:   1.1285                                     
REMARK   3      L33:   4.4323 L12:  -0.0794                                     
REMARK   3      L13:  -0.0880 L23:  -0.3546                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0391 S12:   0.0880 S13:  -0.0105                       
REMARK   3      S21:   0.1020 S22:  -0.0612 S23:   0.0671                       
REMARK   3      S31:  -0.1280 S32:  -0.2646 S33:   0.0791                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 299:718)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  11.9645   5.0771  59.5482              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1590 T22:   0.1887                                     
REMARK   3      T33:   0.2245 T12:  -0.0095                                     
REMARK   3      T13:   0.0366 T23:   0.0125                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9468 L22:   1.3741                                     
REMARK   3      L33:   2.9139 L12:  -0.2909                                     
REMARK   3      L13:  -0.0363 L23:   0.2885                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0187 S12:  -0.0118 S13:   0.0733                       
REMARK   3      S21:  -0.1423 S22:  -0.0598 S23:  -0.0274                       
REMARK   3      S31:  -0.0393 S32:   0.0848 S33:   0.0412                       
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 6NGQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JAN-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000236845.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.8                                
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                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69734                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 82.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : 0.12400                            
REMARK 200  R SYM                      (I) : 0.12400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 2.22600                            
REMARK 200  R SYM FOR SHELL            (I) : 2.22600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: 1OM4                                                 
REMARK 200                                                                      
REMARK 200 REMARK: BRICKS                                                       
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-24% PEG3350, 0.1M MES 0.14-0.20M      
REMARK 280  AMMONIUM ACETATE, 10% ETHYLENE GLYCOL, 30UM SDS, 5 MM GSH, PH       
REMARK 280  5.8, VAPOR 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       25.77500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       81.79000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.88000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       81.79000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.77500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.88000            
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: 9850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33160 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -126.0 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     CYS A   297                                                      
REMARK 465     PRO A   298                                                      
REMARK 465     SER A   339                                                      
REMARK 465     GLN A   340                                                      
REMARK 465     HIS A   341                                                      
REMARK 465     THR A   342                                                      
REMARK 465     ARG A   343                                                      
REMARK 465     LYS A   344                                                      
REMARK 465     PRO A   345                                                      
REMARK 465     GLU A   346                                                      
REMARK 465     ASP A   347                                                      
REMARK 465     VAL A   348                                                      
REMARK 465     ARG A   349                                                      
REMARK 465     LYS A   717                                                      
REMARK 465     GLY A   718                                                      
REMARK 465     CYS B   297                                                      
REMARK 465     PRO B   298                                                      
REMARK 465     SER B   339                                                      
REMARK 465     GLN B   340                                                      
REMARK 465     HIS B   341                                                      
REMARK 465     THR B   342                                                      
REMARK 465     ARG B   343                                                      
REMARK 465     LYS B   344                                                      
REMARK 465     PRO B   345                                                      
REMARK 465     GLU B   346                                                      
REMARK 465     ASP B   347                                                      
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 B   952     O    HOH B  1004              2.02            
REMARK 500   O    HOH A   955     O    HOH A   958              2.05            
REMARK 500   O    HOH B  1106     O    HOH B  1118              2.08            
REMARK 500   O1D  HEM A   801     O    HOH A   901              2.11            
REMARK 500   ND1  HIS B   436     O    HOH B   901              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B  1125     O    HOH B  1136     1655     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 392      -36.00     64.48                                   
REMARK 500    THR A 393     -163.19   -120.39                                   
REMARK 500    LYS A 452       19.09     59.35                                   
REMARK 500    THR A 466      -83.56   -111.73                                   
REMARK 500    ASP A 489      -66.58    -15.19                                   
REMARK 500    PHE A 517       53.80   -141.76                                   
REMARK 500    CYS A 582       58.69   -156.48                                   
REMARK 500    ARG A 603     -134.60   -121.68                                   
REMARK 500    ARG B 349      109.43   -163.65                                   
REMARK 500    LYS B 423       71.87   -112.30                                   
REMARK 500    THR B 466      -89.32   -112.75                                   
REMARK 500    CYS B 582       56.53   -153.42                                   
REMARK 500    ARG B 603     -135.63   -124.78                                   
REMARK 500    ASN B 605       63.61     60.40                                   
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 A1099        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH B1158        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH B1159        DISTANCE =  6.29 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 805  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 326   SG                                                     
REMARK 620 2 CYS A 331   SG  117.0                                              
REMARK 620 3 CYS B 326   SG  118.2 106.1                                        
REMARK 620 4 CYS B 331   SG  103.6  99.4 110.7                                  
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 415   SG                                                     
REMARK 620 2 HEM A 801   NA  103.9                                              
REMARK 620 3 HEM A 801   NB  102.5  87.8                                        
REMARK 620 4 HEM A 801   NC   97.9 158.2  88.2                                  
REMARK 620 5 HEM A 801   ND  101.2  88.0 156.3  87.1                            
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 415   SG                                                     
REMARK 620 2 HEM B 801   NA  102.6                                              
REMARK 620 3 HEM B 801   NB  101.7  86.2                                        
REMARK 620 4 HEM B 801   NC   95.3 162.1  89.3                                  
REMARK 620 5 HEM B 801   ND   98.5  91.1 159.7  87.2                            
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 KLA A 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT 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 KLA B 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 805                  
DBREF  6NGQ A  297   718  UNP    P29476   NOS1_RAT       297    718             
DBREF  6NGQ B  297   718  UNP    P29476   NOS1_RAT       297    718             
SEQRES   1 A  422  CYS PRO ARG PHE LEU LYS VAL LYS ASN TRP GLU THR ASP          
SEQRES   2 A  422  VAL VAL LEU THR ASP THR LEU HIS LEU LYS SER THR LEU          
SEQRES   3 A  422  GLU THR GLY CYS THR GLU HIS ILE CYS MET GLY SER ILE          
SEQRES   4 A  422  MET LEU PRO SER GLN HIS THR ARG LYS PRO GLU ASP VAL          
SEQRES   5 A  422  ARG THR LYS ASP GLN LEU PHE PRO LEU ALA LYS GLU PHE          
SEQRES   6 A  422  LEU ASP GLN TYR TYR SER SER ILE LYS ARG PHE GLY SER          
SEQRES   7 A  422  LYS ALA HIS MET ASP ARG LEU GLU GLU VAL ASN LYS GLU          
SEQRES   8 A  422  ILE GLU SER THR SER THR TYR GLN LEU LYS ASP THR GLU          
SEQRES   9 A  422  LEU ILE TYR GLY ALA LYS HIS ALA TRP ARG ASN ALA SER          
SEQRES  10 A  422  ARG CYS VAL GLY ARG ILE GLN TRP SER LYS LEU GLN VAL          
SEQRES  11 A  422  PHE ASP ALA ARG ASP CYS THR THR ALA HIS GLY MET PHE          
SEQRES  12 A  422  ASN TYR ILE CYS ASN HIS VAL LYS TYR ALA THR ASN LYS          
SEQRES  13 A  422  GLY ASN LEU ARG SER ALA ILE THR ILE PHE PRO GLN ARG          
SEQRES  14 A  422  THR ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN SER GLN          
SEQRES  15 A  422  LEU ILE ARG TYR ALA GLY TYR LYS GLN PRO ASP GLY SER          
SEQRES  16 A  422  THR LEU GLY ASP PRO ALA ASN VAL GLN PHE THR GLU ILE          
SEQRES  17 A  422  CYS ILE GLN GLN GLY TRP LYS ALA PRO ARG GLY ARG PHE          
SEQRES  18 A  422  ASP VAL LEU PRO LEU LEU LEU GLN ALA ASN GLY ASN ASP          
SEQRES  19 A  422  PRO GLU LEU PHE GLN ILE PRO PRO GLU LEU VAL LEU GLU          
SEQRES  20 A  422  VAL PRO ILE ARG HIS PRO LYS PHE ASP TRP PHE LYS ASP          
SEQRES  21 A  422  LEU GLY LEU LYS TRP TYR GLY LEU PRO ALA VAL SER ASN          
SEQRES  22 A  422  MET LEU LEU GLU ILE GLY GLY LEU GLU PHE SER ALA CYS          
SEQRES  23 A  422  PRO PHE SER GLY TRP TYR MET GLY THR GLU ILE GLY VAL          
SEQRES  24 A  422  ARG ASP TYR CYS ASP ASN SER ARG TYR ASN ILE LEU GLU          
SEQRES  25 A  422  GLU VAL ALA LYS LYS MET ASP LEU ASP MET ARG LYS THR          
SEQRES  26 A  422  SER SER LEU TRP LYS ASP GLN ALA LEU VAL GLU ILE ASN          
SEQRES  27 A  422  ILE ALA VAL LEU TYR SER PHE GLN SER ASP LYS VAL THR          
SEQRES  28 A  422  ILE VAL ASP HIS HIS SER ALA THR GLU SER PHE ILE LYS          
SEQRES  29 A  422  HIS MET GLU ASN GLU TYR ARG CYS ARG GLY GLY CYS PRO          
SEQRES  30 A  422  ALA ASP TRP VAL TRP ILE VAL PRO PRO MET SER GLY SER          
SEQRES  31 A  422  ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR ARG          
SEQRES  32 A  422  LEU THR PRO SER PHE GLU TYR GLN PRO ASP PRO TRP ASN          
SEQRES  33 A  422  THR HIS VAL TRP LYS GLY                                      
SEQRES   1 B  422  CYS PRO ARG PHE LEU LYS VAL LYS ASN TRP GLU THR ASP          
SEQRES   2 B  422  VAL VAL LEU THR ASP THR LEU HIS LEU LYS SER THR LEU          
SEQRES   3 B  422  GLU THR GLY CYS THR GLU HIS ILE CYS MET GLY SER ILE          
SEQRES   4 B  422  MET LEU PRO SER GLN HIS THR ARG LYS PRO GLU ASP VAL          
SEQRES   5 B  422  ARG THR LYS ASP GLN LEU PHE PRO LEU ALA LYS GLU PHE          
SEQRES   6 B  422  LEU ASP GLN TYR TYR SER SER ILE LYS ARG PHE GLY SER          
SEQRES   7 B  422  LYS ALA HIS MET ASP ARG LEU GLU GLU VAL ASN LYS GLU          
SEQRES   8 B  422  ILE GLU SER THR SER THR TYR GLN LEU LYS ASP THR GLU          
SEQRES   9 B  422  LEU ILE TYR GLY ALA LYS HIS ALA TRP ARG ASN ALA SER          
SEQRES  10 B  422  ARG CYS VAL GLY ARG ILE GLN TRP SER LYS LEU GLN VAL          
SEQRES  11 B  422  PHE ASP ALA ARG ASP CYS THR THR ALA HIS GLY MET PHE          
SEQRES  12 B  422  ASN TYR ILE CYS ASN HIS VAL LYS TYR ALA THR ASN LYS          
SEQRES  13 B  422  GLY ASN LEU ARG SER ALA ILE THR ILE PHE PRO GLN ARG          
SEQRES  14 B  422  THR ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN SER GLN          
SEQRES  15 B  422  LEU ILE ARG TYR ALA GLY TYR LYS GLN PRO ASP GLY SER          
SEQRES  16 B  422  THR LEU GLY ASP PRO ALA ASN VAL GLN PHE THR GLU ILE          
SEQRES  17 B  422  CYS ILE GLN GLN GLY TRP LYS ALA PRO ARG GLY ARG PHE          
SEQRES  18 B  422  ASP VAL LEU PRO LEU LEU LEU GLN ALA ASN GLY ASN ASP          
SEQRES  19 B  422  PRO GLU LEU PHE GLN ILE PRO PRO GLU LEU VAL LEU GLU          
SEQRES  20 B  422  VAL PRO ILE ARG HIS PRO LYS PHE ASP TRP PHE LYS ASP          
SEQRES  21 B  422  LEU GLY LEU LYS TRP TYR GLY LEU PRO ALA VAL SER ASN          
SEQRES  22 B  422  MET LEU LEU GLU ILE GLY GLY LEU GLU PHE SER ALA CYS          
SEQRES  23 B  422  PRO PHE SER GLY TRP TYR MET GLY THR GLU ILE GLY VAL          
SEQRES  24 B  422  ARG ASP TYR CYS ASP ASN SER ARG TYR ASN ILE LEU GLU          
SEQRES  25 B  422  GLU VAL ALA LYS LYS MET ASP LEU ASP MET ARG LYS THR          
SEQRES  26 B  422  SER SER LEU TRP LYS ASP GLN ALA LEU VAL GLU ILE ASN          
SEQRES  27 B  422  ILE ALA VAL LEU TYR SER PHE GLN SER ASP LYS VAL THR          
SEQRES  28 B  422  ILE VAL ASP HIS HIS SER ALA THR GLU SER PHE ILE LYS          
SEQRES  29 B  422  HIS MET GLU ASN GLU TYR ARG CYS ARG GLY GLY CYS PRO          
SEQRES  30 B  422  ALA ASP TRP VAL TRP ILE VAL PRO PRO MET SER GLY SER          
SEQRES  31 B  422  ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR ARG          
SEQRES  32 B  422  LEU THR PRO SER PHE GLU TYR GLN PRO ASP PRO TRP ASN          
SEQRES  33 B  422  THR HIS VAL TRP LYS GLY                                      
HET    HEM  A 801      43                                                       
HET    H4B  A 802      17                                                       
HET    KLA  A 803      25                                                       
HET    ACT  A 804       4                                                       
HET    HEM  B 801      43                                                       
HET    H4B  B 802      17                                                       
HET    KLA  B 803      25                                                       
HET    ACT  B 804       4                                                       
HET     ZN  B 805       1                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     H4B 5,6,7,8-TETRAHYDROBIOPTERIN                                      
HETNAM     KLA 6-[2-(3-FLUORO-5-{2-[(2R,4S)-4-FLUOROPYRROLIDIN-2-               
HETNAM   2 KLA  YL]ETHYL}PHENYL)ETHYL]-4-METHYLPYRIDIN-2-AMINE                  
HETNAM     ACT ACETATE ION                                                      
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  KLA    2(C20 H25 F2 N3)                                             
FORMUL   6  ACT    2(C2 H3 O2 1-)                                               
FORMUL  11   ZN    ZN 2+                                                        
FORMUL  12  HOH   *458(H2 O)                                                    
HELIX    1 AA1 THR A  315  SER A  320  5                                   6    
HELIX    2 AA2 LYS A  351  ILE A  369  1                                  19    
HELIX    3 AA3 SER A  374  SER A  392  1                                  19    
HELIX    4 AA4 LYS A  397  ASN A  411  1                                  15    
HELIX    5 AA5 GLY A  417  LEU A  424  5                                   8    
HELIX    6 AA6 THR A  434  ASN A  451  1                                  18    
HELIX    7 AA7 LYS A  452  ASN A  454  5                                   3    
HELIX    8 AA8 ASN A  498  GLN A  508  1                                  11    
HELIX    9 AA9 PRO A  537  VAL A  541  5                                   5    
HELIX   10 AB1 PHE A  551  GLY A  558  5                                   8    
HELIX   11 AB2 GLY A  590  VAL A  595  1                                   6    
HELIX   12 AB3 VAL A  595  ASP A  600  1                                   6    
HELIX   13 AB4 ILE A  606  ASP A  615  1                                  10    
HELIX   14 AB5 LYS A  620  SER A  623  5                                   4    
HELIX   15 AB6 LEU A  624  ASP A  644  1                                  21    
HELIX   16 AB7 ASP A  650  GLY A  670  1                                  21    
HELIX   17 AB8 ASP A  675  VAL A  680  1                                   6    
HELIX   18 AB9 SER A  684  GLN A  693  5                                  10    
HELIX   19 AC1 ASP A  709  HIS A  714  1                                   6    
HELIX   20 AC2 THR B  315  SER B  320  5                                   6    
HELIX   21 AC3 THR B  350  ILE B  369  1                                  20    
HELIX   22 AC4 SER B  374  SER B  392  1                                  19    
HELIX   23 AC5 LYS B  397  ASN B  411  1                                  15    
HELIX   24 AC6 GLY B  417  TRP B  421  5                                   5    
HELIX   25 AC7 THR B  434  ASN B  451  1                                  18    
HELIX   26 AC8 LYS B  452  ASN B  454  5                                   3    
HELIX   27 AC9 ASN B  498  GLN B  508  1                                  11    
HELIX   28 AD1 PRO B  537  VAL B  541  5                                   5    
HELIX   29 AD2 TRP B  553  GLY B  558  5                                   6    
HELIX   30 AD3 GLY B  590  VAL B  595  1                                   6    
HELIX   31 AD4 VAL B  595  ASP B  600  1                                   6    
HELIX   32 AD5 ILE B  606  MET B  614  1                                   9    
HELIX   33 AD6 LYS B  620  SER B  623  5                                   4    
HELIX   34 AD7 LEU B  624  ASP B  644  1                                  21    
HELIX   35 AD8 ASP B  650  GLY B  670  1                                  21    
HELIX   36 AD9 ASP B  675  VAL B  680  1                                   6    
HELIX   37 AE1 SER B  684  THR B  688  5                                   5    
HELIX   38 AE2 ASP B  709  HIS B  714  1                                   6    
SHEET    1 AA1 2 LEU A 301  LYS A 304  0                                        
SHEET    2 AA1 2 VAL A 311  ASP A 314 -1  O  ASP A 314   N  LEU A 301           
SHEET    1 AA2 4 GLN A 425  ASP A 428  0                                        
SHEET    2 AA2 4 ALA A 458  ILE A 461  1  O  ILE A 459   N  PHE A 427           
SHEET    3 AA2 4 PHE A 584  SER A 585 -1  O  SER A 585   N  ALA A 458           
SHEET    4 AA2 4 ALA A 566  VAL A 567 -1  N  VAL A 567   O  PHE A 584           
SHEET    1 AA3 3 ARG A 473  VAL A 474  0                                        
SHEET    2 AA3 3 LEU A 522  GLN A 525 -1  O  GLN A 525   N  ARG A 473           
SHEET    3 AA3 3 GLU A 532  PHE A 534 -1  O  PHE A 534   N  LEU A 522           
SHEET    1 AA4 2 GLY A 484  LYS A 486  0                                        
SHEET    2 AA4 2 THR A 492  GLY A 494 -1  O  LEU A 493   N  TYR A 485           
SHEET    1 AA5 2 GLU A 543  PRO A 545  0                                        
SHEET    2 AA5 2 LYS A 560  TYR A 562 -1  O  TRP A 561   N  VAL A 544           
SHEET    1 AA6 3 LEU A 577  PHE A 579  0                                        
SHEET    2 AA6 3 LEU A 571  ILE A 574 -1  N  LEU A 572   O  PHE A 579           
SHEET    3 AA6 3 SER A 703  GLU A 705 -1  O  GLU A 705   N  LEU A 571           
SHEET    1 AA7 2 TYR A 588  MET A 589  0                                        
SHEET    2 AA7 2 ILE A 648  VAL A 649  1  O  VAL A 649   N  TYR A 588           
SHEET    1 AA8 2 LEU B 301  LYS B 304  0                                        
SHEET    2 AA8 2 VAL B 311  ASP B 314 -1  O  ASP B 314   N  LEU B 301           
SHEET    1 AA9 4 GLN B 425  ASP B 428  0                                        
SHEET    2 AA9 4 ALA B 458  ILE B 461  1  O  ILE B 459   N  PHE B 427           
SHEET    3 AA9 4 PHE B 584  SER B 585 -1  O  SER B 585   N  ALA B 458           
SHEET    4 AA9 4 ALA B 566  VAL B 567 -1  N  VAL B 567   O  PHE B 584           
SHEET    1 AB1 3 ARG B 473  VAL B 474  0                                        
SHEET    2 AB1 3 LEU B 522  GLN B 525 -1  O  GLN B 525   N  ARG B 473           
SHEET    3 AB1 3 GLU B 532  PHE B 534 -1  O  PHE B 534   N  LEU B 522           
SHEET    1 AB2 2 GLY B 484  LYS B 486  0                                        
SHEET    2 AB2 2 THR B 492  GLY B 494 -1  O  LEU B 493   N  TYR B 485           
SHEET    1 AB3 2 GLU B 543  PRO B 545  0                                        
SHEET    2 AB3 2 LYS B 560  TYR B 562 -1  O  TRP B 561   N  VAL B 544           
SHEET    1 AB4 3 LEU B 577  PHE B 579  0                                        
SHEET    2 AB4 3 LEU B 571  ILE B 574 -1  N  LEU B 572   O  PHE B 579           
SHEET    3 AB4 3 SER B 703  GLU B 705 -1  O  GLU B 705   N  LEU B 571           
SHEET    1 AB5 2 TYR B 588  MET B 589  0                                        
SHEET    2 AB5 2 ILE B 648  VAL B 649  1  O  VAL B 649   N  TYR B 588           
LINK         SG  CYS A 326                ZN    ZN B 805     1555   1555  2.37  
LINK         SG  CYS A 331                ZN    ZN B 805     1555   1555  2.35  
LINK         SG  CYS A 415                FE   HEM A 801     1555   1555  2.37  
LINK         SG  CYS B 326                ZN    ZN B 805     1555   1555  2.35  
LINK         SG  CYS B 331                ZN    ZN B 805     1555   1555  2.38  
LINK         SG  CYS B 415                FE   HEM B 801     1555   1555  2.36  
CISPEP   1 THR A  701    PRO A  702          0         0.08                     
CISPEP   2 THR B  701    PRO B  702          0         0.49                     
SITE     1 AC1 20 TRP A 409  ARG A 414  CYS A 415  VAL A 416                    
SITE     2 AC1 20 SER A 457  PHE A 584  SER A 585  TRP A 587                    
SITE     3 AC1 20 GLU A 592  TRP A 678  PHE A 704  TYR A 706                    
SITE     4 AC1 20 H4B A 802  KLA A 803  ACT A 804  HOH A 901                    
SITE     5 AC1 20 HOH A 906  HOH A 918  HOH A 938  HOH A 968                    
SITE     1 AC2 15 SER A 334  MET A 336  ARG A 596  VAL A 677                    
SITE     2 AC2 15 TRP A 678  HEM A 801  KLA A 803  HOH A 918                    
SITE     3 AC2 15 HOH A 953  HOH A 954  TRP B 676  PHE B 691                    
SITE     4 AC2 15 HIS B 692  GLN B 693  GLU B 694                               
SITE     1 AC3 10 MET A 336  VAL A 567  GLY A 586  TRP A 587                    
SITE     2 AC3 10 GLU A 592  HEM A 801  H4B A 802  HOH A 918                    
SITE     3 AC3 10 HOH A 964  TRP B 306                                          
SITE     1 AC4  3 TRP A 587  VAL A 649  HEM A 801                               
SITE     1 AC5 16 TRP B 409  ARG B 414  CYS B 415  SER B 457                    
SITE     2 AC5 16 PHE B 584  SER B 585  TRP B 587  MET B 589                    
SITE     3 AC5 16 GLU B 592  TRP B 678  TYR B 706  H4B B 802                    
SITE     4 AC5 16 KLA B 803  HOH B 904  HOH B 916  HOH B1013                    
SITE     1 AC6 15 TRP A 676  PHE A 691  HIS A 692  GLN A 693                    
SITE     2 AC6 15 GLU A 694  SER B 334  ARG B 596  VAL B 677                    
SITE     3 AC6 15 TRP B 678  HEM B 801  HOH B 916  HOH B 929                    
SITE     4 AC6 15 HOH B1005  HOH B1025  HOH B1056                               
SITE     1 AC7  7 GLN B 478  VAL B 567  TRP B 587  TYR B 588                    
SITE     2 AC7  7 GLU B 592  HEM B 801  HOH B 916                               
SITE     1 AC8  4 TRP B 587  VAL B 649  HOH B 968  HOH B 997                    
SITE     1 AC9  4 CYS A 326  CYS A 331  CYS B 326  CYS B 331                    
CRYST1   51.550  111.760  163.580  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      0.019399  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008948  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006113        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system