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Database: PDB
Entry: 5FVP
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HEADER    OXIDOREDUCTASE                          10-FEB-16   5FVP              
TITLE     STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME DOMAIN           
TITLE    2 IN COMPLEX WITH 4-METHYL-6-[2-(5-MORPHOLIN-4-YLPYRIDIN-3-YL)         
TITLE    3 ETHYL]PYRIDIN-2-AMINE                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NITRIC OXIDE SYNTHASE, BRAIN;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: HEME DOMAIN, RESIDUES 297-718;                             
COMPND   5 SYNONYM: BNOS, CONSTITUTIVE NOS, NC-NOS, NOS TYPE I, NEURONAL NOS,   
COMPND   6  N -NOS, NNOS, PEPTIDYL-CYSTEINE S-NITROSYLASE NOS1, NEURONAL        
COMPND   7  NITRIC OXIDE SYNTHASE;                                              
COMPND   8 EC: 1.14.13.39;                                                      
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PCWORI                                     
KEYWDS    OXIDOREDUCTASE, NITRIC OXIDE SYNTHASE, INHIBITOR COMPLEX              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.LI,T.L.POULOS                                                       
REVDAT   2   08-JUN-16 5FVP    1       JRNL                                     
REVDAT   1   20-APR-16 5FVP    0                                                
JRNL        AUTH   H.WANG,Y.QIN,H.LI,L.J.ROMAN,P.MARTASEK,T.L.POULOS,           
JRNL        AUTH 2 R.B.SILVERMAN                                                
JRNL        TITL   POTENT AND SELECTIVE HUMAN NEURONAL NITRIC OXIDE SYNTHASE    
JRNL        TITL 2 INHIBITION BY OPTIMIZATION OF THE 2-AMINOPYRIDINE-BASED      
JRNL        TITL 3 SCAFFOLD WITH A PYRIDINE LINKER.                             
JRNL        REF    J.MED.CHEM.                   V.  59  4913 2016              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   27050842                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.6B00273                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT 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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.099                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.990                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.35                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 71.30                          
REMARK   3   NUMBER OF REFLECTIONS             : 40036                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1762                          
REMARK   3   R VALUE            (WORKING SET) : 0.1732                          
REMARK   3   FREE R VALUE                     : 0.2324                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.9                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1979                            
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 40.9978 -  5.0556    0.96     3913   201  0.1466 0.1819        
REMARK   3     2  5.0556 -  4.0139    0.98     3762   220  0.1220 0.1802        
REMARK   3     3  4.0139 -  3.5068    0.98     3771   197  0.1428 0.2285        
REMARK   3     4  3.5068 -  3.1863    0.99     3807   177  0.1708 0.2121        
REMARK   3     5  3.1863 -  2.9580    0.99     3744   219  0.1991 0.2552        
REMARK   3     6  2.9580 -  2.7836    0.99     3756   205  0.2025 0.2873        
REMARK   3     7  2.7836 -  2.6443    0.99     3785   180  0.2308 0.3104        
REMARK   3     8  2.6443 -  2.5292    0.99     3723   190  0.2356 0.2890        
REMARK   3     9  2.5292 -  2.4318    0.66     2510   127  0.2476 0.3691        
REMARK   3    10  2.4318 -  2.3479    0.47     1758    82  0.2470 0.2771        
REMARK   3    11  2.3479 -  2.2745    0.35     1296    73  0.2259 0.2304        
REMARK   3    12  2.2745 -  2.2095    0.26      985    64  0.2618 0.3108        
REMARK   3    13  2.2095 -  2.1513    0.19      720    26  0.2167 0.3195        
REMARK   3    14  2.1513 -  2.0988    0.14      527    18  0.2114 0.4512        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.26             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.00            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6680                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 173                                     
REMARK   3   SOLVENT ATOMS            : 199                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.96                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 64.25                          
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      :  0.008           7067                                  
REMARK   3   ANGLE     :  1.229           9615                                  
REMARK   3   CHIRALITY :  0.074            993                                  
REMARK   3   PLANARITY :  0.005           1216                                  
REMARK   3   DIHEDRAL  : 15.484           2577                                  
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):  11.2810   4.7624  22.4140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1001 T22:   0.1755                                     
REMARK   3      T33:   0.2003 T12:  -0.0105                                     
REMARK   3      T13:   0.0035 T23:  -0.0168                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9590 L22:   1.7750                                     
REMARK   3      L33:   8.3449 L12:  -0.1744                                     
REMARK   3      L13:  -0.4533 L23:  -0.6352                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0820 S12:   0.1538 S13:  -0.0161                       
REMARK   3      S21:   0.1105 S22:  -0.0972 S23:   0.0721                       
REMARK   3      S31:   0.0767 S32:  -0.5218 S33:   0.0812                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 299:718)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  12.1607   4.7835  59.6514              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1013 T22:   0.1634                                     
REMARK   3      T33:   0.1832 T12:   0.0279                                     
REMARK   3      T13:   0.0437 T23:   0.0273                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0188 L22:   1.6693                                     
REMARK   3      L33:   4.0441 L12:  -0.1991                                     
REMARK   3      L13:  -0.0510 L23:   0.6035                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0046 S12:   0.0200 S13:   0.0945                       
REMARK   3      S21:  -0.1694 S22:  -0.0745 S23:  -0.0326                       
REMARK   3      S31:   0.0376 S32:   0.1199 S33:   0.0321                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3 RESIDUES 339-349 IN CHAIN A AND 339-347 IN CHAIN B ARE               
REMARK   3 DISORDERED.                                                          
REMARK   4                                                                      
REMARK   4 5FVP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-FEB-16.                  
REMARK 100 THE PDBE ID CODE IS EBI-65892.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-AUG-14                          
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                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (Q315R)                        
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55617                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.10                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 3.9                                
REMARK 200  R MERGE                    (I) : 0.09                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.20                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.5                                
REMARK 200  R MERGE FOR SHELL          (I) : 1.00                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.50                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: OVERALL RMERGE 0.091 RPIM 0.059 HIGHEST RESOLUTION           
REMARK 200  SHELL RMERGE HIGHER THAN 1.00 RPIM 0.997 CC ONE HALF 0.335          
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.4                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-24% PEG3350, 0.1M MES                 
REMARK 280  0.14-0.20M AMMONIUM ACETATE, 10% ETHYLENE GLYCOL, 30UM SDS          
REMARK 280  5 MM GSH                                                            
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       25.77000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       81.98000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.68000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       81.98000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.77000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.68000            
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: 9620 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.5 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     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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 717    CA   C    O    CB   CG   CD   CE   NZ               
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   OG   SER A   602     OE1B GLU B   307              2.20            
REMARK 500   OG   SER A   684     OD2  ASP B   627              2.16            
REMARK 500   OH   TYR A   706     O2D  HEM A   750              2.09            
REMARK 500   OH   TYR B   706     O2D  HEM B   750              2.00            
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    ASP A 309       -0.68     59.57                                   
REMARK 500    THR A 466      -91.51   -114.88                                   
REMARK 500    ARG A 514       41.42     33.14                                   
REMARK 500    LYS A 550      -41.32   -132.97                                   
REMARK 500    CYS A 582       61.47   -155.08                                   
REMARK 500    ARG A 603     -128.13   -128.35                                   
REMARK 500    SER A 684       19.97     57.55                                   
REMARK 500    SER B 392       -0.06     67.33                                   
REMARK 500    THR B 466      -88.33   -117.16                                   
REMARK 500    CYS B 582       63.00   -153.06                                   
REMARK 500    ARG B 603     -138.75   -126.77                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                             HEM A 750  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HEM A 750   NA                                                     
REMARK 620 2 HEM A 750   ND   85.9                                              
REMARK 620 3 HEM A 750   NB   86.8 153.8                                        
REMARK 620 4 HEM A 750   NC  156.4  90.8  86.0                                  
REMARK 620 5 CYS A 415   SG  102.1 103.8 102.3 101.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 750  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HEM B 750   NB                                                     
REMARK 620 2 CYS B 415   SG   99.3                                              
REMARK 620 3 HEM B 750   NC   89.9  94.8                                        
REMARK 620 4 HEM B 750   ND  161.7  98.9  86.7                                  
REMARK 620 5 HEM B 750   NA   85.6 100.9 164.2  92.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 900  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 326   SG                                                     
REMARK 620 2 CYS A 331   SG  113.3                                              
REMARK 620 3 CYS B 331   SG  104.1 100.9                                        
REMARK 620 4 CYS B 326   SG  120.0 103.8 113.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 750                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B A 760                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WOS A 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 860                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 750                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B B 760                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WOS B 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 860                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B 900                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5FVO   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME                
REMARK 900  DOMAIN IN COMPLEX WITH 6-(2-(5-(3-METHOXYPROPYLAMINO)               
REMARK 900  PYRIDIN-3-YL)ETHYL)-4-METHYLPYRIDIN-2-AMINE                         
REMARK 900 RELATED ID: 5FVQ   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME                
REMARK 900  DOMAIN IN COMPLEX WITH 4-METHYL-6-(2-(5-(4-                         
REMARK 900  METHYLPIPERAZIN-1-YL)PYRIDIN-3-YL)ETHYL)PYRIDIN-2-                  
REMARK 900  AMINE                                                               
REMARK 900 RELATED ID: 5FVR   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME                
REMARK 900  DOMAIN IN COMPLEX WITH 4-METHYL-6-(2-(5-(1-                         
REMARK 900  METHYLPIPERIDIN-4-YL)PYRIDIN-3-YL)ETHYL)PYRIDIN-2-                  
REMARK 900  AMINE                                                               
REMARK 900 RELATED ID: 5FVS   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME                
REMARK 900  DOMAIN IN COMPLEX WITH 4-METHYL-6-(2-(5-(3-(                        
REMARK 900  METHYLAMINO)PROPYL)PYRIDIN-3-YL)ETHYL)PYRIDIN-2-AMINE               
REMARK 900 RELATED ID: 5FVT   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME                
REMARK 900  DOMAIN IN COMPLEX WITH 6-(2-(5-(3-(DIMETHYLAMINO)                   
REMARK 900  PROPYL)PYRIDIN-3-YL)ETHYL)-4-METHYLPYRIDIN-2-AMINE                  
REMARK 900 RELATED ID: 5FVU   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN NNOS R354A G357D MUTANT HEME DOMAIN              
REMARK 900   IN COMPLEX WITH 4-METHYL-6-(2-(5-(4-                               
REMARK 900  METHYLPIPERAZIN-1-YL)PYRIDIN-3-YL)ETHYL)PYRIDIN-2-                  
REMARK 900  AMINE                                                               
REMARK 900 RELATED ID: 5FVV   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN NNOS R354A G357D MUTANT HEME DOMAIN              
REMARK 900   IN COMPLEX WITH 4-METHYL-6-(2-(5-(1-                               
REMARK 900  METHYLPIPERIDIN-4-YL)PYRIDIN-3-YL)ETHYL)PYRIDIN-2-                  
REMARK 900  AMINE                                                               
REMARK 900 RELATED ID: 5FVW   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN NNOS R354A G357D MUTANT HEME DOMAIN              
REMARK 900   IN COMPLEX WITH 4-METHYL-6-(2-(5-(3-(METHYLAMINO)                  
REMARK 900  PROPYL)PYRIDIN-3-YL)ETHYL)PYRIDIN-2-AMINE                           
REMARK 900 RELATED ID: 5FVX   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN NNOS R354A G357D MUTANT HEME DOMAIN              
REMARK 900   IN COMPLEX WITH HW67                                               
REMARK 900 RELATED ID: 5FVY   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE               
REMARK 900  HEME DOMAIN IN COMPLEX WITH 4-METHYL-6-(2-(5-(4-                    
REMARK 900  METHYLPIPERAZIN-1-YL)PYRIDIN-3-YL)ETHYL)PYRIDIN-2-                  
REMARK 900  AMINE                                                               
REMARK 900 RELATED ID: 5FVZ   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE               
REMARK 900  HEME DOMAIN IN COMPLEX WITH 6-(2-(5-(3-(                            
REMARK 900  DIMETHYLAMINO)PROPYL)PYRIDIN-3-YL)ETHYL)-4-METHYLPYRIDIN            
REMARK 900  -2-AMINE                                                            
REMARK 900 RELATED ID: 5FW0   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME                
REMARK 900  DOMAIN IN COMPLEX WITH 6-(2-(5-((2-METHOXYETHYL)(                   
REMARK 900  METHYL)AMINO)PYRIDIN-3-YL)ETHYL)-4-METHYLPYRIDIN-2-                 
REMARK 900  AMINE                                                               
DBREF  5FVP A  297   718  UNP    P29476   NOS1_RAT       297    718             
DBREF  5FVP 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 750      43                                                       
HET    H4B  A 760      17                                                       
HET    WOS  A 800      22                                                       
HET    ACT  A 860       4                                                       
HET    HEM  B 750      43                                                       
HET    H4B  B 760      17                                                       
HET    WOS  B 800      22                                                       
HET    ACT  B 860       4                                                       
HET     ZN  B 900       1                                                       
HETNAM     H4B 5,6,7,8-TETRAHYDROBIOPTERIN                                      
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM      ZN ZINC ION                                                         
HETNAM     WOS 4-METHYL-6-[2-(5-MORPHOLIN-4-YLPYRIDIN-3-YL)                     
HETNAM   2 WOS  ETHYL]PYRIDIN-2-AMINE                                           
HETNAM     ACT ACETATE ION                                                      
HETSYN     HEM HEME                                                             
FORMUL   3  H4B    2(C9 H15 N5 O3)                                              
FORMUL   4  HEM    2(C34 H32 FE N4 O4)                                          
FORMUL   5   ZN    ZN 2+                                                        
FORMUL   6  WOS    2(C17 H22 N4 O)                                              
FORMUL   7  ACT    2(C2 H3 O2 1-)                                               
FORMUL   8  HOH   *199(H2 O)                                                    
HELIX    1   1 THR A  315  SER A  320  5                                   6    
HELIX    2   2 THR A  350  ILE A  369  1                                  20    
HELIX    3   3 SER A  374  SER A  392  1                                  19    
HELIX    4   4 LYS A  397  ASN A  411  1                                  15    
HELIX    5   5 GLY A  417  TRP A  421  5                                   5    
HELIX    6   6 THR A  434  ASN A  451  1                                  18    
HELIX    7   7 LYS A  452  ASN A  454  5                                   3    
HELIX    8   8 ASN A  498  GLN A  508  1                                  11    
HELIX    9   9 PRO A  537  VAL A  541  5                                   5    
HELIX   10  10 PHE A  551  GLY A  558  5                                   8    
HELIX   11  11 MET A  589  VAL A  595  1                                   7    
HELIX   12  12 VAL A  595  ASP A  600  1                                   6    
HELIX   13  13 ILE A  606  ASP A  615  1                                  10    
HELIX   14  14 LYS A  620  SER A  623  5                                   4    
HELIX   15  15 LEU A  624  ASP A  644  1                                  21    
HELIX   16  16 ASP A  650  ARG A  669  1                                  20    
HELIX   17  17 ASP A  675  VAL A  680  1                                   6    
HELIX   18  18 SER A  684  THR A  688  5                                   5    
HELIX   19  19 THR A  688  HIS A  692  5                                   5    
HELIX   20  20 ASP A  709  HIS A  714  1                                   6    
HELIX   21  21 THR B  315  SER B  320  5                                   6    
HELIX   22  22 THR B  350  ILE B  369  1                                  20    
HELIX   23  23 SER B  374  SER B  392  1                                  19    
HELIX   24  24 LYS B  397  ASN B  411  1                                  15    
HELIX   25  25 GLY B  417  TRP B  421  5                                   5    
HELIX   26  26 THR B  434  ASN B  451  1                                  18    
HELIX   27  27 LYS B  452  ASN B  454  5                                   3    
HELIX   28  28 ASN B  498  GLN B  508  1                                  11    
HELIX   29  29 PRO B  537  VAL B  541  5                                   5    
HELIX   30  30 PHE B  551  GLY B  558  5                                   8    
HELIX   31  31 GLY B  590  VAL B  595  1                                   6    
HELIX   32  32 ILE B  606  MET B  614  1                                   9    
HELIX   33  33 LYS B  620  SER B  623  5                                   4    
HELIX   34  34 LEU B  624  ASP B  644  1                                  21    
HELIX   35  35 ASP B  650  GLY B  670  1                                  21    
HELIX   36  36 ASP B  675  VAL B  680  1                                   6    
HELIX   37  37 SER B  684  THR B  688  5                                   5    
HELIX   38  38 THR B  688  HIS B  692  5                                   5    
HELIX   39  39 ASP B  709  THR B  713  5                                   5    
SHEET    1  AA 2 LEU A 301  LYS A 304  0                                        
SHEET    2  AA 2 VAL A 311  ASP A 314 -1  O  LEU A 312   N  VAL A 303           
SHEET    1  AB 4 GLN A 425  ASP A 428  0                                        
SHEET    2  AB 4 ALA A 458  ILE A 461  1  O  ILE A 459   N  PHE A 427           
SHEET    3  AB 4 PHE A 584  SER A 585 -1  O  SER A 585   N  ALA A 458           
SHEET    4  AB 4 ALA A 566  VAL A 567 -1  O  VAL A 567   N  PHE A 584           
SHEET    1  AC 3 ARG A 473  VAL A 474  0                                        
SHEET    2  AC 3 LEU A 522  GLN A 525 -1  O  GLN A 525   N  ARG A 473           
SHEET    3  AC 3 GLU A 532  PHE A 534 -1  O  GLU A 532   N  LEU A 524           
SHEET    1  AD 2 GLY A 484  LYS A 486  0                                        
SHEET    2  AD 2 THR A 492  GLY A 494 -1  O  LEU A 493   N  TYR A 485           
SHEET    1  AE 2 GLU A 543  PRO A 545  0                                        
SHEET    2  AE 2 LYS A 560  TYR A 562 -1  O  TRP A 561   N  VAL A 544           
SHEET    1  AF 3 LEU A 577  PHE A 579  0                                        
SHEET    2  AF 3 LEU A 571  ILE A 574 -1  O  LEU A 572   N  PHE A 579           
SHEET    3  AF 3 SER A 703  GLU A 705 -1  O  SER A 703   N  GLU A 573           
SHEET    1  BA 2 LEU B 301  LYS B 304  0                                        
SHEET    2  BA 2 VAL B 311  ASP B 314 -1  O  LEU B 312   N  VAL B 303           
SHEET    1  BB 4 GLN B 425  ASP B 428  0                                        
SHEET    2  BB 4 ALA B 458  ILE B 461  1  O  ILE B 459   N  PHE B 427           
SHEET    3  BB 4 PHE B 584  SER B 585 -1  O  SER B 585   N  ALA B 458           
SHEET    4  BB 4 ALA B 566  VAL B 567 -1  O  VAL B 567   N  PHE B 584           
SHEET    1  BC 3 ARG B 473  VAL B 474  0                                        
SHEET    2  BC 3 LEU B 522  GLN B 525 -1  O  GLN B 525   N  ARG B 473           
SHEET    3  BC 3 GLU B 532  PHE B 534 -1  O  GLU B 532   N  LEU B 524           
SHEET    1  BD 2 GLY B 484  LYS B 486  0                                        
SHEET    2  BD 2 THR B 492  GLY B 494 -1  O  LEU B 493   N  TYR B 485           
SHEET    1  BE 2 GLU B 543  PRO B 545  0                                        
SHEET    2  BE 2 LYS B 560  TYR B 562 -1  O  TRP B 561   N  VAL B 544           
SHEET    1  BF 3 LEU B 577  PHE B 579  0                                        
SHEET    2  BF 3 LEU B 571  ILE B 574 -1  O  LEU B 572   N  PHE B 579           
SHEET    3  BF 3 SER B 703  GLU B 705 -1  O  SER B 703   N  GLU B 573           
SHEET    1  BG 2 TYR B 588  MET B 589  0                                        
SHEET    2  BG 2 ILE B 648  VAL B 649  1  N  VAL B 649   O  TYR B 588           
LINK         SG  CYS A 415                FE   HEM A 750     1555   1555  2.31  
LINK         SG  CYS B 415                FE   HEM B 750     1555   1555  2.38  
LINK        ZN    ZN B 900                 SG  CYS B 331     1555   1555  2.45  
LINK        ZN    ZN B 900                 SG  CYS A 331     1555   1555  2.38  
LINK        ZN    ZN B 900                 SG  CYS B 326     1555   1555  2.33  
LINK        ZN    ZN B 900                 SG  CYS A 326     1555   1555  2.36  
CISPEP   1 THR A  701    PRO A  702          0        -1.01                     
CISPEP   2 THR B  701    PRO B  702          0        -0.77                     
SITE     1 AC1 12 TRP A 409  CYS A 415  VAL A 416  SER A 457                    
SITE     2 AC1 12 PHE A 584  SER A 585  TRP A 587  TRP A 678                    
SITE     3 AC1 12 TYR A 706  H4B A 760  WOS A 800  HOH A2024                    
SITE     1 AC2 12 SER A 334  ARG A 596  VAL A 677  TRP A 678                    
SITE     2 AC2 12 HEM A 750  HOH A2082  HOH A2091  TRP B 676                    
SITE     3 AC2 12 PHE B 691  HIS B 692  GLN B 693  GLU B 694                    
SITE     1 AC3  7 VAL A 567  ASN A 569  GLY A 586  TRP A 587                    
SITE     2 AC3  7 TYR A 588  GLU A 592  HEM A 750                               
SITE     1 AC4  2 GLN A 420  TRP A 587                                          
SITE     1 AC5 14 TRP B 409  ARG B 414  CYS B 415  SER B 457                    
SITE     2 AC5 14 PHE B 584  SER B 585  GLY B 586  TRP B 587                    
SITE     3 AC5 14 GLU B 592  TRP B 678  PHE B 704  TYR B 706                    
SITE     4 AC5 14 H4B B 760  WOS B 800                                          
SITE     1 AC6 12 TRP A 676  PHE A 691  HIS A 692  GLN A 693                    
SITE     2 AC6 12 GLU A 694  SER B 334  ARG B 596  VAL B 677                    
SITE     3 AC6 12 TRP B 678  HEM B 750  HOH B2093  HOH B2103                    
SITE     1 AC7  7 VAL B 567  ASN B 569  PHE B 584  TRP B 587                    
SITE     2 AC7  7 GLU B 592  HEM B 750  HOH B2058                               
SITE     1 AC8  3 ILE B 419  TRP B 587  VAL B 649                               
SITE     1 AC9  4 CYS A 326  CYS A 331  CYS B 326  CYS B 331                    
CRYST1   51.540  111.360  163.960  90.00  90.00  90.00 P 21 21 21    1          
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      0.019402  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008980  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006099        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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