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Database: PDB
Entry: 3UFW
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HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 01-NOV-11   3UFW              
TITLE     STRUCTURE OF RAT NITRIC OXIDE SYNTHASE HEME DOMAIN IN COMPLEX WITH 6- 
TITLE    2 (((3R,4R)-4-((5-(6-AMINOPYRIDIN-2-YL)PENTYL)OXY)PYRROLIDIN-3-YL)     
TITLE    3 METHYL)-4-METHYLPYRIDIN-2-AMINE                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NITRIC OXIDE SYNTHASE, BRAIN;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: 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: BROWN RAT,RAT,RATS;                                 
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, INHIBITOR BINDING, OXIDOREDUCTASE-             
KEYWDS   2 OXIDOREDUCTASE INHIBITOR COMPLEX                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.LI,T.L.POULOS                                                       
REVDAT   3   08-NOV-17 3UFW    1       REMARK                                   
REVDAT   2   01-AUG-12 3UFW    1       JRNL                                     
REVDAT   1   11-JUL-12 3UFW    0                                                
JRNL        AUTH   H.HUANG,H.JI,H.LI,Q.JING,K.J.LABBY,P.MARTASEK,L.J.ROMAN,     
JRNL        AUTH 2 T.L.POULOS,R.B.SILVERMAN                                     
JRNL        TITL   SELECTIVE MONOCATIONIC INHIBITORS OF NEURONAL NITRIC OXIDE   
JRNL        TITL 2 SYNTHASE. BINDING MODE INSIGHTS FROM MOLECULAR DYNAMICS      
JRNL        TITL 3 SIMULATIONS.                                                 
JRNL        REF    J.AM.CHEM.SOC.                V. 134 11559 2012              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   22731813                                                     
JRNL        DOI    10.1021/JA302269R                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.49                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 61504                          
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) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3186                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4417                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.34                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3440                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 216                          
REMARK   3   BIN FREE R VALUE                    : 0.3540                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6658                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 183                                     
REMARK   3   SOLVENT ATOMS            : 252                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 54.35                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.36000                                              
REMARK   3    B22 (A**2) : 0.19000                                              
REMARK   3    B33 (A**2) : -0.54000                                             
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): 0.185         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.169         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.155         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.816        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7055 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9601 ; 1.513 ; 1.992       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   818 ; 6.181 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   332 ;33.617 ;23.855       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1168 ;15.505 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    41 ;17.774 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   994 ; 0.101 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5411 ; 0.008 ; 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):  4087 ; 0.746 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6628 ; 1.312 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2968 ; 2.253 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2971 ; 3.300 ; 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 : 5                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   299        A   716                          
REMARK   3    RESIDUE RANGE :   A   750        A   750                          
REMARK   3    RESIDUE RANGE :   A   760        A   760                          
REMARK   3    RESIDUE RANGE :   A   860        A   860                          
REMARK   3    RESIDUE RANGE :   A   800        A   800                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.4530   4.6330  22.5970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0463 T22:   0.1246                                     
REMARK   3      T33:   0.2204 T12:   0.0120                                     
REMARK   3      T13:   0.0072 T23:  -0.0185                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5530 L22:   0.7391                                     
REMARK   3      L33:   5.9500 L12:  -0.0626                                     
REMARK   3      L13:  -0.5786 L23:  -0.3597                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0352 S12:   0.1451 S13:   0.0141                       
REMARK   3      S21:  -0.0255 S22:  -0.0586 S23:   0.0566                       
REMARK   3      S31:   0.0118 S32:  -0.3863 S33:   0.0938                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 5                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   299        B   718                          
REMARK   3    RESIDUE RANGE :   B   750        B   750                          
REMARK   3    RESIDUE RANGE :   B   760        B   760                          
REMARK   3    RESIDUE RANGE :   B   800        B   800                          
REMARK   3    RESIDUE RANGE :   B   860        B   860                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.1370   4.8160  59.8910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0192 T22:   0.0715                                     
REMARK   3      T33:   0.2209 T12:   0.0060                                     
REMARK   3      T13:   0.0164 T23:   0.0233                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7615 L22:   0.9052                                     
REMARK   3      L33:   2.7326 L12:  -0.2044                                     
REMARK   3      L13:  -0.2221 L23:   0.2775                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0145 S12:  -0.0453 S13:   0.0769                       
REMARK   3      S21:  -0.0576 S22:  -0.0432 S23:  -0.0297                       
REMARK   3      S31:   0.0024 S32:   0.0781 S33:   0.0577                       
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3UFW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-NOV-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000068703.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-JUL-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                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.097                              
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 64761                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
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     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.07700                            
REMARK 200  R SYM                      (I) : 0.07700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.65400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.65400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
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   (%): 49.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-24% PEG3350, 0.1M MES, 140-200MM      
REMARK 280  AMMONIUM SULFATE, 10% ETHYLENE GLYCOL, 5MM GSH, 35UM SDS, PH 5.8,   
REMARK 280  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       25.95100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       82.04200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.62250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       82.04200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.95100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.62250            
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: 5350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     CYS A   297                                                      
REMARK 465     PRO A   298                                                      
REMARK 465     SER A   339                                                      
REMARK 465     GLN A   340                                                      
REMARK 465     HIS A   341                                                      
REMARK 465     THR A   342                                                      
REMARK 465     ARG A   343                                                      
REMARK 465     LYS A   344                                                      
REMARK 465     PRO A   345                                                      
REMARK 465     GLU A   346                                                      
REMARK 465     ASP A   347                                                      
REMARK 465     VAL A   348                                                      
REMARK 465     ARG A   349                                                      
REMARK 465     LYS A   717                                                      
REMARK 465     GLY A   718                                                      
REMARK 465     CYS B   297                                                      
REMARK 465     PRO B   298                                                      
REMARK 465     SER B   339                                                      
REMARK 465     GLN B   340                                                      
REMARK 465     HIS B   341                                                      
REMARK 465     THR B   342                                                      
REMARK 465     ARG B   343                                                      
REMARK 465     LYS B   344                                                      
REMARK 465     PRO B   345                                                      
REMARK 465     GLU B   346                                                      
REMARK 465     ASP B   347                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   SG   CYS B   668     O    HOH B   185              2.06            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A 300      102.77    161.35                                   
REMARK 500    ASP A 309       -1.88     69.81                                   
REMARK 500    THR A 321      -57.93   -121.95                                   
REMARK 500    THR A 466      -83.25   -112.02                                   
REMARK 500    HIS A 470       30.53   -141.14                                   
REMARK 500    ASP A 489      -35.85    -32.80                                   
REMARK 500    SER A 491     -156.67    -86.26                                   
REMARK 500    CYS A 582       58.07   -157.64                                   
REMARK 500    ARG A 603     -136.08   -105.72                                   
REMARK 500    CYS A 672      105.92   -163.64                                   
REMARK 500    ASP A 709      124.43    -36.86                                   
REMARK 500    LEU B 322     -179.51    -68.53                                   
REMARK 500    SER B 392       -6.49     78.73                                   
REMARK 500    THR B 466      -83.05   -111.31                                   
REMARK 500    CYS B 582       63.03   -153.01                                   
REMARK 500    ARG B 603     -137.19   -117.90                                   
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 900  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 326   SG                                                     
REMARK 620 2 CYS B 331   SG  100.0                                              
REMARK 620 3 CYS A 331   SG  114.9 101.1                                        
REMARK 620 4 CYS B 326   SG  123.7 111.8 103.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 750  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 415   SG                                                     
REMARK 620 2 HEM A 750   NA   94.6                                              
REMARK 620 3 HEM A 750   NB   92.2  88.4                                        
REMARK 620 4 HEM A 750   NC   93.0 172.4  91.3                                  
REMARK 620 5 HEM A 750   ND   95.6  89.9 172.2  89.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 750  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 415   SG                                                     
REMARK 620 2 HEM B 750   NA   94.5                                              
REMARK 620 3 HEM B 750   NB   90.6  87.7                                        
REMARK 620 4 HEM B 750   NC   92.2 173.3  91.9                                  
REMARK 620 5 HEM B 750   ND   95.2  92.5 174.1  87.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 750                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B A 760                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 860                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HW0 A 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 900                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 750                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B B 760                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HW0 B 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 860                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3UFO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3UFP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3UFQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3UFR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3UFS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3UFT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3UFU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3UFV   RELATED DB: PDB                                   
DBREF  3UFW A  297   718  UNP    P29476   NOS1_RAT       297    718             
DBREF  3UFW B  297   718  UNP    P29476   NOS1_RAT       297    718             
SEQRES   1 A  422  CYS PRO ARG PHE LEU LYS VAL LYS ASN TRP GLU THR ASP          
SEQRES   2 A  422  VAL VAL LEU THR ASP THR LEU HIS LEU LYS SER THR LEU          
SEQRES   3 A  422  GLU THR GLY CYS THR GLU HIS ILE CYS MET GLY SER ILE          
SEQRES   4 A  422  MET LEU PRO SER GLN HIS THR ARG LYS PRO GLU ASP VAL          
SEQRES   5 A  422  ARG THR LYS ASP GLN LEU PHE PRO LEU ALA LYS GLU PHE          
SEQRES   6 A  422  LEU ASP GLN TYR TYR SER SER ILE LYS ARG PHE GLY SER          
SEQRES   7 A  422  LYS ALA HIS MET ASP ARG LEU GLU GLU VAL ASN LYS GLU          
SEQRES   8 A  422  ILE GLU SER THR SER THR TYR GLN LEU LYS ASP THR GLU          
SEQRES   9 A  422  LEU ILE TYR GLY ALA LYS HIS ALA TRP ARG ASN ALA SER          
SEQRES  10 A  422  ARG CYS VAL GLY ARG ILE GLN TRP SER LYS LEU GLN VAL          
SEQRES  11 A  422  PHE ASP ALA ARG ASP CYS THR THR ALA HIS GLY MET PHE          
SEQRES  12 A  422  ASN TYR ILE CYS ASN HIS VAL LYS TYR ALA THR ASN LYS          
SEQRES  13 A  422  GLY ASN LEU ARG SER ALA ILE THR ILE PHE PRO GLN ARG          
SEQRES  14 A  422  THR ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN SER GLN          
SEQRES  15 A  422  LEU ILE ARG TYR ALA GLY TYR LYS GLN PRO ASP GLY SER          
SEQRES  16 A  422  THR LEU GLY ASP PRO ALA ASN VAL GLN PHE THR GLU ILE          
SEQRES  17 A  422  CYS ILE GLN GLN GLY TRP LYS ALA PRO ARG GLY ARG PHE          
SEQRES  18 A  422  ASP VAL LEU PRO LEU LEU LEU GLN ALA ASN GLY ASN ASP          
SEQRES  19 A  422  PRO GLU LEU PHE GLN ILE PRO PRO GLU LEU VAL LEU GLU          
SEQRES  20 A  422  VAL PRO ILE ARG HIS PRO LYS PHE ASP TRP PHE LYS ASP          
SEQRES  21 A  422  LEU GLY LEU LYS TRP TYR GLY LEU PRO ALA VAL SER ASN          
SEQRES  22 A  422  MET LEU LEU GLU ILE GLY GLY LEU GLU PHE SER ALA CYS          
SEQRES  23 A  422  PRO PHE SER GLY TRP TYR MET GLY THR GLU ILE GLY VAL          
SEQRES  24 A  422  ARG ASP TYR CYS ASP ASN SER ARG TYR ASN ILE LEU GLU          
SEQRES  25 A  422  GLU VAL ALA LYS LYS MET ASP LEU ASP MET ARG LYS THR          
SEQRES  26 A  422  SER SER LEU TRP LYS ASP GLN ALA LEU VAL GLU ILE ASN          
SEQRES  27 A  422  ILE ALA VAL LEU TYR SER PHE GLN SER ASP LYS VAL THR          
SEQRES  28 A  422  ILE VAL ASP HIS HIS SER ALA THR GLU SER PHE ILE LYS          
SEQRES  29 A  422  HIS MET GLU ASN GLU TYR ARG CYS ARG GLY GLY CYS PRO          
SEQRES  30 A  422  ALA ASP TRP VAL TRP ILE VAL PRO PRO MET SER GLY SER          
SEQRES  31 A  422  ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR ARG          
SEQRES  32 A  422  LEU THR PRO SER PHE GLU TYR GLN PRO ASP PRO TRP ASN          
SEQRES  33 A  422  THR HIS VAL TRP LYS GLY                                      
SEQRES   1 B  422  CYS PRO ARG PHE LEU LYS VAL LYS ASN TRP GLU THR ASP          
SEQRES   2 B  422  VAL VAL LEU THR ASP THR LEU HIS LEU LYS SER THR LEU          
SEQRES   3 B  422  GLU THR GLY CYS THR GLU HIS ILE CYS MET GLY SER ILE          
SEQRES   4 B  422  MET LEU PRO SER GLN HIS THR ARG LYS PRO GLU ASP VAL          
SEQRES   5 B  422  ARG THR LYS ASP GLN LEU PHE PRO LEU ALA LYS GLU PHE          
SEQRES   6 B  422  LEU ASP GLN TYR TYR SER SER ILE LYS ARG PHE GLY SER          
SEQRES   7 B  422  LYS ALA HIS MET ASP ARG LEU GLU GLU VAL ASN LYS GLU          
SEQRES   8 B  422  ILE GLU SER THR SER THR TYR GLN LEU LYS ASP THR GLU          
SEQRES   9 B  422  LEU ILE TYR GLY ALA LYS HIS ALA TRP ARG ASN ALA SER          
SEQRES  10 B  422  ARG CYS VAL GLY ARG ILE GLN TRP SER LYS LEU GLN VAL          
SEQRES  11 B  422  PHE ASP ALA ARG ASP CYS THR THR ALA HIS GLY MET PHE          
SEQRES  12 B  422  ASN TYR ILE CYS ASN HIS VAL LYS TYR ALA THR ASN LYS          
SEQRES  13 B  422  GLY ASN LEU ARG SER ALA ILE THR ILE PHE PRO GLN ARG          
SEQRES  14 B  422  THR ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN SER GLN          
SEQRES  15 B  422  LEU ILE ARG TYR ALA GLY TYR LYS GLN PRO ASP GLY SER          
SEQRES  16 B  422  THR LEU GLY ASP PRO ALA ASN VAL GLN PHE THR GLU ILE          
SEQRES  17 B  422  CYS ILE GLN GLN GLY TRP LYS ALA PRO ARG GLY ARG PHE          
SEQRES  18 B  422  ASP VAL LEU PRO LEU LEU LEU GLN ALA ASN GLY ASN ASP          
SEQRES  19 B  422  PRO GLU LEU PHE GLN ILE PRO PRO GLU LEU VAL LEU GLU          
SEQRES  20 B  422  VAL PRO ILE ARG HIS PRO LYS PHE ASP TRP PHE LYS ASP          
SEQRES  21 B  422  LEU GLY LEU LYS TRP TYR GLY LEU PRO ALA VAL SER ASN          
SEQRES  22 B  422  MET LEU LEU GLU ILE GLY GLY LEU GLU PHE SER ALA CYS          
SEQRES  23 B  422  PRO PHE SER GLY TRP TYR MET GLY THR GLU ILE GLY VAL          
SEQRES  24 B  422  ARG ASP TYR CYS ASP ASN SER ARG TYR ASN ILE LEU GLU          
SEQRES  25 B  422  GLU VAL ALA LYS LYS MET ASP LEU ASP MET ARG LYS THR          
SEQRES  26 B  422  SER SER LEU TRP LYS ASP GLN ALA LEU VAL GLU ILE ASN          
SEQRES  27 B  422  ILE ALA VAL LEU TYR SER PHE GLN SER ASP LYS VAL THR          
SEQRES  28 B  422  ILE VAL ASP HIS HIS SER ALA THR GLU SER PHE ILE LYS          
SEQRES  29 B  422  HIS MET GLU ASN GLU TYR ARG CYS ARG GLY GLY CYS PRO          
SEQRES  30 B  422  ALA ASP TRP VAL TRP ILE VAL PRO PRO MET SER GLY SER          
SEQRES  31 B  422  ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR ARG          
SEQRES  32 B  422  LEU THR PRO SER PHE GLU TYR GLN PRO ASP PRO TRP ASN          
SEQRES  33 B  422  THR HIS VAL TRP LYS GLY                                      
HET    HEM  A 750      43                                                       
HET    H4B  A 760      17                                                       
HET    ACT  A 860       4                                                       
HET    HW0  A 800      27                                                       
HET     ZN  A 900       1                                                       
HET    HEM  B 750      43                                                       
HET    H4B  B 760      17                                                       
HET    HW0  B 800      27                                                       
HET    ACT  B 860       4                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     H4B 5,6,7,8-TETRAHYDROBIOPTERIN                                      
HETNAM     ACT ACETATE ION                                                      
HETNAM     HW0 6-{[(3R,4R)-4-{[5-(6-AMINOPYRIDIN-2-YL)                          
HETNAM   2 HW0  PENTYL]OXY}PYRROLIDIN-3-YL]METHYL}-4-METHYLPYRIDIN-2-           
HETNAM   3 HW0  AMINE                                                           
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  ACT    2(C2 H3 O2 1-)                                               
FORMUL   6  HW0    2(C21 H31 N5 O)                                              
FORMUL   7   ZN    ZN 2+                                                        
FORMUL  12  HOH   *252(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  507  1                                  10    
HELIX    9   9 PHE A  551  GLY A  558  5                                   8    
HELIX   10  10 GLY A  590  VAL A  595  1                                   6    
HELIX   11  11 VAL A  595  ASP A  600  1                                   6    
HELIX   12  12 ILE A  606  MET A  614  1                                   9    
HELIX   13  13 LYS A  620  SER A  623  5                                   4    
HELIX   14  14 LEU A  624  ASP A  644  1                                  21    
HELIX   15  15 ASP A  650  GLY A  670  1                                  21    
HELIX   16  16 ASP A  675  VAL A  680  1                                   6    
HELIX   17  17 SER A  684  GLN A  693  5                                  10    
HELIX   18  18 ASP A  709  THR A  713  5                                   5    
HELIX   19  19 THR B  315  SER B  320  5                                   6    
HELIX   20  20 THR B  350  ILE B  369  1                                  20    
HELIX   21  21 SER B  374  SER B  392  1                                  19    
HELIX   22  22 LYS B  397  ASN B  411  1                                  15    
HELIX   23  23 GLY B  417  TRP B  421  5                                   5    
HELIX   24  24 THR B  434  ASN B  451  1                                  18    
HELIX   25  25 LYS B  452  ASN B  454  5                                   3    
HELIX   26  26 ASN B  498  GLN B  508  1                                  11    
HELIX   27  27 PRO B  537  VAL B  541  5                                   5    
HELIX   28  28 TRP B  553  GLY B  558  5                                   6    
HELIX   29  29 GLY B  590  VAL B  595  1                                   6    
HELIX   30  30 VAL B  595  ASP B  600  1                                   6    
HELIX   31  31 ILE B  606  MET B  614  1                                   9    
HELIX   32  32 LYS B  620  SER B  623  5                                   4    
HELIX   33  33 LEU B  624  ASP B  644  1                                  21    
HELIX   34  34 ASP B  650  GLY B  670  1                                  21    
HELIX   35  35 ASP B  675  VAL B  680  1                                   6    
HELIX   36  36 SER B  684  GLN B  693  5                                  10    
HELIX   37  37 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  GLU B 532   N  LEU B 524           
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 326                ZN    ZN A 900     1555   1555  2.24  
LINK         SG  CYS B 331                ZN    ZN A 900     1555   1555  2.35  
LINK         SG  CYS A 331                ZN    ZN A 900     1555   1555  2.36  
LINK         SG  CYS B 326                ZN    ZN A 900     1555   1555  2.37  
LINK         SG  CYS A 415                FE   HEM A 750     1555   1555  2.38  
LINK         SG  CYS B 415                FE   HEM B 750     1555   1555  2.43  
CISPEP   1 THR A  701    PRO A  702          0        -1.72                     
CISPEP   2 THR B  701    PRO B  702          0        -4.89                     
SITE     1 AC1 12 HOH A  46  HOH A 167  TRP A 409  CYS A 415                    
SITE     2 AC1 12 VAL A 416  SER A 457  PHE A 584  SER A 585                    
SITE     3 AC1 12 TRP A 587  GLU A 592  H4B A 760  HW0 A 800                    
SITE     1 AC2 14 HOH A  88  HOH A 160  HOH A 228  SER A 334                    
SITE     2 AC2 14 ARG A 596  VAL A 677  TRP A 678  HEM A 750                    
SITE     3 AC2 14 HW0 A 800  TRP B 676  PHE B 691  HIS B 692                    
SITE     4 AC2 14 GLN B 693  GLU B 694                                          
SITE     1 AC3  2 GLN A 420  TRP A 587                                          
SITE     1 AC4 12 HOH A 216  MET A 336  LEU A 337  ARG A 414                    
SITE     2 AC4 12 VAL A 567  TRP A 587  GLU A 592  TRP A 678                    
SITE     3 AC4 12 TYR A 706  HEM A 750  H4B A 760  TRP B 306                    
SITE     1 AC5  4 CYS A 326  CYS A 331  CYS B 326  CYS B 331                    
SITE     1 AC6 12 HOH B  51  HOH B  92  TRP B 409  CYS B 415                    
SITE     2 AC6 12 SER B 457  PHE B 584  SER B 585  TRP B 587                    
SITE     3 AC6 12 GLU B 592  TRP B 678  H4B B 760  HW0 B 800                    
SITE     1 AC7 13 TRP A 676  PHE A 691  HIS A 692  GLU A 694                    
SITE     2 AC7 13 HOH B 110  HOH B 229  HOH B 231  SER B 334                    
SITE     3 AC7 13 ARG B 596  VAL B 677  TRP B 678  HEM B 750                    
SITE     4 AC7 13 HW0 B 800                                                     
SITE     1 AC8 11 MET B 336  ARG B 414  PRO B 565  VAL B 567                    
SITE     2 AC8 11 TRP B 587  TYR B 588  GLU B 592  TRP B 678                    
SITE     3 AC8 11 TYR B 706  HEM B 750  H4B B 760                               
SITE     1 AC9  5 HOH B 172  HOH B 206  HOH B 213  TRP B 587                    
SITE     2 AC9  5 VAL B 649                                                     
CRYST1   51.902  111.245  164.084  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      0.019267  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008989  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006094        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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