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Database: PDB
Entry: 1M9M
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Original site: 1M9M 
HEADER    OXIDOREDUCTASE                          29-JUL-02   1M9M              
TITLE     HUMAN ENDOTHELIAL NITRIC OXIDE SYNTHASE WITH 6-                       
TITLE    2 NITROINDAZOLE BOUND                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDOTHELIAL NITRIC-OXIDE SYNTHASE;                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: OXYGENASE DOMAIN;                                          
COMPND   5 SYNONYM: EC-NOS, NOS, TYPE III, NOSIII, ENDOTHELIAL NOS,             
COMPND   6 ENOS, CONSTITUTIVE NOS, CNOS;                                        
COMPND   7 EC: 1.14.13.39;                                                      
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    OXIDOREDUCTASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.J.ROSENFELD,E.D.GARCIN,K.PANDA,G.ANDERSSON,A.ABERG,                 
AUTHOR   2 A.V.WALLACE,D.J.STUEHR,J.A.TAINER,E.D.GETZOFF                        
REVDAT   3   24-FEB-09 1M9M    1       VERSN                                    
REVDAT   2   11-DEC-02 1M9M    1       JRNL                                     
REVDAT   1   07-AUG-02 1M9M    0                                                
JRNL        AUTH   R.J.ROSENFELD,E.D.GARCIN,K.PANDA,G.ANDERSSON,                
JRNL        AUTH 2 A.ABERG,A.V.WALLACE,G.M.MORRIS,A.J.OLSON,                    
JRNL        AUTH 3 D.J.STUEHR,J.A.TAINER,E.D.GETZOFF                            
JRNL        TITL   CONFORMATIONAL CHANGES IN NITRIC OXIDE SYNTHASES             
JRNL        TITL 2 INDUCED BY CHLORZOXAZONE AND NITROINDAZOLES:                 
JRNL        TITL 3 CRYSTALLOGRAPHIC AND COMPUTATIONAL ANALYSES OF               
JRNL        TITL 4 INHIBITOR POTENCY                                            
JRNL        REF    BIOCHEMISTRY                  V.  41 13915 2002              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   12437348                                                     
JRNL        DOI    10.1021/BI026313J                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   B.R.CRANE,A.S.ARVAI,D.K.GHOSH,C.WU,E.D.GETZOFF,              
REMARK   1  AUTH 2 D.J.STUEHR,J.A.TAINER                                        
REMARK   1  TITL   STRUCTURE OF NITRIC OXIDE SYNTHASE OXYGENASE DIMER           
REMARK   1  TITL 2 WITH PTERIN AND SUBSTRATE                                    
REMARK   1  REF    SCIENCE                       V. 279  2121 1998              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   1  DOI    10.1126/SCIENCE.279.5359.2121                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.96 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.96                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.03                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 69278                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3517                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.96                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.08                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 9941                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2720                       
REMARK   3   BIN FREE R VALUE                    : 0.2930                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 516                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.013                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6354                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 112                                     
REMARK   3   SOLVENT ATOMS            : 449                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 7.62000                                              
REMARK   3    B22 (A**2) : 1.69000                                              
REMARK   3    B33 (A**2) : -9.31000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.27                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.22                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.16                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.440 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.170 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.150 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.220 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.31                                                 
REMARK   3   BSOL        : 23.18                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  3  : PARAM19X.HEME                                  
REMARK   3  PARAMETER FILE  4  : 6NITRO_FLEX.PAR                                
REMARK   3  PARAMETER FILE  5  : MISC.PAR                                       
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  3   : TOPH19X.HEME                                   
REMARK   3  TOPOLOGY FILE  4   : 6NITRO_FLEX.TOP                                
REMARK   3  TOPOLOGY FILE  5   : MISC.TOP                                       
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1M9M COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-AUG-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB016768.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JAN-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
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                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69487                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.960                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.04600                            
REMARK 200  R SYM                      (I) : 0.04600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.01                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.32100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NACL, MPD, PEG, PH 5.5, VAPOR            
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       34.87850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       77.77550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.39100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       77.77550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.87850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.39100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10270 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 31940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -117.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO A   106                                                      
REMARK 465     ARG A   107                                                      
REMARK 465     LYS A   108                                                      
REMARK 465     LEU A   109                                                      
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 A   119                                                      
REMARK 465     LYS A   481                                                      
REMARK 465     PRO B   106                                                      
REMARK 465     ARG B   107                                                      
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 B   119                                                      
REMARK 465     LYS B   481                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  67    CG   CD   CE   NZ                                   
REMARK 470     ARG A  97    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 121    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 154    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  67    CG   CD   CE   NZ                                   
REMARK 470     ARG B  97    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 121    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 388    CG   CD   NE   CZ   NH1  NH2                        
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      -77.46    -55.89                                   
REMARK 500    ARG A 140       26.77   -141.64                                   
REMARK 500    ASN A 283       26.86   -146.35                                   
REMARK 500    ALA A 351       71.15   -157.90                                   
REMARK 500    ARG A 372     -135.78   -119.21                                   
REMARK 500    GLN B  89      -87.59    -61.29                                   
REMARK 500    ARG B 238      140.42    178.97                                   
REMARK 500    ASN B 283       19.30   -151.22                                   
REMARK 500    ALA B 351       72.09   -156.43                                   
REMARK 500    ARG B 372     -136.73   -120.23                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C SSEQI                                                      
REMARK 615     6NI A  906                                                       
REMARK 615     6NI B  907                                                       
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 903  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  94   SG                                                     
REMARK 620 2 CYS A  99   SG  108.7                                              
REMARK 620 3 CYS B  99   SG  107.7 104.9                                        
REMARK 620 4 CYS A  94   SG  119.4 107.6 107.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A1000  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 357   OH                                                     
REMARK 620 2 HOH A1147   O   132.4                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 903                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1000                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 901                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6NI A 906                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 901                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6NI B 907                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA B 600                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA B 601                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 602                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 603                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 604                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 605                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1M8D   RELATED DB: PDB                                   
REMARK 900 INOS WITH CHLORZOXAZONE BOUND                                        
REMARK 900 RELATED ID: 1M8E   RELATED DB: PDB                                   
REMARK 900 INOS WITH 7-NITROINDAZOLE BOUND                                      
REMARK 900 RELATED ID: 1M8H   RELATED DB: PDB                                   
REMARK 900 INOS WITH 6-NITROINDAZOLE BOUND                                      
REMARK 900 RELATED ID: 1M8I   RELATED DB: PDB                                   
REMARK 900 INOS WITH 5-NITROINDAZOLE BOUND                                      
REMARK 900 RELATED ID: 1M9J   RELATED DB: PDB                                   
REMARK 900 HUMAN ENOS WITH CHLORZOXAZONE BOUND                                  
REMARK 900 RELATED ID: 1M9K   RELATED DB: PDB                                   
REMARK 900 HUMAN ENOS WITH 7-NITROINDAZOLE BOUND                                
REMARK 900 RELATED ID: 1M9Q   RELATED DB: PDB                                   
REMARK 900 HUMAN ENOS WITH 5-NITROINDAZOLE BOUND                                
REMARK 900 RELATED ID: 1M9R   RELATED DB: PDB                                   
REMARK 900 HUMAN ENOS WITH 3-BROMO-7-NITROINDAZOLE BOUND                        
REMARK 900 RELATED ID: 1M9T   RELATED DB: PDB                                   
REMARK 900 INOS WITH WITH 3-BROMO-7-NITROINDAZOLE BOUND                         
REMARK 900 RELATED ID: 1NOD   RELATED DB: PDB                                   
REMARK 900 INOS WITH SUBSTRATE BOUND                                            
REMARK 900 RELATED ID: 3NOD   RELATED DB: PDB                                   
REMARK 900 HUMAN ENOS WITH SUBSTRATE BOUND                                      
DBREF  1M9M A   67   481  UNP    P29474   NOS3_HUMAN      66    480             
DBREF  1M9M B   67   481  UNP    P29474   NOS3_HUMAN      66    480             
SEQRES   1 A  415  LYS PHE PRO ARG VAL LYS ASN TRP GLU VAL GLY SER ILE          
SEQRES   2 A  415  THR TYR ASP THR LEU SER ALA GLN ALA GLN GLN ASP GLY          
SEQRES   3 A  415  PRO CYS THR PRO ARG ARG CYS LEU GLY SER LEU VAL PHE          
SEQRES   4 A  415  PRO ARG LYS LEU GLN GLY ARG PRO SER PRO GLY PRO PRO          
SEQRES   5 A  415  ALA PRO GLU GLN LEU LEU SER GLN ALA ARG ASP PHE ILE          
SEQRES   6 A  415  ASN GLN TYR TYR SER SER ILE LYS ARG SER GLY SER GLN          
SEQRES   7 A  415  ALA HIS GLU GLN ARG LEU GLN GLU VAL GLU ALA GLU VAL          
SEQRES   8 A  415  ALA ALA THR GLY THR TYR GLN LEU ARG GLU SER GLU LEU          
SEQRES   9 A  415  VAL PHE GLY ALA LYS GLN ALA TRP ARG ASN ALA PRO ARG          
SEQRES  10 A  415  CYS VAL GLY ARG ILE GLN TRP GLY LYS LEU GLN VAL PHE          
SEQRES  11 A  415  ASP ALA ARG ASP CYS ARG SER ALA GLN GLU MET PHE THR          
SEQRES  12 A  415  TYR ILE CYS ASN HIS ILE LYS TYR ALA THR ASN ARG GLY          
SEQRES  13 A  415  ASN LEU ARG SER ALA ILE THR VAL PHE PRO GLN ARG CYS          
SEQRES  14 A  415  PRO GLY ARG GLY ASP PHE ARG ILE TRP ASN SER GLN LEU          
SEQRES  15 A  415  VAL ARG TYR ALA GLY TYR ARG GLN GLN ASP GLY SER VAL          
SEQRES  16 A  415  ARG GLY ASP PRO ALA ASN VAL GLU ILE THR GLU LEU CYS          
SEQRES  17 A  415  ILE GLN HIS GLY TRP THR PRO GLY ASN GLY ARG PHE ASP          
SEQRES  18 A  415  VAL LEU PRO LEU LEU LEU GLN ALA PRO ASP GLU PRO PRO          
SEQRES  19 A  415  GLU LEU PHE LEU LEU PRO PRO GLU LEU VAL LEU GLU VAL          
SEQRES  20 A  415  PRO LEU GLU HIS PRO THR LEU GLU TRP PHE ALA ALA LEU          
SEQRES  21 A  415  GLY LEU ARG TRP TYR ALA LEU PRO ALA VAL SER ASN MET          
SEQRES  22 A  415  LEU LEU GLU ILE GLY GLY LEU GLU PHE PRO ALA ALA PRO          
SEQRES  23 A  415  PHE SER GLY TRP TYR MET SER THR GLU ILE GLY THR ARG          
SEQRES  24 A  415  ASN LEU CYS ASP PRO HIS ARG TYR ASN ILE LEU GLU ASP          
SEQRES  25 A  415  VAL ALA VAL CYS MET ASP LEU ASP THR ARG THR THR SER          
SEQRES  26 A  415  SER LEU TRP LYS ASP LYS ALA ALA VAL GLU ILE ASN VAL          
SEQRES  27 A  415  ALA VAL LEU HIS SER TYR GLN LEU ALA LYS VAL THR ILE          
SEQRES  28 A  415  VAL ASP HIS HIS ALA ALA THR ALA SER PHE MET LYS HIS          
SEQRES  29 A  415  LEU GLU ASN GLU GLN LYS ALA ARG GLY GLY CYS PRO ALA          
SEQRES  30 A  415  ASP TRP ALA TRP ILE VAL PRO PRO ILE SER GLY SER LEU          
SEQRES  31 A  415  THR PRO VAL PHE HIS GLN GLU MET VAL ASN TYR PHE LEU          
SEQRES  32 A  415  SER PRO ALA PHE ARG TYR GLN PRO ASP PRO TRP LYS              
SEQRES   1 B  415  LYS PHE PRO ARG VAL LYS ASN TRP GLU VAL GLY SER ILE          
SEQRES   2 B  415  THR TYR ASP THR LEU SER ALA GLN ALA GLN GLN ASP GLY          
SEQRES   3 B  415  PRO CYS THR PRO ARG ARG CYS LEU GLY SER LEU VAL PHE          
SEQRES   4 B  415  PRO ARG LYS LEU GLN GLY ARG PRO SER PRO GLY PRO PRO          
SEQRES   5 B  415  ALA PRO GLU GLN LEU LEU SER GLN ALA ARG ASP PHE ILE          
SEQRES   6 B  415  ASN GLN TYR TYR SER SER ILE LYS ARG SER GLY SER GLN          
SEQRES   7 B  415  ALA HIS GLU GLN ARG LEU GLN GLU VAL GLU ALA GLU VAL          
SEQRES   8 B  415  ALA ALA THR GLY THR TYR GLN LEU ARG GLU SER GLU LEU          
SEQRES   9 B  415  VAL PHE GLY ALA LYS GLN ALA TRP ARG ASN ALA PRO ARG          
SEQRES  10 B  415  CYS VAL GLY ARG ILE GLN TRP GLY LYS LEU GLN VAL PHE          
SEQRES  11 B  415  ASP ALA ARG ASP CYS ARG SER ALA GLN GLU MET PHE THR          
SEQRES  12 B  415  TYR ILE CYS ASN HIS ILE LYS TYR ALA THR ASN ARG GLY          
SEQRES  13 B  415  ASN LEU ARG SER ALA ILE THR VAL PHE PRO GLN ARG CYS          
SEQRES  14 B  415  PRO GLY ARG GLY ASP PHE ARG ILE TRP ASN SER GLN LEU          
SEQRES  15 B  415  VAL ARG TYR ALA GLY TYR ARG GLN GLN ASP GLY SER VAL          
SEQRES  16 B  415  ARG GLY ASP PRO ALA ASN VAL GLU ILE THR GLU LEU CYS          
SEQRES  17 B  415  ILE GLN HIS GLY TRP THR PRO GLY ASN GLY ARG PHE ASP          
SEQRES  18 B  415  VAL LEU PRO LEU LEU LEU GLN ALA PRO ASP GLU PRO PRO          
SEQRES  19 B  415  GLU LEU PHE LEU LEU PRO PRO GLU LEU VAL LEU GLU VAL          
SEQRES  20 B  415  PRO LEU GLU HIS PRO THR LEU GLU TRP PHE ALA ALA LEU          
SEQRES  21 B  415  GLY LEU ARG TRP TYR ALA LEU PRO ALA VAL SER ASN MET          
SEQRES  22 B  415  LEU LEU GLU ILE GLY GLY LEU GLU PHE PRO ALA ALA PRO          
SEQRES  23 B  415  PHE SER GLY TRP TYR MET SER THR GLU ILE GLY THR ARG          
SEQRES  24 B  415  ASN LEU CYS ASP PRO HIS ARG TYR ASN ILE LEU GLU ASP          
SEQRES  25 B  415  VAL ALA VAL CYS MET ASP LEU ASP THR ARG THR THR SER          
SEQRES  26 B  415  SER LEU TRP LYS ASP LYS ALA ALA VAL GLU ILE ASN VAL          
SEQRES  27 B  415  ALA VAL LEU HIS SER TYR GLN LEU ALA LYS VAL THR ILE          
SEQRES  28 B  415  VAL ASP HIS HIS ALA ALA THR ALA SER PHE MET LYS HIS          
SEQRES  29 B  415  LEU GLU ASN GLU GLN LYS ALA ARG GLY GLY CYS PRO ALA          
SEQRES  30 B  415  ASP TRP ALA TRP ILE VAL PRO PRO ILE SER GLY SER LEU          
SEQRES  31 B  415  THR PRO VAL PHE HIS GLN GLU MET VAL ASN TYR PHE LEU          
SEQRES  32 B  415  SER PRO ALA PHE ARG TYR GLN PRO ASP PRO TRP LYS              
HET     ZN  A 903       1                                                       
HET     NA  A1000       1                                                       
HET    HEM  A 901      43                                                       
HET    6NI  A 906      12                                                       
HET    HEM  B 901      43                                                       
HET    6NI  B 907      12                                                       
HET    IPA  B 600       4                                                       
HET    IPA  B 601       4                                                       
HET    IPA  A 602       4                                                       
HET    MPD  A 603       8                                                       
HET    MPD  A 604       8                                                       
HET    MPD  A 605       8                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      NA SODIUM ION                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     6NI 6-NITROINDAZOLE                                                  
HETNAM     IPA ISOPROPYL ALCOHOL                                                
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
HETSYN     HEM HEME                                                             
HETSYN     IPA 2-PROPANOL                                                       
FORMUL   3   ZN    ZN 2+                                                        
FORMUL   4   NA    NA 1+                                                        
FORMUL   5  HEM    2(C34 H32 FE N4 O4)                                          
FORMUL   6  6NI    2(C7 H5 N3 O2)                                               
FORMUL   9  IPA    3(C3 H8 O)                                                   
FORMUL  12  MPD    3(C6 H14 O2)                                                 
FORMUL  15  HOH   *413(H2 O)                                                    
HELIX    1   1 LEU A   84  ALA A   88  5                                   5    
HELIX    2   2 PRO A  120  ILE A  138  1                                  19    
HELIX    3   3 SER A  143  GLY A  161  1                                  19    
HELIX    4   4 ARG A  166  ALA A  181  1                                  16    
HELIX    5   5 GLY A  186  TRP A  190  5                                   5    
HELIX    6   6 SER A  203  ASN A  220  1                                  18    
HELIX    7   7 ARG A  221  ASN A  223  5                                   3    
HELIX    8   8 ASN A  267  HIS A  277  1                                  11    
HELIX    9   9 PRO A  306  VAL A  310  5                                   5    
HELIX   10  10 LEU A  320  GLY A  327  5                                   8    
HELIX   11  11 SER A  359  THR A  364  1                                   6    
HELIX   12  12 THR A  364  ASP A  369  1                                   6    
HELIX   13  13 ILE A  375  MET A  383  1                                   9    
HELIX   14  14 THR A  389  SER A  392  5                                   4    
HELIX   15  15 LEU A  393  LYS A  414  1                                  22    
HELIX   16  16 ASP A  419  GLY A  439  1                                  21    
HELIX   17  17 ASP A  444  VAL A  449  1                                   6    
HELIX   18  18 SER A  453  GLN A  462  5                                  10    
HELIX   19  19 LEU B   84  ALA B   88  5                                   5    
HELIX   20  20 PRO B  120  ILE B  138  1                                  19    
HELIX   21  21 SER B  143  GLY B  161  1                                  19    
HELIX   22  22 ARG B  166  ALA B  181  1                                  16    
HELIX   23  23 GLY B  186  LEU B  193  5                                   8    
HELIX   24  24 SER B  203  ASN B  220  1                                  18    
HELIX   25  25 ARG B  221  ASN B  223  5                                   3    
HELIX   26  26 ASN B  267  HIS B  277  1                                  11    
HELIX   27  27 PRO B  306  VAL B  310  5                                   5    
HELIX   28  28 TRP B  322  GLY B  327  5                                   6    
HELIX   29  29 SER B  359  THR B  364  1                                   6    
HELIX   30  30 THR B  364  ASP B  369  1                                   6    
HELIX   31  31 ILE B  375  MET B  383  1                                   9    
HELIX   32  32 THR B  389  SER B  392  5                                   4    
HELIX   33  33 LEU B  393  LYS B  414  1                                  22    
HELIX   34  34 ASP B  419  GLY B  439  1                                  21    
HELIX   35  35 ASP B  444  VAL B  449  1                                   6    
HELIX   36  36 SER B  453  GLN B  462  5                                  10    
SHEET    1   A 2 ARG A  70  LYS A  72  0                                        
SHEET    2   A 2 ILE A  79  TYR A  81 -1  O  THR A  80   N  VAL A  71           
SHEET    1   B 4 GLN A 194  ASP A 197  0                                        
SHEET    2   B 4 ALA A 227  VAL A 230  1  O  ILE A 228   N  PHE A 196           
SHEET    3   B 4 PHE A 353  SER A 354 -1  O  SER A 354   N  ALA A 227           
SHEET    4   B 4 ALA A 335  VAL A 336 -1  N  VAL A 336   O  PHE A 353           
SHEET    1   C 3 ARG A 242  ILE A 243  0                                        
SHEET    2   C 3 LEU A 291  GLN A 294 -1  O  GLN A 294   N  ARG A 242           
SHEET    3   C 3 GLU A 301  PHE A 303 -1  O  PHE A 303   N  LEU A 291           
SHEET    1   D 2 GLY A 253  ARG A 255  0                                        
SHEET    2   D 2 VAL A 261  GLY A 263 -1  O  ARG A 262   N  TYR A 254           
SHEET    1   E 2 GLU A 312  PRO A 314  0                                        
SHEET    2   E 2 ARG A 329  TYR A 331 -1  O  TRP A 330   N  VAL A 313           
SHEET    1   F 3 LEU A 346  PHE A 348  0                                        
SHEET    2   F 3 LEU A 340  ILE A 343 -1  N  LEU A 341   O  PHE A 348           
SHEET    3   F 3 ALA A 472  ARG A 474 -1  O  ARG A 474   N  LEU A 340           
SHEET    1   G 2 TYR A 357  MET A 358  0                                        
SHEET    2   G 2 ILE A 417  VAL A 418  1  O  VAL A 418   N  TYR A 357           
SHEET    1   H 2 ARG B  70  LYS B  72  0                                        
SHEET    2   H 2 ILE B  79  TYR B  81 -1  O  THR B  80   N  VAL B  71           
SHEET    1   I 4 GLN B 194  ASP B 197  0                                        
SHEET    2   I 4 ALA B 227  VAL B 230  1  O  ILE B 228   N  PHE B 196           
SHEET    3   I 4 PHE B 353  SER B 354 -1  O  SER B 354   N  ALA B 227           
SHEET    4   I 4 ALA B 335  VAL B 336 -1  N  VAL B 336   O  PHE B 353           
SHEET    1   J 3 ARG B 242  ILE B 243  0                                        
SHEET    2   J 3 LEU B 291  GLN B 294 -1  O  GLN B 294   N  ARG B 242           
SHEET    3   J 3 GLU B 301  PHE B 303 -1  O  PHE B 303   N  LEU B 291           
SHEET    1   K 2 GLY B 253  ARG B 255  0                                        
SHEET    2   K 2 VAL B 261  GLY B 263 -1  O  ARG B 262   N  TYR B 254           
SHEET    1   L 2 GLU B 312  PRO B 314  0                                        
SHEET    2   L 2 ARG B 329  TYR B 331 -1  O  TRP B 330   N  VAL B 313           
SHEET    1   M 3 LEU B 346  PHE B 348  0                                        
SHEET    2   M 3 LEU B 340  ILE B 343 -1  N  LEU B 341   O  PHE B 348           
SHEET    3   M 3 ALA B 472  ARG B 474 -1  O  ARG B 474   N  LEU B 340           
SHEET    1   N 2 TYR B 357  MET B 358  0                                        
SHEET    2   N 2 ILE B 417  VAL B 418  1  O  VAL B 418   N  TYR B 357           
LINK        FE   HEM A 901                 SG  CYS A 184     1555   1555  2.33  
LINK        ZN    ZN A 903                 SG  CYS B  94     1555   1555  2.27  
LINK        ZN    ZN A 903                 SG  CYS A  99     1555   1555  2.28  
LINK        ZN    ZN A 903                 SG  CYS B  99     1555   1555  2.33  
LINK        ZN    ZN A 903                 SG  CYS A  94     1555   1555  2.29  
LINK        FE   HEM B 901                 SG  CYS B 184     1555   1555  2.38  
LINK         OH  TYR A 357                NA    NA A1000     1555   1555  2.87  
LINK        NA    NA A1000                 O   HOH A1147     1555   1555  2.82  
CISPEP   1 SER A  470    PRO A  471          0         0.06                     
CISPEP   2 SER B  470    PRO B  471          0         0.00                     
SITE     1 AC1  4 CYS A  94  CYS A  99  CYS B  94  CYS B  99                    
SITE     1 AC2  4 GLN A 247  TYR A 357  ASN A 366  HOH A1147                    
SITE     1 AC3 12 TRP A 178  ARG A 183  CYS A 184  SER A 226                    
SITE     2 AC3 12 PHE A 353  SER A 354  TRP A 356  GLU A 361                    
SITE     3 AC3 12 TRP A 447  PHE A 473  TYR A 475  6NI A 906                    
SITE     1 AC4  7 GLY A 355  TRP A 356  TYR A 357  MET A 358                    
SITE     2 AC4  7 GLU A 361  HEM A 901  HOH A1202                               
SITE     1 AC5 10 TRP B 178  CYS B 184  PHE B 353  SER B 354                    
SITE     2 AC5 10 TRP B 356  GLU B 361  TRP B 447  PHE B 473                    
SITE     3 AC5 10 TYR B 475  6NI B 907                                          
SITE     1 AC6  7 PRO B 334  PHE B 353  TRP B 356  TYR B 357                    
SITE     2 AC6  7 MET B 358  GLU B 361  HEM B 901                               
SITE     1 AC7  4 TRP B 356  VAL B 418  SER B 426  HOH B1092                    
SITE     1 AC8  4 GLY A 101  SER A 102  HOH A1199  HOH B1091                    
SITE     1 AC9  8 TRP A 279  THR A 280  PRO A 281  GLY A 282                    
SITE     2 AC9  8 HOH A1034  GLY B 142  HIS B 146  GLU B 147                    
SITE     1 BC1 11 TRP A 445  PHE A 460  HIS A 461  GLN A 462                    
SITE     2 BC1 11 HOH A1197  VAL B 104  ALA B 446  TRP B 447                    
SITE     3 BC1 11 HOH B1086  HOH B1089  HOH B1090                               
SITE     1 BC2  3 TRP A 356  VAL A 418  SER A 426                               
SITE     1 BC3  8 VAL A 104  ALA A 446  TRP A 447  HOH A1198                    
SITE     2 BC3  8 TRP B  74  PHE B 460  HIS B 461  HOH B1045                    
CRYST1   69.757   90.782  155.551  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014335  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011015  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006429        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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