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Database: PDB
Entry: 6CIF
LinkDB: 6CIF
Original site: 6CIF 
HEADER    OXIDOREDUCTASE                          23-FEB-18   6CIF              
TITLE     STRUCTURE OF THE HUMAN ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN  
TITLE    2 IN COMPLEX WITH N-(1-(PIPERIDIN-4-YL)INDOLIN-5-YL)THIOPHENE-2-       
TITLE    3 CARBOXIMIDAMIDE                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NITRIC OXIDE SYNTHASE, ENDOTHELIAL;                        
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: CONSTITUTIVE NOS,CNOS,EC-NOS,ENDOTHELIAL NOS,ENOS,NOS TYPE  
COMPND   5 III,NOSIII;                                                          
COMPND   6 EC: 1.14.13.39;                                                      
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELL: ENDOTHELIAL;                                                   
SOURCE   6 GENE: NOS3;                                                          
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PCWORI                                    
KEYWDS    NITRIC OXIDE SYNTHASE INHIBITOR COMPLEX HEME ENZYME, OXIDOREDUCTASE   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.CHREIFI,H.LI,T.L.POULOS                                             
REVDAT   4   20-FEB-19 6CIF    1       REMARK                                   
REVDAT   3   21-NOV-18 6CIF    1       JRNL                                     
REVDAT   2   07-NOV-18 6CIF    1       JRNL                                     
REVDAT   1   31-OCT-18 6CIF    0                                                
JRNL        AUTH   H.LI,R.J.EVENSON,G.CHREIFI,R.B.SILVERMAN,T.L.POULOS          
JRNL        TITL   STRUCTURAL BASIS FOR ISOFORM SELECTIVE NITRIC OXIDE SYNTHASE 
JRNL        TITL 2 INHIBITION BY THIOPHENE-2-CARBOXIMIDAMIDES.                  
JRNL        REF    BIOCHEMISTRY                  V.  57  6319 2018              
JRNL        REFN                   ISSN 1520-4995                               
JRNL        PMID   30335983                                                     
JRNL        DOI    10.1021/ACS.BIOCHEM.8B00895                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.07                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.010                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 94090                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4713                            
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 46.0750 -  6.8287    0.93     5762   276  0.1737 0.1669        
REMARK   3     2  6.8287 -  5.4229    0.96     5877   303  0.1595 0.2155        
REMARK   3     3  5.4229 -  4.7382    0.90     5580   296  0.1456 0.2137        
REMARK   3     4  4.7382 -  4.3053    0.97     5984   294  0.1289 0.1713        
REMARK   3     5  4.3053 -  3.9969    0.98     6007   324  0.1394 0.1884        
REMARK   3     6  3.9969 -  3.7614    0.98     6117   297  0.1485 0.1996        
REMARK   3     7  3.7614 -  3.5731    0.87     5370   290  0.1558 0.2177        
REMARK   3     8  3.5731 -  3.4176    0.94     5804   320  0.1640 0.2271        
REMARK   3     9  3.4176 -  3.2861    0.96     5888   320  0.1788 0.2324        
REMARK   3    10  3.2861 -  3.1727    0.97     5947   339  0.1953 0.2801        
REMARK   3    11  3.1727 -  3.0735    0.95     5929   275  0.2015 0.2622        
REMARK   3    12  3.0735 -  2.9857    0.97     5969   263  0.1956 0.2796        
REMARK   3    13  2.9857 -  2.9071    0.96     6017   293  0.2026 0.3107        
REMARK   3    14  2.9071 -  2.8362    0.97     5865   362  0.2043 0.2531        
REMARK   3    15  2.8362 -  2.7717    0.86     5345   242  0.2281 0.2895        
REMARK   3    16  2.7717 -  2.7128    0.90     5496   305  0.2239 0.2746        
REMARK   3    17  2.7128 -  2.6585    0.94     5822   334  0.2258 0.3055        
REMARK   3    18  2.6585 -  2.6083    0.95     5807   330  0.2185 0.2744        
REMARK   3    19  2.6083 -  2.5618    0.94     5805   362  0.2305 0.3002        
REMARK   3    20  2.5618 -  2.5183    0.96     5975   275  0.2439 0.2886        
REMARK   3    21  2.5183 -  2.4777    0.96     5896   318  0.2425 0.3289        
REMARK   3    22  2.4777 -  2.4396    0.97     6015   351  0.2503 0.3053        
REMARK   3    23  2.4396 -  2.4037    0.97     5941   299  0.2503 0.3442        
REMARK   3    24  2.4037 -  2.3699    0.95     5874   329  0.2598 0.3082        
REMARK   3    25  2.3699 -  2.3378    0.96     5997   277  0.2670 0.3468        
REMARK   3    26  2.3378 -  2.3075    0.95     5711   343  0.2877 0.3463        
REMARK   3    27  2.3075 -  2.2786    0.83     5188   293  0.2953 0.3631        
REMARK   3    28  2.2786 -  2.2512    0.90     5665   240  0.2850 0.3367        
REMARK   3    29  2.2512 -  2.2250    0.95     5824   328  0.2952 0.3549        
REMARK   3    30  2.2250 -  2.2000    0.94     5779   293  0.2931 0.3408        
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)     : 0.300            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.890           
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      :  0.009          13850                                  
REMARK   3   ANGLE     :  1.150          18891                                  
REMARK   3   CHIRALITY :  0.053           1960                                  
REMARK   3   PLANARITY :  0.006           2432                                  
REMARK   3   DIHEDRAL  : 15.016           8118                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A): -49.3201  -0.0703-190.2025              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2011 T22:   0.2113                                     
REMARK   3      T33:   0.2155 T12:  -0.0489                                     
REMARK   3      T13:   0.0350 T23:  -0.0375                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2479 L22:   0.2696                                     
REMARK   3      L33:   0.6907 L12:  -0.1533                                     
REMARK   3      L13:   0.2876 L23:  -0.1970                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0534 S12:  -0.0072 S13:  -0.0245                       
REMARK   3      S21:  -0.0258 S22:  -0.0010 S23:  -0.0175                       
REMARK   3      S31:   0.0332 S32:   0.0108 S33:  -0.0373                       
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 6CIF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-FEB-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000232680.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-JUN-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 94161                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.21200                            
REMARK 200  R SYM                      (I) : 0.21200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 2.79800                            
REMARK 200  R SYM FOR SHELL            (I) : 2.79800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4DIP                                                 
REMARK 200                                                                      
REMARK 200 REMARK: RODS                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12-15% PEG3350, 0.1M BIS-TRIS 0.2-0.3M   
REMARK 280  MG ACETATE, 0.1M GDCL3 10% GLYCEROL, 5 MM TCEP, PH 7.5, VAPOR       
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       76.28950            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11070 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 34380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -146.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10870 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 33510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -145.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A    41                                                      
REMARK 465     PRO A    42                                                      
REMARK 465     ALA A    43                                                      
REMARK 465     SER A    44                                                      
REMARK 465     LEU A    45                                                      
REMARK 465     LEU A    46                                                      
REMARK 465     PRO A    47                                                      
REMARK 465     PRO A    48                                                      
REMARK 465     ALA A    49                                                      
REMARK 465     PRO A    50                                                      
REMARK 465     GLU A    51                                                      
REMARK 465     HIS A    52                                                      
REMARK 465     SER A    53                                                      
REMARK 465     PRO A    54                                                      
REMARK 465     PRO A    55                                                      
REMARK 465     SER A    56                                                      
REMARK 465     SER A    57                                                      
REMARK 465     PRO A    58                                                      
REMARK 465     LEU A    59                                                      
REMARK 465     THR A    60                                                      
REMARK 465     GLN A    61                                                      
REMARK 465     PRO A    62                                                      
REMARK 465     PRO A    63                                                      
REMARK 465     GLU A    64                                                      
REMARK 465     GLY A    65                                                      
REMARK 465     PRO A    66                                                      
REMARK 465     LYS A    67                                                      
REMARK 465     GLN A   110                                                      
REMARK 465     GLY A   111                                                      
REMARK 465     ARG A   112                                                      
REMARK 465     PRO A   113                                                      
REMARK 465     SER A   114                                                      
REMARK 465     PRO A   115                                                      
REMARK 465     GLY A   116                                                      
REMARK 465     PRO A   117                                                      
REMARK 465     PRO A   118                                                      
REMARK 465     ALA B    41                                                      
REMARK 465     PRO B    42                                                      
REMARK 465     ALA B    43                                                      
REMARK 465     SER B    44                                                      
REMARK 465     LEU B    45                                                      
REMARK 465     LEU B    46                                                      
REMARK 465     PRO B    47                                                      
REMARK 465     PRO B    48                                                      
REMARK 465     ALA B    49                                                      
REMARK 465     PRO B    50                                                      
REMARK 465     GLU B    51                                                      
REMARK 465     HIS B    52                                                      
REMARK 465     SER B    53                                                      
REMARK 465     PRO B    54                                                      
REMARK 465     PRO B    55                                                      
REMARK 465     SER B    56                                                      
REMARK 465     SER B    57                                                      
REMARK 465     PRO B    58                                                      
REMARK 465     LEU B    59                                                      
REMARK 465     THR B    60                                                      
REMARK 465     GLN B    61                                                      
REMARK 465     PRO B    62                                                      
REMARK 465     PRO B    63                                                      
REMARK 465     GLU B    64                                                      
REMARK 465     GLY B    65                                                      
REMARK 465     PRO B    66                                                      
REMARK 465     LYS B   108                                                      
REMARK 465     LEU B   109                                                      
REMARK 465     GLN B   110                                                      
REMARK 465     GLY B   111                                                      
REMARK 465     ARG B   112                                                      
REMARK 465     PRO B   113                                                      
REMARK 465     SER B   114                                                      
REMARK 465     PRO B   115                                                      
REMARK 465     GLY B   116                                                      
REMARK 465     PRO B   117                                                      
REMARK 465     PRO B   118                                                      
REMARK 465     ALA C    41                                                      
REMARK 465     PRO C    42                                                      
REMARK 465     ALA C    43                                                      
REMARK 465     SER C    44                                                      
REMARK 465     LEU C    45                                                      
REMARK 465     LEU C    46                                                      
REMARK 465     PRO C    47                                                      
REMARK 465     PRO C    48                                                      
REMARK 465     ALA C    49                                                      
REMARK 465     PRO C    50                                                      
REMARK 465     GLU C    51                                                      
REMARK 465     HIS C    52                                                      
REMARK 465     SER C    53                                                      
REMARK 465     PRO C    54                                                      
REMARK 465     PRO C    55                                                      
REMARK 465     SER C    56                                                      
REMARK 465     SER C    57                                                      
REMARK 465     PRO C    58                                                      
REMARK 465     LEU C    59                                                      
REMARK 465     THR C    60                                                      
REMARK 465     GLN C    61                                                      
REMARK 465     PRO C    62                                                      
REMARK 465     PRO C    63                                                      
REMARK 465     GLU C    64                                                      
REMARK 465     GLY C    65                                                      
REMARK 465     PRO C    66                                                      
REMARK 465     LYS C    67                                                      
REMARK 465     ARG C   107                                                      
REMARK 465     LYS C   108                                                      
REMARK 465     LEU C   109                                                      
REMARK 465     GLN C   110                                                      
REMARK 465     GLY C   111                                                      
REMARK 465     ARG C   112                                                      
REMARK 465     PRO C   113                                                      
REMARK 465     SER C   114                                                      
REMARK 465     PRO C   115                                                      
REMARK 465     GLY C   116                                                      
REMARK 465     PRO C   117                                                      
REMARK 465     PRO C   118                                                      
REMARK 465     ALA D    41                                                      
REMARK 465     PRO D    42                                                      
REMARK 465     ALA D    43                                                      
REMARK 465     SER D    44                                                      
REMARK 465     LEU D    45                                                      
REMARK 465     LEU D    46                                                      
REMARK 465     PRO D    47                                                      
REMARK 465     PRO D    48                                                      
REMARK 465     ALA D    49                                                      
REMARK 465     PRO D    50                                                      
REMARK 465     GLU D    51                                                      
REMARK 465     HIS D    52                                                      
REMARK 465     SER D    53                                                      
REMARK 465     PRO D    54                                                      
REMARK 465     PRO D    55                                                      
REMARK 465     SER D    56                                                      
REMARK 465     SER D    57                                                      
REMARK 465     PRO D    58                                                      
REMARK 465     LEU D    59                                                      
REMARK 465     THR D    60                                                      
REMARK 465     GLN D    61                                                      
REMARK 465     PRO D    62                                                      
REMARK 465     PRO D    63                                                      
REMARK 465     GLU D    64                                                      
REMARK 465     GLY D    65                                                      
REMARK 465     PRO D    66                                                      
REMARK 465     LEU D   109                                                      
REMARK 465     GLN D   110                                                      
REMARK 465     GLY D   111                                                      
REMARK 465     ARG D   112                                                      
REMARK 465     PRO D   113                                                      
REMARK 465     SER D   114                                                      
REMARK 465     PRO D   115                                                      
REMARK 465     GLY D   116                                                      
REMARK 465     PRO D   117                                                      
REMARK 465     PRO D   118                                                      
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   OH   TYR D   475     O2D  HEM D   501              2.04            
REMARK 500   OE1  GLU D   321     O4   BTB D   504              2.05            
REMARK 500   OE1  GLU C   167     O    HOH C   601              2.08            
REMARK 500   OE2  GLU B   342     O    HOH B   601              2.10            
REMARK 500   O    HOH C   609     O    HOH C   625              2.12            
REMARK 500   OD2  ASP A   384     O3   BTB A   504              2.14            
REMARK 500   OE2  GLU A   298     O    HOH A   601              2.14            
REMARK 500   O    HOH B   755     O    HOH B   761              2.15            
REMARK 500   O    HOH C   715     O    HOH C   716              2.16            
REMARK 500   N    PHE A    68     O    HOH A   602              2.17            
REMARK 500   O    ASN C   132     OG   SER C   136              2.17            
REMARK 500   NE2  GLN A   256     O    HOH A   603              2.18            
REMARK 500   O    ARG C   234     O    HOH C   602              2.18            
REMARK 500   O    HOH B   680     O    HOH B   736              2.19            
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   OE2  GLU C   152     O3   BTB B   505     2352     2.13            
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    GLN A  89     -105.97    -99.47                                   
REMARK 500    ARG A 107     -147.00     50.50                                   
REMARK 500    PRO A 120       33.88    -81.05                                   
REMARK 500    ILE A 138       34.64    -94.24                                   
REMARK 500    LYS A 139      -43.35     79.83                                   
REMARK 500    SER A 143     -148.21     48.73                                   
REMARK 500    GLN A 144     -146.78     57.36                                   
REMARK 500    ARG A 238      -74.18   -143.10                                   
REMARK 500    PRO A 281      170.36    -56.96                                   
REMARK 500    ASP A 297      -46.60     68.40                                   
REMARK 500    ARG A 372     -133.62   -111.40                                   
REMARK 500    CYS A 441      113.33   -171.48                                   
REMARK 500    ARG B 140       34.52   -145.69                                   
REMARK 500    ALA B 351       70.85   -153.65                                   
REMARK 500    ARG B 372     -129.66   -114.15                                   
REMARK 500    CYS B 441      114.87   -169.82                                   
REMARK 500    ALA C  86        0.22    -59.29                                   
REMARK 500    LYS C 139      -22.12     82.75                                   
REMARK 500    THR C 162     -160.25   -125.82                                   
REMARK 500    ARG C 238     -176.51     65.81                                   
REMARK 500    HIS C 277       34.73    -85.71                                   
REMARK 500    ASP C 297      -21.94     67.45                                   
REMARK 500    ALA C 351       63.86   -152.31                                   
REMARK 500    ARG C 372     -135.78   -119.87                                   
REMARK 500    GLN D  89       75.04   -164.79                                   
REMARK 500    ARG D 140       37.31   -145.19                                   
REMARK 500    THR D 160       -5.30   -147.25                                   
REMARK 500    ALA D 351       75.11   -154.70                                   
REMARK 500    ARG D 372     -127.86   -117.40                                   
REMARK 500    CYS D 441      119.61   -162.98                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLN D   89     GLN D   90                  127.92                    
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 A 702        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH B 783        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH B 784        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH B 785        DISTANCE =  6.20 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 506  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  94   SG                                                     
REMARK 620 2 CYS A  99   SG  104.1                                              
REMARK 620 3 CYS B  94   SG  123.6 106.8                                        
REMARK 620 4 CYS B  99   SG  110.9 103.8 105.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 501  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 184   SG                                                     
REMARK 620 2 HEM A 501   NA   99.0                                              
REMARK 620 3 HEM A 501   NB   97.9  88.1                                        
REMARK 620 4 HEM A 501   NC   99.5 161.4  91.0                                  
REMARK 620 5 HEM A 501   ND  103.9  89.3 158.2  84.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 501  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 184   SG                                                     
REMARK 620 2 HEM B 501   NA  100.4                                              
REMARK 620 3 HEM B 501   NB  101.2  90.7                                        
REMARK 620 4 HEM B 501   NC   98.1 161.5  86.6                                  
REMARK 620 5 HEM B 501   ND  100.2  87.7 158.5  88.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              GD B 508  GD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B 319   O                                                      
REMARK 620 2 GLU B 321   OE1  82.5                                              
REMARK 620 3 BTB B 504   O3   77.2 120.5                                        
REMARK 620 4 BTB B 504   O4   92.8  66.6  59.4                                  
REMARK 620 5 BTB B 504   N   139.3 107.3  63.6  58.6                            
REMARK 620 6 BTB B 504   O6  121.9 144.0  92.4 130.4  72.6                      
REMARK 620 7 BTB B 504   O8  150.2  68.0 121.3  80.1  59.3  83.0                
REMARK 620 8 HOH B 602   O    72.6 132.3  93.2 151.7 118.2  50.8 124.4          
REMARK 620 9 HOH C 611   O    83.4  75.2 152.5 141.8 137.3  81.5  84.7  62.2    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 507  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  94   SG                                                     
REMARK 620 2 CYS C  99   SG  104.3                                              
REMARK 620 3 CYS D  94   SG  122.9 112.2                                        
REMARK 620 4 CYS D  99   SG  108.1 102.6 105.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 501  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 184   SG                                                     
REMARK 620 2 HEM C 501   NA  102.1                                              
REMARK 620 3 HEM C 501   NB  102.4  86.6                                        
REMARK 620 4 HEM C 501   NC   97.3 160.6  89.4                                  
REMARK 620 5 HEM C 501   ND   99.8  89.7 157.8  86.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              GD C 510  GD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 384   OD1                                                    
REMARK 620 2 HOH C 710   O   141.6                                              
REMARK 620 3 HOH B 755   O   127.3  61.8                                        
REMARK 620 4 HOH B 761   O    91.3  75.5  41.4                                  
REMARK 620 5 HOH C 690   O    65.4  82.5 132.9 103.3                            
REMARK 620 6 GLN A 257   NE2 119.1  44.9  32.2  31.3 100.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM D 501  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 184   SG                                                     
REMARK 620 2 HEM D 501   NA  100.8                                              
REMARK 620 3 HEM D 501   NB  101.1  90.5                                        
REMARK 620 4 HEM D 501   NC   97.9 161.2  87.5                                  
REMARK 620 5 HEM D 501   ND  101.4  86.2 157.5  88.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              GD D 507  GD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR D 319   O                                                      
REMARK 620 2 GLU D 321   OE1  82.4                                              
REMARK 620 3 GLU D 321   OE2  87.4  44.1                                        
REMARK 620 4 BTB D 504   O3   73.8  90.9 133.6                                  
REMARK 620 5 BTB D 504   O4   94.0  39.9  82.5  57.9                            
REMARK 620 6 BTB D 504   N   139.7  91.2 115.0  66.5  59.2                      
REMARK 620 7 BTB D 504   O6  131.1 144.7 116.3 107.6 129.2  70.4                
REMARK 620 8 BTB D 504   O8  144.8  67.2  58.6 122.0  74.3  61.4  77.5          
REMARK 620 9 HOH D 698   O    87.2 107.3  63.8 151.9 146.1 132.2  69.5  85.4    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              GD A 509  GD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 692   O                                                      
REMARK 620 2 HOH A 696   O   111.6                                              
REMARK 620 3 HOH A 691   O   127.4  48.2                                        
REMARK 620 4 HOH A 702   O    66.0 144.9 103.3                                  
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 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue F2J A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 506                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 508                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GD A 509                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue F2J B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB B 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB B 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB B 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GD B 508                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue F2J C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB C 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 509                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GD C 510                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B D 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue F2J D 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB D 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB D 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB D 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GD D 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 508                  
DBREF  6CIF A   41   480  UNP    P29474   NOS3_HUMAN      41    480             
DBREF  6CIF B   41   480  UNP    P29474   NOS3_HUMAN      41    480             
DBREF  6CIF C   41   480  UNP    P29474   NOS3_HUMAN      41    480             
DBREF  6CIF D   41   480  UNP    P29474   NOS3_HUMAN      41    480             
SEQRES   1 A  440  ALA PRO ALA SER LEU LEU PRO PRO ALA PRO GLU HIS SER          
SEQRES   2 A  440  PRO PRO SER SER PRO LEU THR GLN PRO PRO GLU GLY PRO          
SEQRES   3 A  440  LYS PHE PRO ARG VAL LYS ASN TRP GLU VAL GLY SER ILE          
SEQRES   4 A  440  THR TYR ASP THR LEU SER ALA GLN ALA GLN GLN ASP GLY          
SEQRES   5 A  440  PRO CYS THR PRO ARG ARG CYS LEU GLY SER LEU VAL PHE          
SEQRES   6 A  440  PRO ARG LYS LEU GLN GLY ARG PRO SER PRO GLY PRO PRO          
SEQRES   7 A  440  ALA PRO GLU GLN LEU LEU SER GLN ALA ARG ASP PHE ILE          
SEQRES   8 A  440  ASN GLN TYR TYR SER SER ILE LYS ARG SER GLY SER GLN          
SEQRES   9 A  440  ALA HIS GLU GLN ARG LEU GLN GLU VAL GLU ALA GLU VAL          
SEQRES  10 A  440  ALA ALA THR GLY THR TYR GLN LEU ARG GLU SER GLU LEU          
SEQRES  11 A  440  VAL PHE GLY ALA LYS GLN ALA TRP ARG ASN ALA PRO ARG          
SEQRES  12 A  440  CYS VAL GLY ARG ILE GLN TRP GLY LYS LEU GLN VAL PHE          
SEQRES  13 A  440  ASP ALA ARG ASP CYS ARG SER ALA GLN GLU MET PHE THR          
SEQRES  14 A  440  TYR ILE CYS ASN HIS ILE LYS TYR ALA THR ASN ARG GLY          
SEQRES  15 A  440  ASN LEU ARG SER ALA ILE THR VAL PHE PRO GLN ARG CYS          
SEQRES  16 A  440  PRO GLY ARG GLY ASP PHE ARG ILE TRP ASN SER GLN LEU          
SEQRES  17 A  440  VAL ARG TYR ALA GLY TYR ARG GLN GLN ASP GLY SER VAL          
SEQRES  18 A  440  ARG GLY ASP PRO ALA ASN VAL GLU ILE THR GLU LEU CYS          
SEQRES  19 A  440  ILE GLN HIS GLY TRP THR PRO GLY ASN GLY ARG PHE ASP          
SEQRES  20 A  440  VAL LEU PRO LEU LEU LEU GLN ALA PRO ASP GLU PRO PRO          
SEQRES  21 A  440  GLU LEU PHE LEU LEU PRO PRO GLU LEU VAL LEU GLU VAL          
SEQRES  22 A  440  PRO LEU GLU HIS PRO THR LEU GLU TRP PHE ALA ALA LEU          
SEQRES  23 A  440  GLY LEU ARG TRP TYR ALA LEU PRO ALA VAL SER ASN MET          
SEQRES  24 A  440  LEU LEU GLU ILE GLY GLY LEU GLU PHE PRO ALA ALA PRO          
SEQRES  25 A  440  PHE SER GLY TRP TYR MET SER THR GLU ILE GLY THR ARG          
SEQRES  26 A  440  ASN LEU CYS ASP PRO HIS ARG TYR ASN ILE LEU GLU ASP          
SEQRES  27 A  440  VAL ALA VAL CYS MET ASP LEU ASP THR ARG THR THR SER          
SEQRES  28 A  440  SER LEU TRP LYS ASP LYS ALA ALA VAL GLU ILE ASN VAL          
SEQRES  29 A  440  ALA VAL LEU HIS SER TYR GLN LEU ALA LYS VAL THR ILE          
SEQRES  30 A  440  VAL ASP HIS HIS ALA ALA THR ALA SER PHE MET LYS HIS          
SEQRES  31 A  440  LEU GLU ASN GLU GLN LYS ALA ARG GLY GLY CYS PRO ALA          
SEQRES  32 A  440  ASP TRP ALA TRP ILE VAL PRO PRO ILE SER GLY SER LEU          
SEQRES  33 A  440  THR PRO VAL PHE HIS GLN GLU MET VAL ASN TYR PHE LEU          
SEQRES  34 A  440  SER PRO ALA PHE ARG TYR GLN PRO ASP PRO TRP                  
SEQRES   1 B  440  ALA PRO ALA SER LEU LEU PRO PRO ALA PRO GLU HIS SER          
SEQRES   2 B  440  PRO PRO SER SER PRO LEU THR GLN PRO PRO GLU GLY PRO          
SEQRES   3 B  440  LYS PHE PRO ARG VAL LYS ASN TRP GLU VAL GLY SER ILE          
SEQRES   4 B  440  THR TYR ASP THR LEU SER ALA GLN ALA GLN GLN ASP GLY          
SEQRES   5 B  440  PRO CYS THR PRO ARG ARG CYS LEU GLY SER LEU VAL PHE          
SEQRES   6 B  440  PRO ARG LYS LEU GLN GLY ARG PRO SER PRO GLY PRO PRO          
SEQRES   7 B  440  ALA PRO GLU GLN LEU LEU SER GLN ALA ARG ASP PHE ILE          
SEQRES   8 B  440  ASN GLN TYR TYR SER SER ILE LYS ARG SER GLY SER GLN          
SEQRES   9 B  440  ALA HIS GLU GLN ARG LEU GLN GLU VAL GLU ALA GLU VAL          
SEQRES  10 B  440  ALA ALA THR GLY THR TYR GLN LEU ARG GLU SER GLU LEU          
SEQRES  11 B  440  VAL PHE GLY ALA LYS GLN ALA TRP ARG ASN ALA PRO ARG          
SEQRES  12 B  440  CYS VAL GLY ARG ILE GLN TRP GLY LYS LEU GLN VAL PHE          
SEQRES  13 B  440  ASP ALA ARG ASP CYS ARG SER ALA GLN GLU MET PHE THR          
SEQRES  14 B  440  TYR ILE CYS ASN HIS ILE LYS TYR ALA THR ASN ARG GLY          
SEQRES  15 B  440  ASN LEU ARG SER ALA ILE THR VAL PHE PRO GLN ARG CYS          
SEQRES  16 B  440  PRO GLY ARG GLY ASP PHE ARG ILE TRP ASN SER GLN LEU          
SEQRES  17 B  440  VAL ARG TYR ALA GLY TYR ARG GLN GLN ASP GLY SER VAL          
SEQRES  18 B  440  ARG GLY ASP PRO ALA ASN VAL GLU ILE THR GLU LEU CYS          
SEQRES  19 B  440  ILE GLN HIS GLY TRP THR PRO GLY ASN GLY ARG PHE ASP          
SEQRES  20 B  440  VAL LEU PRO LEU LEU LEU GLN ALA PRO ASP GLU PRO PRO          
SEQRES  21 B  440  GLU LEU PHE LEU LEU PRO PRO GLU LEU VAL LEU GLU VAL          
SEQRES  22 B  440  PRO LEU GLU HIS PRO THR LEU GLU TRP PHE ALA ALA LEU          
SEQRES  23 B  440  GLY LEU ARG TRP TYR ALA LEU PRO ALA VAL SER ASN MET          
SEQRES  24 B  440  LEU LEU GLU ILE GLY GLY LEU GLU PHE PRO ALA ALA PRO          
SEQRES  25 B  440  PHE SER GLY TRP TYR MET SER THR GLU ILE GLY THR ARG          
SEQRES  26 B  440  ASN LEU CYS ASP PRO HIS ARG TYR ASN ILE LEU GLU ASP          
SEQRES  27 B  440  VAL ALA VAL CYS MET ASP LEU ASP THR ARG THR THR SER          
SEQRES  28 B  440  SER LEU TRP LYS ASP LYS ALA ALA VAL GLU ILE ASN VAL          
SEQRES  29 B  440  ALA VAL LEU HIS SER TYR GLN LEU ALA LYS VAL THR ILE          
SEQRES  30 B  440  VAL ASP HIS HIS ALA ALA THR ALA SER PHE MET LYS HIS          
SEQRES  31 B  440  LEU GLU ASN GLU GLN LYS ALA ARG GLY GLY CYS PRO ALA          
SEQRES  32 B  440  ASP TRP ALA TRP ILE VAL PRO PRO ILE SER GLY SER LEU          
SEQRES  33 B  440  THR PRO VAL PHE HIS GLN GLU MET VAL ASN TYR PHE LEU          
SEQRES  34 B  440  SER PRO ALA PHE ARG TYR GLN PRO ASP PRO TRP                  
SEQRES   1 C  440  ALA PRO ALA SER LEU LEU PRO PRO ALA PRO GLU HIS SER          
SEQRES   2 C  440  PRO PRO SER SER PRO LEU THR GLN PRO PRO GLU GLY PRO          
SEQRES   3 C  440  LYS PHE PRO ARG VAL LYS ASN TRP GLU VAL GLY SER ILE          
SEQRES   4 C  440  THR TYR ASP THR LEU SER ALA GLN ALA GLN GLN ASP GLY          
SEQRES   5 C  440  PRO CYS THR PRO ARG ARG CYS LEU GLY SER LEU VAL PHE          
SEQRES   6 C  440  PRO ARG LYS LEU GLN GLY ARG PRO SER PRO GLY PRO PRO          
SEQRES   7 C  440  ALA PRO GLU GLN LEU LEU SER GLN ALA ARG ASP PHE ILE          
SEQRES   8 C  440  ASN GLN TYR TYR SER SER ILE LYS ARG SER GLY SER GLN          
SEQRES   9 C  440  ALA HIS GLU GLN ARG LEU GLN GLU VAL GLU ALA GLU VAL          
SEQRES  10 C  440  ALA ALA THR GLY THR TYR GLN LEU ARG GLU SER GLU LEU          
SEQRES  11 C  440  VAL PHE GLY ALA LYS GLN ALA TRP ARG ASN ALA PRO ARG          
SEQRES  12 C  440  CYS VAL GLY ARG ILE GLN TRP GLY LYS LEU GLN VAL PHE          
SEQRES  13 C  440  ASP ALA ARG ASP CYS ARG SER ALA GLN GLU MET PHE THR          
SEQRES  14 C  440  TYR ILE CYS ASN HIS ILE LYS TYR ALA THR ASN ARG GLY          
SEQRES  15 C  440  ASN LEU ARG SER ALA ILE THR VAL PHE PRO GLN ARG CYS          
SEQRES  16 C  440  PRO GLY ARG GLY ASP PHE ARG ILE TRP ASN SER GLN LEU          
SEQRES  17 C  440  VAL ARG TYR ALA GLY TYR ARG GLN GLN ASP GLY SER VAL          
SEQRES  18 C  440  ARG GLY ASP PRO ALA ASN VAL GLU ILE THR GLU LEU CYS          
SEQRES  19 C  440  ILE GLN HIS GLY TRP THR PRO GLY ASN GLY ARG PHE ASP          
SEQRES  20 C  440  VAL LEU PRO LEU LEU LEU GLN ALA PRO ASP GLU PRO PRO          
SEQRES  21 C  440  GLU LEU PHE LEU LEU PRO PRO GLU LEU VAL LEU GLU VAL          
SEQRES  22 C  440  PRO LEU GLU HIS PRO THR LEU GLU TRP PHE ALA ALA LEU          
SEQRES  23 C  440  GLY LEU ARG TRP TYR ALA LEU PRO ALA VAL SER ASN MET          
SEQRES  24 C  440  LEU LEU GLU ILE GLY GLY LEU GLU PHE PRO ALA ALA PRO          
SEQRES  25 C  440  PHE SER GLY TRP TYR MET SER THR GLU ILE GLY THR ARG          
SEQRES  26 C  440  ASN LEU CYS ASP PRO HIS ARG TYR ASN ILE LEU GLU ASP          
SEQRES  27 C  440  VAL ALA VAL CYS MET ASP LEU ASP THR ARG THR THR SER          
SEQRES  28 C  440  SER LEU TRP LYS ASP LYS ALA ALA VAL GLU ILE ASN VAL          
SEQRES  29 C  440  ALA VAL LEU HIS SER TYR GLN LEU ALA LYS VAL THR ILE          
SEQRES  30 C  440  VAL ASP HIS HIS ALA ALA THR ALA SER PHE MET LYS HIS          
SEQRES  31 C  440  LEU GLU ASN GLU GLN LYS ALA ARG GLY GLY CYS PRO ALA          
SEQRES  32 C  440  ASP TRP ALA TRP ILE VAL PRO PRO ILE SER GLY SER LEU          
SEQRES  33 C  440  THR PRO VAL PHE HIS GLN GLU MET VAL ASN TYR PHE LEU          
SEQRES  34 C  440  SER PRO ALA PHE ARG TYR GLN PRO ASP PRO TRP                  
SEQRES   1 D  440  ALA PRO ALA SER LEU LEU PRO PRO ALA PRO GLU HIS SER          
SEQRES   2 D  440  PRO PRO SER SER PRO LEU THR GLN PRO PRO GLU GLY PRO          
SEQRES   3 D  440  LYS PHE PRO ARG VAL LYS ASN TRP GLU VAL GLY SER ILE          
SEQRES   4 D  440  THR TYR ASP THR LEU SER ALA GLN ALA GLN GLN ASP GLY          
SEQRES   5 D  440  PRO CYS THR PRO ARG ARG CYS LEU GLY SER LEU VAL PHE          
SEQRES   6 D  440  PRO ARG LYS LEU GLN GLY ARG PRO SER PRO GLY PRO PRO          
SEQRES   7 D  440  ALA PRO GLU GLN LEU LEU SER GLN ALA ARG ASP PHE ILE          
SEQRES   8 D  440  ASN GLN TYR TYR SER SER ILE LYS ARG SER GLY SER GLN          
SEQRES   9 D  440  ALA HIS GLU GLN ARG LEU GLN GLU VAL GLU ALA GLU VAL          
SEQRES  10 D  440  ALA ALA THR GLY THR TYR GLN LEU ARG GLU SER GLU LEU          
SEQRES  11 D  440  VAL PHE GLY ALA LYS GLN ALA TRP ARG ASN ALA PRO ARG          
SEQRES  12 D  440  CYS VAL GLY ARG ILE GLN TRP GLY LYS LEU GLN VAL PHE          
SEQRES  13 D  440  ASP ALA ARG ASP CYS ARG SER ALA GLN GLU MET PHE THR          
SEQRES  14 D  440  TYR ILE CYS ASN HIS ILE LYS TYR ALA THR ASN ARG GLY          
SEQRES  15 D  440  ASN LEU ARG SER ALA ILE THR VAL PHE PRO GLN ARG CYS          
SEQRES  16 D  440  PRO GLY ARG GLY ASP PHE ARG ILE TRP ASN SER GLN LEU          
SEQRES  17 D  440  VAL ARG TYR ALA GLY TYR ARG GLN GLN ASP GLY SER VAL          
SEQRES  18 D  440  ARG GLY ASP PRO ALA ASN VAL GLU ILE THR GLU LEU CYS          
SEQRES  19 D  440  ILE GLN HIS GLY TRP THR PRO GLY ASN GLY ARG PHE ASP          
SEQRES  20 D  440  VAL LEU PRO LEU LEU LEU GLN ALA PRO ASP GLU PRO PRO          
SEQRES  21 D  440  GLU LEU PHE LEU LEU PRO PRO GLU LEU VAL LEU GLU VAL          
SEQRES  22 D  440  PRO LEU GLU HIS PRO THR LEU GLU TRP PHE ALA ALA LEU          
SEQRES  23 D  440  GLY LEU ARG TRP TYR ALA LEU PRO ALA VAL SER ASN MET          
SEQRES  24 D  440  LEU LEU GLU ILE GLY GLY LEU GLU PHE PRO ALA ALA PRO          
SEQRES  25 D  440  PHE SER GLY TRP TYR MET SER THR GLU ILE GLY THR ARG          
SEQRES  26 D  440  ASN LEU CYS ASP PRO HIS ARG TYR ASN ILE LEU GLU ASP          
SEQRES  27 D  440  VAL ALA VAL CYS MET ASP LEU ASP THR ARG THR THR SER          
SEQRES  28 D  440  SER LEU TRP LYS ASP LYS ALA ALA VAL GLU ILE ASN VAL          
SEQRES  29 D  440  ALA VAL LEU HIS SER TYR GLN LEU ALA LYS VAL THR ILE          
SEQRES  30 D  440  VAL ASP HIS HIS ALA ALA THR ALA SER PHE MET LYS HIS          
SEQRES  31 D  440  LEU GLU ASN GLU GLN LYS ALA ARG GLY GLY CYS PRO ALA          
SEQRES  32 D  440  ASP TRP ALA TRP ILE VAL PRO PRO ILE SER GLY SER LEU          
SEQRES  33 D  440  THR PRO VAL PHE HIS GLN GLU MET VAL ASN TYR PHE LEU          
SEQRES  34 D  440  SER PRO ALA PHE ARG TYR GLN PRO ASP PRO TRP                  
HET    HEM  A 501      43                                                       
HET    H4B  A 502      17                                                       
HET    F2J  A 503      23                                                       
HET    BTB  A 504      14                                                       
HET    BTB  A 505      14                                                       
HET     ZN  A 506       1                                                       
HET    GOL  A 507       6                                                       
HET     CL  A 508       1                                                       
HET     GD  A 509       1                                                       
HET    HEM  B 501      43                                                       
HET    H4B  B 502      17                                                       
HET    F2J  B 503      23                                                       
HET    BTB  B 504      14                                                       
HET    BTB  B 505      14                                                       
HET    BTB  B 506      14                                                       
HET     CL  B 507       1                                                       
HET     GD  B 508       1                                                       
HET    HEM  C 501      43                                                       
HET    H4B  C 502      17                                                       
HET    F2J  C 503      23                                                       
HET    BTB  C 504      14                                                       
HET    BTB  C 505      14                                                       
HET    BTB  C 506      14                                                       
HET     ZN  C 507       1                                                       
HET    GOL  C 508       6                                                       
HET     CL  C 509       1                                                       
HET     GD  C 510       1                                                       
HET    HEM  D 501      43                                                       
HET    H4B  D 502      17                                                       
HET    F2J  D 503      23                                                       
HET    BTB  D 504      14                                                       
HET    BTB  D 505      14                                                       
HET    BTB  D 506      14                                                       
HET     GD  D 507       1                                                       
HET     CL  D 508       1                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     H4B 5,6,7,8-TETRAHYDROBIOPTERIN                                      
HETNAM     F2J N-[1-(PIPERIDIN-4-YL)-1H-INDOL-5-YL]THIOPHENE-2-                 
HETNAM   2 F2J  CARBOXIMIDAMIDE                                                 
HETNAM     BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-                 
HETNAM   2 BTB  PROPANE-1,3-DIOL                                                
HETNAM      ZN ZINC ION                                                         
HETNAM     GOL GLYCEROL                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM      GD GADOLINIUM ATOM                                                  
HETSYN     HEM HEME                                                             
HETSYN     BTB BIS-TRIS BUFFER                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL   6  H4B    4(C9 H15 N5 O3)                                              
FORMUL   7  F2J    4(C18 H20 N4 S)                                              
FORMUL   8  BTB    11(C8 H19 N O5)                                              
FORMUL  10   ZN    2(ZN 2+)                                                     
FORMUL  11  GOL    2(C3 H8 O3)                                                  
FORMUL  12   CL    4(CL 1-)                                                     
FORMUL  13   GD    4(GD)                                                        
FORMUL  40  HOH   *565(H2 O)                                                    
HELIX    1 AA1 THR A   83  ALA A   88  5                                   6    
HELIX    2 AA2 PRO A  120  ILE A  138  1                                  19    
HELIX    3 AA3 SER A  143  GLY A  161  1                                  19    
HELIX    4 AA4 ARG A  166  ASN A  180  1                                  15    
HELIX    5 AA5 GLY A  186  TRP A  190  5                                   5    
HELIX    6 AA6 SER A  203  ASN A  220  1                                  18    
HELIX    7 AA7 ARG A  221  ASN A  223  5                                   3    
HELIX    8 AA8 ASN A  267  HIS A  277  1                                  11    
HELIX    9 AA9 PRO A  306  VAL A  310  5                                   5    
HELIX   10 AB1 LEU A  320  GLY A  327  5                                   8    
HELIX   11 AB2 SER A  359  THR A  364  1                                   6    
HELIX   12 AB3 THR A  364  ASP A  369  1                                   6    
HELIX   13 AB4 ILE A  375  MET A  383  1                                   9    
HELIX   14 AB5 THR A  389  SER A  392  5                                   4    
HELIX   15 AB6 LEU A  393  ALA A  413  1                                  21    
HELIX   16 AB7 ASP A  419  GLY A  439  1                                  21    
HELIX   17 AB8 ASP A  444  VAL A  449  1                                   6    
HELIX   18 AB9 SER A  453  GLN A  462  5                                  10    
HELIX   19 AC1 THR B   83  ALA B   88  5                                   6    
HELIX   20 AC2 PRO B  120  ILE B  138  1                                  19    
HELIX   21 AC3 SER B  143  GLY B  161  1                                  19    
HELIX   22 AC4 ARG B  166  ALA B  181  1                                  16    
HELIX   23 AC5 GLY B  186  TRP B  190  5                                   5    
HELIX   24 AC6 SER B  203  ASN B  220  1                                  18    
HELIX   25 AC7 ARG B  221  ASN B  223  5                                   3    
HELIX   26 AC8 ASN B  267  HIS B  277  1                                  11    
HELIX   27 AC9 PRO B  306  VAL B  310  5                                   5    
HELIX   28 AD1 LEU B  320  GLY B  327  5                                   8    
HELIX   29 AD2 MET B  358  THR B  364  1                                   7    
HELIX   30 AD3 THR B  364  ASP B  369  1                                   6    
HELIX   31 AD4 ILE B  375  MET B  383  1                                   9    
HELIX   32 AD5 THR B  389  SER B  392  5                                   4    
HELIX   33 AD6 LEU B  393  ALA B  413  1                                  21    
HELIX   34 AD7 ASP B  419  GLY B  439  1                                  21    
HELIX   35 AD8 ASP B  444  VAL B  449  1                                   6    
HELIX   36 AD9 SER B  453  GLN B  462  5                                  10    
HELIX   37 AE1 THR C   83  ALA C   88  5                                   6    
HELIX   38 AE2 PRO C  120  SER C  137  1                                  18    
HELIX   39 AE3 GLN C  144  GLY C  161  1                                  18    
HELIX   40 AE4 ARG C  166  ALA C  181  1                                  16    
HELIX   41 AE5 GLY C  186  TRP C  190  5                                   5    
HELIX   42 AE6 SER C  203  ASN C  220  1                                  18    
HELIX   43 AE7 ARG C  221  ASN C  223  5                                   3    
HELIX   44 AE8 ASN C  267  HIS C  277  1                                  11    
HELIX   45 AE9 PRO C  306  VAL C  310  5                                   5    
HELIX   46 AF1 LEU C  320  GLY C  327  5                                   8    
HELIX   47 AF2 SER C  359  THR C  364  1                                   6    
HELIX   48 AF3 THR C  364  ASP C  369  1                                   6    
HELIX   49 AF4 ILE C  375  MET C  383  1                                   9    
HELIX   50 AF5 THR C  389  SER C  392  5                                   4    
HELIX   51 AF6 LEU C  393  ALA C  413  1                                  21    
HELIX   52 AF7 ASP C  419  GLY C  439  1                                  21    
HELIX   53 AF8 ASP C  444  VAL C  449  1                                   6    
HELIX   54 AF9 SER C  453  GLN C  462  5                                  10    
HELIX   55 AG1 THR D   83  ALA D   88  5                                   6    
HELIX   56 AG2 PRO D  120  ILE D  138  1                                  19    
HELIX   57 AG3 SER D  143  GLY D  161  1                                  19    
HELIX   58 AG4 ARG D  166  ASN D  180  1                                  15    
HELIX   59 AG5 GLY D  186  TRP D  190  5                                   5    
HELIX   60 AG6 SER D  203  ASN D  220  1                                  18    
HELIX   61 AG7 ARG D  221  ASN D  223  5                                   3    
HELIX   62 AG8 ASN D  267  HIS D  277  1                                  11    
HELIX   63 AG9 PRO D  306  VAL D  310  5                                   5    
HELIX   64 AH1 LEU D  320  GLY D  327  5                                   8    
HELIX   65 AH2 MET D  358  THR D  364  1                                   7    
HELIX   66 AH3 THR D  364  ASP D  369  1                                   6    
HELIX   67 AH4 ILE D  375  MET D  383  1                                   9    
HELIX   68 AH5 THR D  389  SER D  392  5                                   4    
HELIX   69 AH6 LEU D  393  LYS D  414  1                                  22    
HELIX   70 AH7 ASP D  419  GLY D  439  1                                  21    
HELIX   71 AH8 ASP D  444  VAL D  449  1                                   6    
HELIX   72 AH9 SER D  453  THR D  457  5                                   5    
SHEET    1 AA1 2 ARG A  70  LYS A  72  0                                        
SHEET    2 AA1 2 ILE A  79  TYR A  81 -1  O  THR A  80   N  VAL A  71           
SHEET    1 AA2 4 GLN A 194  ASP A 197  0                                        
SHEET    2 AA2 4 ALA A 227  VAL A 230  1  O  ILE A 228   N  GLN A 194           
SHEET    3 AA2 4 PHE A 353  SER A 354 -1  O  SER A 354   N  ALA A 227           
SHEET    4 AA2 4 ALA A 335  VAL A 336 -1  N  VAL A 336   O  PHE A 353           
SHEET    1 AA3 3 ARG A 242  ILE A 243  0                                        
SHEET    2 AA3 3 LEU A 291  GLN A 294 -1  O  GLN A 294   N  ARG A 242           
SHEET    3 AA3 3 GLU A 301  PHE A 303 -1  O  PHE A 303   N  LEU A 291           
SHEET    1 AA4 2 GLY A 253  ARG A 255  0                                        
SHEET    2 AA4 2 VAL A 261  GLY A 263 -1  O  ARG A 262   N  TYR A 254           
SHEET    1 AA5 2 GLU A 312  PRO A 314  0                                        
SHEET    2 AA5 2 ARG A 329  TYR A 331 -1  O  TRP A 330   N  VAL A 313           
SHEET    1 AA6 3 LEU A 346  PHE A 348  0                                        
SHEET    2 AA6 3 LEU A 340  ILE A 343 -1  N  LEU A 341   O  PHE A 348           
SHEET    3 AA6 3 ALA A 472  ARG A 474 -1  O  ARG A 474   N  LEU A 340           
SHEET    1 AA7 2 TYR A 357  MET A 358  0                                        
SHEET    2 AA7 2 ILE A 417  VAL A 418  1  O  VAL A 418   N  TYR A 357           
SHEET    1 AA8 2 ARG B  70  ASN B  73  0                                        
SHEET    2 AA8 2 SER B  78  TYR B  81 -1  O  THR B  80   N  VAL B  71           
SHEET    1 AA9 4 GLN B 194  ASP B 197  0                                        
SHEET    2 AA9 4 ALA B 227  VAL B 230  1  O  ILE B 228   N  PHE B 196           
SHEET    3 AA9 4 PHE B 353  SER B 354 -1  O  SER B 354   N  ALA B 227           
SHEET    4 AA9 4 ALA B 335  VAL B 336 -1  N  VAL B 336   O  PHE B 353           
SHEET    1 AB1 3 ARG B 242  ILE B 243  0                                        
SHEET    2 AB1 3 LEU B 291  GLN B 294 -1  O  GLN B 294   N  ARG B 242           
SHEET    3 AB1 3 GLU B 301  PHE B 303 -1  O  GLU B 301   N  LEU B 293           
SHEET    1 AB2 2 GLY B 253  ARG B 255  0                                        
SHEET    2 AB2 2 VAL B 261  GLY B 263 -1  O  ARG B 262   N  TYR B 254           
SHEET    1 AB3 2 GLU B 312  PRO B 314  0                                        
SHEET    2 AB3 2 ARG B 329  TYR B 331 -1  O  TRP B 330   N  VAL B 313           
SHEET    1 AB4 3 LEU B 346  PHE B 348  0                                        
SHEET    2 AB4 3 LEU B 340  ILE B 343 -1  N  LEU B 341   O  PHE B 348           
SHEET    3 AB4 3 ALA B 472  ARG B 474 -1  O  ARG B 474   N  LEU B 340           
SHEET    1 AB5 2 ARG C  70  LYS C  72  0                                        
SHEET    2 AB5 2 ILE C  79  TYR C  81 -1  O  THR C  80   N  VAL C  71           
SHEET    1 AB6 4 GLN C 194  ASP C 197  0                                        
SHEET    2 AB6 4 ALA C 227  VAL C 230  1  O  VAL C 230   N  PHE C 196           
SHEET    3 AB6 4 PHE C 353  SER C 354 -1  O  SER C 354   N  ALA C 227           
SHEET    4 AB6 4 ALA C 335  VAL C 336 -1  N  VAL C 336   O  PHE C 353           
SHEET    1 AB7 3 ARG C 242  ILE C 243  0                                        
SHEET    2 AB7 3 LEU C 291  GLN C 294 -1  O  GLN C 294   N  ARG C 242           
SHEET    3 AB7 3 GLU C 301  PHE C 303 -1  O  PHE C 303   N  LEU C 291           
SHEET    1 AB8 2 GLY C 253  ARG C 255  0                                        
SHEET    2 AB8 2 VAL C 261  GLY C 263 -1  O  ARG C 262   N  TYR C 254           
SHEET    1 AB9 2 GLU C 312  PRO C 314  0                                        
SHEET    2 AB9 2 ARG C 329  TYR C 331 -1  O  TRP C 330   N  VAL C 313           
SHEET    1 AC1 3 LEU C 346  PHE C 348  0                                        
SHEET    2 AC1 3 LEU C 340  ILE C 343 -1  N  LEU C 341   O  PHE C 348           
SHEET    3 AC1 3 ALA C 472  ARG C 474 -1  O  ARG C 474   N  LEU C 340           
SHEET    1 AC2 2 TYR C 357  MET C 358  0                                        
SHEET    2 AC2 2 ILE C 417  VAL C 418  1  O  VAL C 418   N  TYR C 357           
SHEET    1 AC3 2 ARG D  70  LYS D  72  0                                        
SHEET    2 AC3 2 ILE D  79  TYR D  81 -1  O  THR D  80   N  VAL D  71           
SHEET    1 AC4 4 GLN D 194  ASP D 197  0                                        
SHEET    2 AC4 4 ALA D 227  VAL D 230  1  O  ILE D 228   N  PHE D 196           
SHEET    3 AC4 4 PHE D 353  SER D 354 -1  O  SER D 354   N  ALA D 227           
SHEET    4 AC4 4 ALA D 335  VAL D 336 -1  N  VAL D 336   O  PHE D 353           
SHEET    1 AC5 3 ARG D 242  ILE D 243  0                                        
SHEET    2 AC5 3 LEU D 291  GLN D 294 -1  O  GLN D 294   N  ARG D 242           
SHEET    3 AC5 3 GLU D 301  PHE D 303 -1  O  GLU D 301   N  LEU D 293           
SHEET    1 AC6 2 GLY D 253  ARG D 255  0                                        
SHEET    2 AC6 2 VAL D 261  GLY D 263 -1  O  ARG D 262   N  TYR D 254           
SHEET    1 AC7 2 GLU D 312  PRO D 314  0                                        
SHEET    2 AC7 2 ARG D 329  TYR D 331 -1  O  TRP D 330   N  VAL D 313           
SHEET    1 AC8 3 LEU D 346  PHE D 348  0                                        
SHEET    2 AC8 3 LEU D 340  ILE D 343 -1  N  LEU D 341   O  PHE D 348           
SHEET    3 AC8 3 ALA D 472  ARG D 474 -1  O  ALA D 472   N  GLU D 342           
LINK         SG  CYS A  94                ZN    ZN A 506     1555   1555  2.36  
LINK         SG  CYS A  99                ZN    ZN A 506     1555   1555  2.32  
LINK         SG  CYS A 184                FE   HEM A 501     1555   1555  2.41  
LINK         SG  CYS B  94                ZN    ZN A 506     1555   1555  2.49  
LINK         SG  CYS B  99                ZN    ZN A 506     1555   1555  2.33  
LINK         SG  CYS B 184                FE   HEM B 501     1555   1555  2.29  
LINK         O   THR B 319                GD    GD B 508     1555   1555  2.69  
LINK         OE1 GLU B 321                GD    GD B 508     1555   1555  2.67  
LINK         SG  CYS C  94                ZN    ZN C 507     1555   1555  2.46  
LINK         SG  CYS C  99                ZN    ZN C 507     1555   1555  2.34  
LINK         SG  CYS C 184                FE   HEM C 501     1555   1555  2.29  
LINK         OD1 ASP C 384                GD    GD C 510     1555   1555  2.72  
LINK         SG  CYS D  94                ZN    ZN C 507     1555   1555  2.27  
LINK         SG  CYS D  99                ZN    ZN C 507     1555   1555  2.47  
LINK         SG  CYS D 184                FE   HEM D 501     1555   1555  2.35  
LINK         O   THR D 319                GD    GD D 507     1555   1555  2.61  
LINK         OE1 GLU D 321                GD    GD D 507     1555   1555  3.07  
LINK         OE2 GLU D 321                GD    GD D 507     1555   1555  2.69  
LINK        GD    GD A 509                 O   HOH A 692     1555   1555  3.34  
LINK        GD    GD A 509                 O   HOH A 696     1555   1555  2.80  
LINK        GD    GD A 509                 O   HOH A 691     1555   1555  2.75  
LINK        GD    GD A 509                 O   HOH A 702     1555   1555  3.42  
LINK         O3  BTB B 504                GD    GD B 508     1555   1555  2.66  
LINK         O4  BTB B 504                GD    GD B 508     1555   1555  2.61  
LINK         N   BTB B 504                GD    GD B 508     1555   1555  2.86  
LINK         O6  BTB B 504                GD    GD B 508     1555   1555  2.68  
LINK         O8  BTB B 504                GD    GD B 508     1555   1555  3.08  
LINK        GD    GD B 508                 O   HOH B 602     1555   1555  2.65  
LINK        GD    GD B 508                 O   HOH C 611     1555   1555  2.54  
LINK        GD    GD C 510                 O   HOH C 710     1555   1555  2.79  
LINK        GD    GD C 510                 O   HOH B 755     1555   1555  3.21  
LINK        GD    GD C 510                 O   HOH B 761     1555   1555  2.75  
LINK        GD    GD C 510                 O   HOH C 690     1555   1555  2.82  
LINK         O3  BTB D 504                GD    GD D 507     1555   1555  2.61  
LINK         O4  BTB D 504                GD    GD D 507     1555   1555  2.92  
LINK         N   BTB D 504                GD    GD D 507     1555   1555  2.77  
LINK         O6  BTB D 504                GD    GD D 507     1555   1555  2.98  
LINK         O8  BTB D 504                GD    GD D 507     1555   1555  2.70  
LINK        GD    GD D 507                 O   HOH D 698     1555   1555  2.71  
LINK        GD    GD D 507                 O   HOH D 702     1555   1555  2.64  
LINK         NE2 GLN A 257                GD    GD C 510     1555   1655  3.02  
CISPEP   1 SER A  470    PRO A  471          0        -5.94                     
CISPEP   2 SER B  470    PRO B  471          0        -0.97                     
CISPEP   3 SER C  470    PRO C  471          0        -0.74                     
CISPEP   4 SER D  470    PRO D  471          0         3.20                     
SITE     1 AC1 16 TRP A 178  PRO A 182  ARG A 183  CYS A 184                    
SITE     2 AC1 16 SER A 226  PHE A 353  SER A 354  GLY A 355                    
SITE     3 AC1 16 TRP A 356  MET A 358  GLU A 361  PHE A 473                    
SITE     4 AC1 16 TYR A 475  H4B A 502  F2J A 503  HOH A 661                    
SITE     1 AC2 11 SER A 102  ARG A 365  ALA A 446  TRP A 447                    
SITE     2 AC2 11 HEM A 501  HOH A 628  TRP B 445  PHE B 460                    
SITE     3 AC2 11 GLN B 462  GLU B 463  HOH B 609                               
SITE     1 AC3  8 PRO A 334  VAL A 336  PHE A 353  SER A 354                    
SITE     2 AC3  8 GLY A 355  TRP A 356  GLU A 361  HEM A 501                    
SITE     1 AC4  3 CYS A 382  ASP A 384  BTB D 506                               
SITE     1 AC5  4 GLU A 377  HOH A 608  HOH A 651  ASP D 384                    
SITE     1 AC6  4 CYS A  94  CYS A  99  CYS B  94  CYS B  99                    
SITE     1 AC7  1 GLU A 167                                                     
SITE     1 AC8  4 GLN A 247  TYR A 357  ASN A 366  HOH A 668                    
SITE     1 AC9  2 HOH A 691  HOH A 696                                          
SITE     1 AD1 17 TRP B 178  PRO B 182  ARG B 183  CYS B 184                    
SITE     2 AD1 17 SER B 226  PHE B 353  SER B 354  TRP B 356                    
SITE     3 AD1 17 GLU B 361  TRP B 447  PHE B 473  TYR B 475                    
SITE     4 AD1 17 H4B B 502  F2J B 503  HOH B 610  HOH B 629                    
SITE     5 AD1 17 HOH B 682                                                     
SITE     1 AD2 13 TRP A 445  PHE A 460  HIS A 461  GLN A 462                    
SITE     2 AD2 13 SER B 102  VAL B 104  ARG B 365  ALA B 446                    
SITE     3 AD2 13 TRP B 447  HEM B 501  HOH B 610  HOH B 616                    
SITE     4 AD2 13 HOH B 674                                                     
SITE     1 AD3  9 GLN B 247  PRO B 334  VAL B 336  PHE B 353                    
SITE     2 AD3  9 SER B 354  GLY B 355  TRP B 356  GLU B 361                    
SITE     3 AD3  9 HEM B 501                                                     
SITE     1 AD4 10 THR B 319  GLU B 321   GD B 508  HOH B 602                    
SITE     2 AD4 10 HOH B 603  SER C 260  VAL C 261  TYR C 373                    
SITE     3 AD4 10 ASN C 374  ASP C 378                                          
SITE     1 AD5  2 ASP B 297  GLU B 298                                          
SITE     1 AD6  2 ASN B 374  ASP B 378                                          
SITE     1 AD7  4 GLN B 247  TYR B 357  ASN B 366  HOH B 686                    
SITE     1 AD8  5 THR B 319  GLU B 321  BTB B 504  HOH B 602                    
SITE     2 AD8  5 HOH C 611                                                     
SITE     1 AD9 15 TRP C 178  ALA C 181  PRO C 182  ARG C 183                    
SITE     2 AD9 15 CYS C 184  SER C 226  PHE C 353  SER C 354                    
SITE     3 AD9 15 TRP C 356  GLU C 361  PHE C 473  TYR C 475                    
SITE     4 AD9 15 H4B C 502  F2J C 503  HOH C 628                               
SITE     1 AE1 13 SER C 102  ARG C 365  ALA C 446  TRP C 447                    
SITE     2 AE1 13 HEM C 501  HOH C 639  HOH C 647  HOH C 669                    
SITE     3 AE1 13 HOH C 681  TRP D 445  PHE D 460  GLN D 462                    
SITE     4 AE1 13 GLU D 463                                                     
SITE     1 AE2  9 GLN C 247  PRO C 334  VAL C 336  PHE C 353                    
SITE     2 AE2  9 SER C 354  GLY C 355  TRP C 356  GLU C 361                    
SITE     3 AE2  9 HEM C 501                                                     
SITE     1 AE3  3 VAL C 381  CYS C 382  ASP C 384                               
SITE     1 AE4  2 ASP B 384  GLU C 377                                          
SITE     1 AE5  1 GLU C 298                                                     
SITE     1 AE6  4 CYS C  94  CYS C  99  CYS D  94  CYS D  99                    
SITE     1 AE7  2 GLU C 167  HOH C 618                                          
SITE     1 AE8  3 GLN C 247  TYR C 357  ASN C 366                               
SITE     1 AE9  5 GLN A 257  HOH B 761  ASP C 384  HOH C 690                    
SITE     2 AE9  5 HOH C 710                                                     
SITE     1 AF1 16 TRP D 178  ALA D 181  ARG D 183  CYS D 184                    
SITE     2 AF1 16 SER D 226  PHE D 353  SER D 354  TRP D 356                    
SITE     3 AF1 16 GLU D 361  PHE D 473  TYR D 475  H4B D 502                    
SITE     4 AF1 16 F2J D 503  HOH D 603  HOH D 606  HOH D 641                    
SITE     1 AF2 11 TRP C 445  PHE C 460  GLU C 463  HOH C 640                    
SITE     2 AF2 11 SER D 102  ARG D 365  ALA D 446  TRP D 447                    
SITE     3 AF2 11 HEM D 501  HOH D 641  HOH D 655                               
SITE     1 AF3  9 GLN D 247  PRO D 334  VAL D 336  PHE D 353                    
SITE     2 AF3  9 GLY D 355  TRP D 356  GLU D 361  HEM D 501                    
SITE     3 AF3  9 HOH D 667                                                     
SITE     1 AF4  9 VAL A 261  TYR A 373  ASN A 374  ASP A 378                    
SITE     2 AF4  9 THR D 319  GLU D 321   GD D 507  HOH D 612                    
SITE     3 AF4  9 HOH D 702                                                     
SITE     1 AF5  3 GLU B 167  GLU D 298  HOH D 642                               
SITE     1 AF6  4 BTB A 504  GLU D 377  ASP D 378  HOH D 620                    
SITE     1 AF7  5 THR D 319  GLU D 321  BTB D 504  HOH D 698                    
SITE     2 AF7  5 HOH D 702                                                     
SITE     1 AF8  3 GLN D 247  TYR D 357  ASN D 366                               
CRYST1   59.789  152.579  108.690  90.00  90.81  90.00 P 1 21 1      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      0.016726  0.000000  0.000236        0.00000                         
SCALE2      0.000000  0.006554  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009201        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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