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Database: PDB
Entry: 4K5E
LinkDB: 4K5E
Original site: 4K5E 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 14-APR-13   4K5E              
TITLE     STRUCTURE OF NEURONAL NITRIC OXIDE SYNTHASE HEME DOMAIN IN COMPLEX    
TITLE    2 WITH (R)-1,2-BIS((2-AMINO-4-METHYLPYRIDIN-6-YL)-METHOXY)-PROPAN-3-   
TITLE    3 AMINE                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NITRIC OXIDE SYNTHASE, BRAIN;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: HEME DOMAIN (UNP RESIDUES 297-718);                        
COMPND   5 SYNONYM: BNOS, CONSTITUTIVE NOS, NC-NOS, NOS TYPE I, NEURONAL NOS, N-
COMPND   6 NOS, NNOS, PEPTIDYL-CYSTEINE S-NITROSYLASE NOS1;                     
COMPND   7 EC: 1.14.13.39;                                                      
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: NOS1, BNOS;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PCWORI                                    
KEYWDS    NITRIC OXIDE SYNTHASE, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR        
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.LI,T.L.POULOS                                                       
REVDAT   3   15-NOV-17 4K5E    1       REMARK                                   
REVDAT   2   02-OCT-13 4K5E    1       JRNL                                     
REVDAT   1   18-SEP-13 4K5E    0                                                
JRNL        AUTH   Q.JING,H.LI,G.CHREIFI,L.J.ROMAN,P.MARTASEK,T.L.POULOS,       
JRNL        AUTH 2 R.B.SILVERMAN                                                
JRNL        TITL   CHIRAL LINKERS TO IMPROVE SELECTIVITY OF DOUBLE-HEADED       
JRNL        TITL 2 NEURONAL NITRIC OXIDE SYNTHASE INHIBITORS.                   
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  23  5674 2013              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   23993333                                                     
JRNL        DOI    10.1016/J.BMCL.2013.08.034                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.89 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.89                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.24                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 71966                          
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 + TEST SET) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.212                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3761                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.89                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.94                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4936                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.83                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3030                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 258                          
REMARK   3   BIN FREE R VALUE                    : 0.3310                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6646                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 177                                     
REMARK   3   SOLVENT ATOMS            : 462                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.16                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.14000                                              
REMARK   3    B22 (A**2) : 0.06000                                              
REMARK   3    B33 (A**2) : -0.20000                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.144         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.130         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.097         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.372         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.952                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7052 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9604 ; 1.417 ; 1.991       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   825 ; 5.798 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   331 ;33.251 ;23.897       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1172 ;14.279 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    41 ;17.005 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   997 ; 0.102 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5417 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4099 ; 0.755 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6653 ; 1.364 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2953 ; 2.301 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2945 ; 3.657 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   299        A   716                          
REMARK   3    RESIDUE RANGE :   A   801        A   803                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.4340   4.9540  22.5930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0508 T22:   0.1178                                     
REMARK   3      T33:   0.1267 T12:  -0.0161                                     
REMARK   3      T13:   0.0151 T23:  -0.0217                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4180 L22:   0.7352                                     
REMARK   3      L33:   2.9505 L12:  -0.0535                                     
REMARK   3      L13:  -0.2499 L23:  -0.3081                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0479 S12:   0.0953 S13:   0.0059                       
REMARK   3      S21:  -0.0225 S22:  -0.0068 S23:   0.0487                       
REMARK   3      S31:  -0.0236 S32:  -0.2282 S33:   0.0547                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   299        B   718                          
REMARK   3    RESIDUE RANGE :   B   801        B   803                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.9770   4.8930  60.2820              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0134 T22:   0.0366                                     
REMARK   3      T33:   0.1089 T12:  -0.0012                                     
REMARK   3      T13:   0.0194 T23:   0.0095                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7041 L22:   0.7890                                     
REMARK   3      L33:   1.5784 L12:  -0.1515                                     
REMARK   3      L13:  -0.0791 L23:   0.2801                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0242 S12:  -0.0233 S13:   0.0559                       
REMARK   3      S21:  -0.0646 S22:  -0.0145 S23:  -0.0126                       
REMARK   3      S31:   0.0069 S32:   0.0671 S33:   0.0387                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: U VALUES      : WITH TLS ADDED            
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS                   
REMARK   4                                                                      
REMARK   4 4K5E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-APR-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000078912.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-DEC-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : 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) : 1.000                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : RH COATED FLAT MIRROR, TOROIDAL    
REMARK 200                                   FOCUSING MIRROR                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 75781                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.892                              
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     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.05400                            
REMARK 200  R SYM                      (I) : 0.05400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 29.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.89                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.93                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.58500                            
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: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1OM4                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-22% PEG3350, 0.1 M MES, 0.14-0.20 M   
REMARK 280  AMMONIUM ACETATE, 10% ETHYLENE GLYCOL, 5 MM GSH, 30 UM SDS, PH      
REMARK 280  5.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       25.99800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       82.19550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.33300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       82.19550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.99800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.33300            
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: 9940 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -130.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     CYS A   297                                                      
REMARK 465     PRO A   298                                                      
REMARK 465     SER A   339                                                      
REMARK 465     GLN A   340                                                      
REMARK 465     HIS A   341                                                      
REMARK 465     THR A   342                                                      
REMARK 465     ARG A   343                                                      
REMARK 465     LYS A   344                                                      
REMARK 465     PRO A   345                                                      
REMARK 465     GLU A   346                                                      
REMARK 465     ASP A   347                                                      
REMARK 465     VAL A   348                                                      
REMARK 465     ARG A   349                                                      
REMARK 465     LYS A   717                                                      
REMARK 465     GLY A   718                                                      
REMARK 465     CYS B   297                                                      
REMARK 465     PRO B   298                                                      
REMARK 465     SER B   339                                                      
REMARK 465     GLN B   340                                                      
REMARK 465     HIS B   341                                                      
REMARK 465     THR B   342                                                      
REMARK 465     ARG B   343                                                      
REMARK 465     LYS B   344                                                      
REMARK 465     PRO B   345                                                      
REMARK 465     GLU B   346                                                      
REMARK 465     ASP B   347                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 309       -1.48     67.18                                   
REMARK 500    SER A 392       -2.24     69.46                                   
REMARK 500    THR A 466      -89.96   -107.90                                   
REMARK 500    CYS A 582       54.01   -153.27                                   
REMARK 500    ARG A 603     -135.50   -109.19                                   
REMARK 500    THR B 321      -56.91   -121.41                                   
REMARK 500    SER B 392       -1.89     71.68                                   
REMARK 500    THR B 466      -86.27   -110.69                                   
REMARK 500    CYS B 582       58.56   -150.15                                   
REMARK 500    VAL B 595      -61.84    -93.68                                   
REMARK 500    ARG B 603     -136.26   -120.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 805  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 331   SG                                                     
REMARK 620 2 CYS A 326   SG  115.0                                              
REMARK 620 3 CYS B 331   SG   99.4 106.3                                        
REMARK 620 4 CYS B 326   SG  103.0 120.0 111.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 801  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 415   SG                                                     
REMARK 620 2 HEM A 801   NA   94.4                                              
REMARK 620 3 HEM A 801   NB   91.6  90.4                                        
REMARK 620 4 HEM A 801   NC   94.1 171.5  88.8                                  
REMARK 620 5 HEM A 801   ND   96.6  89.3 171.8  90.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 801  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 415   SG                                                     
REMARK 620 2 HEM B 801   NA   95.5                                              
REMARK 620 3 HEM B 801   NB   94.2  85.4                                        
REMARK 620 4 HEM B 801   NC   93.0 171.4  92.6                                  
REMARK 620 5 HEM B 801   ND   95.4  93.2 170.5  87.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1Q7 A 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 805                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B B 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1Q7 B 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 804                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4K5D   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4K5F   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4K5G   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4K5H   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4K5I   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4K5J   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4K5K   RELATED DB: PDB                                   
DBREF  4K5E A  297   718  UNP    P29476   NOS1_RAT       297    718             
DBREF  4K5E B  297   718  UNP    P29476   NOS1_RAT       297    718             
SEQADV 4K5E CYS A  598  UNP  P29476    TYR   598 CLONING ARTIFACT               
SEQADV 4K5E CYS B  598  UNP  P29476    TYR   598 CLONING ARTIFACT               
SEQRES   1 A  422  CYS PRO ARG PHE LEU LYS VAL LYS ASN TRP GLU THR ASP          
SEQRES   2 A  422  VAL VAL LEU THR ASP THR LEU HIS LEU LYS SER THR LEU          
SEQRES   3 A  422  GLU THR GLY CYS THR GLU HIS ILE CYS MET GLY SER ILE          
SEQRES   4 A  422  MET LEU PRO SER GLN HIS THR ARG LYS PRO GLU ASP VAL          
SEQRES   5 A  422  ARG THR LYS ASP GLN LEU PHE PRO LEU ALA LYS GLU PHE          
SEQRES   6 A  422  LEU ASP GLN TYR TYR SER SER ILE LYS ARG PHE GLY SER          
SEQRES   7 A  422  LYS ALA HIS MET ASP ARG LEU GLU GLU VAL ASN LYS GLU          
SEQRES   8 A  422  ILE GLU SER THR SER THR TYR GLN LEU LYS ASP THR GLU          
SEQRES   9 A  422  LEU ILE TYR GLY ALA LYS HIS ALA TRP ARG ASN ALA SER          
SEQRES  10 A  422  ARG CYS VAL GLY ARG ILE GLN TRP SER LYS LEU GLN VAL          
SEQRES  11 A  422  PHE ASP ALA ARG ASP CYS THR THR ALA HIS GLY MET PHE          
SEQRES  12 A  422  ASN TYR ILE CYS ASN HIS VAL LYS TYR ALA THR ASN LYS          
SEQRES  13 A  422  GLY ASN LEU ARG SER ALA ILE THR ILE PHE PRO GLN ARG          
SEQRES  14 A  422  THR ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN SER GLN          
SEQRES  15 A  422  LEU ILE ARG TYR ALA GLY TYR LYS GLN PRO ASP GLY SER          
SEQRES  16 A  422  THR LEU GLY ASP PRO ALA ASN VAL GLN PHE THR GLU ILE          
SEQRES  17 A  422  CYS ILE GLN GLN GLY TRP LYS ALA PRO ARG GLY ARG PHE          
SEQRES  18 A  422  ASP VAL LEU PRO LEU LEU LEU GLN ALA ASN GLY ASN ASP          
SEQRES  19 A  422  PRO GLU LEU PHE GLN ILE PRO PRO GLU LEU VAL LEU GLU          
SEQRES  20 A  422  VAL PRO ILE ARG HIS PRO LYS PHE ASP TRP PHE LYS ASP          
SEQRES  21 A  422  LEU GLY LEU LYS TRP TYR GLY LEU PRO ALA VAL SER ASN          
SEQRES  22 A  422  MET LEU LEU GLU ILE GLY GLY LEU GLU PHE SER ALA CYS          
SEQRES  23 A  422  PRO PHE SER GLY TRP TYR MET GLY THR GLU ILE GLY VAL          
SEQRES  24 A  422  ARG ASP CYS CYS ASP ASN SER ARG TYR ASN ILE LEU GLU          
SEQRES  25 A  422  GLU VAL ALA LYS LYS MET ASP LEU ASP MET ARG LYS THR          
SEQRES  26 A  422  SER SER LEU TRP LYS ASP GLN ALA LEU VAL GLU ILE ASN          
SEQRES  27 A  422  ILE ALA VAL LEU TYR SER PHE GLN SER ASP LYS VAL THR          
SEQRES  28 A  422  ILE VAL ASP HIS HIS SER ALA THR GLU SER PHE ILE LYS          
SEQRES  29 A  422  HIS MET GLU ASN GLU TYR ARG CYS ARG GLY GLY CYS PRO          
SEQRES  30 A  422  ALA ASP TRP VAL TRP ILE VAL PRO PRO MET SER GLY SER          
SEQRES  31 A  422  ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR ARG          
SEQRES  32 A  422  LEU THR PRO SER PHE GLU TYR GLN PRO ASP PRO TRP ASN          
SEQRES  33 A  422  THR HIS VAL TRP LYS GLY                                      
SEQRES   1 B  422  CYS PRO ARG PHE LEU LYS VAL LYS ASN TRP GLU THR ASP          
SEQRES   2 B  422  VAL VAL LEU THR ASP THR LEU HIS LEU LYS SER THR LEU          
SEQRES   3 B  422  GLU THR GLY CYS THR GLU HIS ILE CYS MET GLY SER ILE          
SEQRES   4 B  422  MET LEU PRO SER GLN HIS THR ARG LYS PRO GLU ASP VAL          
SEQRES   5 B  422  ARG THR LYS ASP GLN LEU PHE PRO LEU ALA LYS GLU PHE          
SEQRES   6 B  422  LEU ASP GLN TYR TYR SER SER ILE LYS ARG PHE GLY SER          
SEQRES   7 B  422  LYS ALA HIS MET ASP ARG LEU GLU GLU VAL ASN LYS GLU          
SEQRES   8 B  422  ILE GLU SER THR SER THR TYR GLN LEU LYS ASP THR GLU          
SEQRES   9 B  422  LEU ILE TYR GLY ALA LYS HIS ALA TRP ARG ASN ALA SER          
SEQRES  10 B  422  ARG CYS VAL GLY ARG ILE GLN TRP SER LYS LEU GLN VAL          
SEQRES  11 B  422  PHE ASP ALA ARG ASP CYS THR THR ALA HIS GLY MET PHE          
SEQRES  12 B  422  ASN TYR ILE CYS ASN HIS VAL LYS TYR ALA THR ASN LYS          
SEQRES  13 B  422  GLY ASN LEU ARG SER ALA ILE THR ILE PHE PRO GLN ARG          
SEQRES  14 B  422  THR ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN SER GLN          
SEQRES  15 B  422  LEU ILE ARG TYR ALA GLY TYR LYS GLN PRO ASP GLY SER          
SEQRES  16 B  422  THR LEU GLY ASP PRO ALA ASN VAL GLN PHE THR GLU ILE          
SEQRES  17 B  422  CYS ILE GLN GLN GLY TRP LYS ALA PRO ARG GLY ARG PHE          
SEQRES  18 B  422  ASP VAL LEU PRO LEU LEU LEU GLN ALA ASN GLY ASN ASP          
SEQRES  19 B  422  PRO GLU LEU PHE GLN ILE PRO PRO GLU LEU VAL LEU GLU          
SEQRES  20 B  422  VAL PRO ILE ARG HIS PRO LYS PHE ASP TRP PHE LYS ASP          
SEQRES  21 B  422  LEU GLY LEU LYS TRP TYR GLY LEU PRO ALA VAL SER ASN          
SEQRES  22 B  422  MET LEU LEU GLU ILE GLY GLY LEU GLU PHE SER ALA CYS          
SEQRES  23 B  422  PRO PHE SER GLY TRP TYR MET GLY THR GLU ILE GLY VAL          
SEQRES  24 B  422  ARG ASP CYS CYS ASP ASN SER ARG TYR ASN ILE LEU GLU          
SEQRES  25 B  422  GLU VAL ALA LYS LYS MET ASP LEU ASP MET ARG LYS THR          
SEQRES  26 B  422  SER SER LEU TRP LYS ASP GLN ALA LEU VAL GLU ILE ASN          
SEQRES  27 B  422  ILE ALA VAL LEU TYR SER PHE GLN SER ASP LYS VAL THR          
SEQRES  28 B  422  ILE VAL ASP HIS HIS SER ALA THR GLU SER PHE ILE LYS          
SEQRES  29 B  422  HIS MET GLU ASN GLU TYR ARG CYS ARG GLY GLY CYS PRO          
SEQRES  30 B  422  ALA ASP TRP VAL TRP ILE VAL PRO PRO MET SER GLY SER          
SEQRES  31 B  422  ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR ARG          
SEQRES  32 B  422  LEU THR PRO SER PHE GLU TYR GLN PRO ASP PRO TRP ASN          
SEQRES  33 B  422  THR HIS VAL TRP LYS GLY                                      
HET    HEM  A 801      43                                                       
HET    H4B  A 802      17                                                       
HET    1Q7  A 803      24                                                       
HET    ACT  A 804       4                                                       
HET     ZN  A 805       1                                                       
HET    HEM  B 801      43                                                       
HET    H4B  B 802      17                                                       
HET    1Q7  B 803      24                                                       
HET    ACT  B 804       4                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     H4B 5,6,7,8-TETRAHYDROBIOPTERIN                                      
HETNAM     1Q7 6,6'-{[(2R)-3-AMINOPROPANE-1,2-                                  
HETNAM   2 1Q7  DIYL]BIS(OXYMETHANEDIYL)}BIS(4-METHYLPYRIDIN-2-AMINE)           
HETNAM     ACT ACETATE ION                                                      
HETNAM      ZN ZINC ION                                                         
HETSYN     HEM HEME                                                             
FORMUL   3  HEM    2(C34 H32 FE N4 O4)                                          
FORMUL   4  H4B    2(C9 H15 N5 O3)                                              
FORMUL   5  1Q7    2(C17 H25 N5 O2)                                             
FORMUL   6  ACT    2(C2 H3 O2 1-)                                               
FORMUL   7   ZN    ZN 2+                                                        
FORMUL  12  HOH   *462(H2 O)                                                    
HELIX    1   1 THR A  315  SER A  320  5                                   6    
HELIX    2   2 LYS A  351  ILE A  369  1                                  19    
HELIX    3   3 SER A  374  SER A  392  1                                  19    
HELIX    4   4 LYS A  397  ASN A  411  1                                  15    
HELIX    5   5 GLY A  417  TRP A  421  5                                   5    
HELIX    6   6 THR A  434  ASN A  451  1                                  18    
HELIX    7   7 LYS A  452  ASN A  454  5                                   3    
HELIX    8   8 ASN A  498  GLN A  508  1                                  11    
HELIX    9   9 PRO A  537  VAL A  541  5                                   5    
HELIX   10  10 PHE A  551  GLY A  558  5                                   8    
HELIX   11  11 GLY A  590  VAL A  595  1                                   6    
HELIX   12  12 VAL A  595  ASP A  600  1                                   6    
HELIX   13  13 ILE A  606  MET A  614  1                                   9    
HELIX   14  14 LYS A  620  SER A  623  5                                   4    
HELIX   15  15 LEU A  624  ASP A  644  1                                  21    
HELIX   16  16 ASP A  650  GLY A  670  1                                  21    
HELIX   17  17 ASP A  675  VAL A  680  1                                   6    
HELIX   18  18 SER A  684  GLN A  693  5                                  10    
HELIX   19  19 ASP A  709  HIS A  714  1                                   6    
HELIX   20  20 THR B  315  SER B  320  5                                   6    
HELIX   21  21 THR B  350  ILE B  369  1                                  20    
HELIX   22  22 SER B  374  SER B  392  1                                  19    
HELIX   23  23 LYS B  397  ASN B  411  1                                  15    
HELIX   24  24 GLY B  417  TRP B  421  5                                   5    
HELIX   25  25 THR B  434  ASN B  451  1                                  18    
HELIX   26  26 LYS B  452  ASN B  454  5                                   3    
HELIX   27  27 ASN B  498  GLN B  508  1                                  11    
HELIX   28  28 PRO B  537  VAL B  541  5                                   5    
HELIX   29  29 PHE B  551  GLY B  558  5                                   8    
HELIX   30  30 GLY B  590  VAL B  595  1                                   6    
HELIX   31  31 VAL B  595  ASP B  600  1                                   6    
HELIX   32  32 ILE B  606  MET B  614  1                                   9    
HELIX   33  33 LYS B  620  SER B  623  5                                   4    
HELIX   34  34 LEU B  624  ASP B  644  1                                  21    
HELIX   35  35 ASP B  650  GLY B  670  1                                  21    
HELIX   36  36 ASP B  675  VAL B  680  1                                   6    
HELIX   37  37 SER B  684  GLN B  693  5                                  10    
HELIX   38  38 ASP B  709  HIS B  714  1                                   6    
SHEET    1   A 2 LEU A 301  LYS A 304  0                                        
SHEET    2   A 2 VAL A 311  ASP A 314 -1  O  ASP A 314   N  LEU A 301           
SHEET    1   B 4 GLN A 425  ASP A 428  0                                        
SHEET    2   B 4 ALA A 458  ILE A 461  1  O  ILE A 459   N  PHE A 427           
SHEET    3   B 4 PHE A 584  SER A 585 -1  O  SER A 585   N  ALA A 458           
SHEET    4   B 4 ALA A 566  VAL A 567 -1  N  VAL A 567   O  PHE A 584           
SHEET    1   C 3 ARG A 473  VAL A 474  0                                        
SHEET    2   C 3 LEU A 522  GLN A 525 -1  O  GLN A 525   N  ARG A 473           
SHEET    3   C 3 GLU A 532  PHE A 534 -1  O  PHE A 534   N  LEU A 522           
SHEET    1   D 2 GLY A 484  LYS A 486  0                                        
SHEET    2   D 2 THR A 492  GLY A 494 -1  O  LEU A 493   N  TYR A 485           
SHEET    1   E 2 GLU A 543  PRO A 545  0                                        
SHEET    2   E 2 LYS A 560  TYR A 562 -1  O  TRP A 561   N  VAL A 544           
SHEET    1   F 3 LEU A 577  PHE A 579  0                                        
SHEET    2   F 3 LEU A 571  ILE A 574 -1  N  LEU A 572   O  PHE A 579           
SHEET    3   F 3 SER A 703  GLU A 705 -1  O  GLU A 705   N  LEU A 571           
SHEET    1   G 2 TYR A 588  MET A 589  0                                        
SHEET    2   G 2 ILE A 648  VAL A 649  1  O  VAL A 649   N  TYR A 588           
SHEET    1   H 2 LEU B 301  LYS B 304  0                                        
SHEET    2   H 2 VAL B 311  ASP B 314 -1  O  ASP B 314   N  LEU B 301           
SHEET    1   I 4 GLN B 425  ASP B 428  0                                        
SHEET    2   I 4 ALA B 458  ILE B 461  1  O  ILE B 459   N  PHE B 427           
SHEET    3   I 4 PHE B 584  SER B 585 -1  O  SER B 585   N  ALA B 458           
SHEET    4   I 4 ALA B 566  VAL B 567 -1  N  VAL B 567   O  PHE B 584           
SHEET    1   J 3 ARG B 473  VAL B 474  0                                        
SHEET    2   J 3 LEU B 522  GLN B 525 -1  O  GLN B 525   N  ARG B 473           
SHEET    3   J 3 GLU B 532  PHE B 534 -1  O  PHE B 534   N  LEU B 522           
SHEET    1   K 2 GLY B 484  LYS B 486  0                                        
SHEET    2   K 2 THR B 492  GLY B 494 -1  O  LEU B 493   N  TYR B 485           
SHEET    1   L 2 GLU B 543  PRO B 545  0                                        
SHEET    2   L 2 LYS B 560  TYR B 562 -1  O  TRP B 561   N  VAL B 544           
SHEET    1   M 3 LEU B 577  PHE B 579  0                                        
SHEET    2   M 3 LEU B 571  ILE B 574 -1  N  LEU B 572   O  PHE B 579           
SHEET    3   M 3 SER B 703  GLU B 705 -1  O  SER B 703   N  GLU B 573           
SHEET    1   N 2 TYR B 588  MET B 589  0                                        
SHEET    2   N 2 ILE B 648  VAL B 649  1  O  VAL B 649   N  TYR B 588           
LINK         SG  CYS A 331                ZN    ZN A 805     1555   1555  2.34  
LINK         SG  CYS A 326                ZN    ZN A 805     1555   1555  2.35  
LINK         SG  CYS B 331                ZN    ZN A 805     1555   1555  2.38  
LINK         SG  CYS B 326                ZN    ZN A 805     1555   1555  2.40  
LINK         SG  CYS A 415                FE   HEM A 801     1555   1555  2.47  
LINK         SG  CYS B 415                FE   HEM B 801     1555   1555  2.50  
CISPEP   1 THR A  701    PRO A  702          0        -4.04                     
CISPEP   2 THR A  701    PRO A  702          0        -3.85                     
CISPEP   3 THR B  701    PRO B  702          0        -2.50                     
SITE     1 AC1 18 TRP A 409  ARG A 414  CYS A 415  VAL A 416                    
SITE     2 AC1 18 SER A 457  PHE A 584  SER A 585  GLY A 586                    
SITE     3 AC1 18 TRP A 587  GLU A 592  TRP A 678  PHE A 704                    
SITE     4 AC1 18 TYR A 706  H4B A 802  1Q7 A 803  HOH A 926                    
SITE     5 AC1 18 HOH A 930  HOH A 939                                          
SITE     1 AC2 15 SER A 334  ARG A 596  VAL A 677  TRP A 678                    
SITE     2 AC2 15 HEM A 801  HOH A 904  HOH A 930  HOH A 949                    
SITE     3 AC2 15 HOH A1043  HOH A1064  TRP B 676  PHE B 691                    
SITE     4 AC2 15 HIS B 692  GLN B 693  GLU B 694                               
SITE     1 AC3 14 MET A 336  GLN A 478  ARG A 481  ALA A 497                    
SITE     2 AC3 14 PRO A 565  VAL A 567  PHE A 584  GLY A 586                    
SITE     3 AC3 14 TRP A 587  TYR A 588  GLU A 592  HEM A 801                    
SITE     4 AC3 14 HOH A 920  HOH A 930                                          
SITE     1 AC4  3 GLN A 420  TRP A 587  VAL A 649                               
SITE     1 AC5  4 CYS A 326  CYS A 331  CYS B 326  CYS B 331                    
SITE     1 AC6 15 TRP B 409  CYS B 415  SER B 457  PHE B 584                    
SITE     2 AC6 15 SER B 585  TRP B 587  GLU B 592  TRP B 678                    
SITE     3 AC6 15 TYR B 706  H4B B 802  1Q7 B 803  HOH B 963                    
SITE     4 AC6 15 HOH B 973  HOH B 988  HOH B1084                               
SITE     1 AC7 14 TRP A 676  PHE A 691  HIS A 692  GLU A 694                    
SITE     2 AC7 14 SER B 334  ARG B 596  VAL B 677  TRP B 678                    
SITE     3 AC7 14 HEM B 801  HOH B 988  HOH B1003  HOH B1031                    
SITE     4 AC7 14 HOH B1095  HOH B1105                                          
SITE     1 AC8 12 GLN B 478  ARG B 481  ALA B 497  VAL B 567                    
SITE     2 AC8 12 PHE B 584  GLY B 586  TRP B 587  TYR B 588                    
SITE     3 AC8 12 GLU B 592  HEM B 801  HOH B 911  HOH B1009                    
SITE     1 AC9  6 TRP B 587  VAL B 649  HOH B 998  HOH B1002                    
SITE     2 AC9  6 HOH B1005  HOH B1024                                          
CRYST1   51.996  110.666  164.391  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      0.019232  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009036  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006083        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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