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Database: PDB
Entry: 3N62
LinkDB: 3N62
Original site: 3N62 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 25-MAY-10   3N62              
TITLE     STRUCTURE OF NEURONAL NITRIC OXIDE SYNTHASE D597N MUTANT HEME DOMAIN  
TITLE    2 IN COMPLEX WITH 6,6'-(2,2'-(PYRIDINE-3,5-DIYL)BIS(ETHANE-2,1-DIYL))  
TITLE    3 BIS(4-METHYLPYRIDIN-2-AMINE)                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NITRIC OXIDE SYNTHASE;                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ENDOTHELIAL NOS, ENOS, EC-NOS, NOS TYPE III, NOSIII,        
COMPND   5 CONSTITUTIVE NOS, CNOS;                                              
COMPND   6 EC: 1.14.13.39;                                                      
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: NOS3;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PCWORI                                    
KEYWDS    HEME ENZYME, NITRIC OXIDE SYNTHASE, SUBSTRATE INHIBITOR, ZN BINDING', 
KEYWDS   2 OXIDOREDUCTASE, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.LI,S.L.DELKER,T.L.POULOS                                            
REVDAT   3   17-JUL-19 3N62    1       REMARK                                   
REVDAT   2   08-NOV-17 3N62    1       REMARK                                   
REVDAT   1   09-FEB-11 3N62    0                                                
JRNL        AUTH   S.L.DELKER,F.XUE,H.LI,J.JAMAL,R.B.SILVERMAN,T.L.POULOS       
JRNL        TITL   ROLE OF ZINC IN ISOFORM-SELECTIVE INHIBITOR BINDING TO       
JRNL        TITL 2 NEURONAL NITRIC OXIDE SYNTHASE .                             
JRNL        REF    BIOCHEMISTRY                  V.  49 10803 2010              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   21138269                                                     
JRNL        DOI    10.1021/BI1013479                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0089                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.64                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 66262                          
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) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.208                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3453                            
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) : 1.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.00                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4720                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.00                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2440                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 261                          
REMARK   3   BIN FREE R VALUE                    : 0.2860                       
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          : 261                                     
REMARK   3   SOLVENT ATOMS            : 402                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.28                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.35000                                              
REMARK   3    B22 (A**2) : 0.70000                                              
REMARK   3    B33 (A**2) : -2.04000                                             
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.138         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.104         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.944         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.951                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7182 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9787 ; 1.393 ; 2.004       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   833 ; 5.730 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   333 ;34.192 ;23.814       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1180 ;14.490 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    42 ;18.322 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1008 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5544 ; 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):  4111 ; 0.670 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6678 ; 1.221 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3071 ; 2.019 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3099 ; 3.171 ; 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 : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   299        A   860                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.3860   4.7190  22.5580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0894 T22:   0.1150                                     
REMARK   3      T33:   0.0161 T12:  -0.0102                                     
REMARK   3      T13:   0.0084 T23:  -0.0177                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4756 L22:   0.7654                                     
REMARK   3      L33:   3.9784 L12:  -0.0113                                     
REMARK   3      L13:  -0.2643 L23:  -0.3748                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0628 S12:   0.0966 S13:   0.0013                       
REMARK   3      S21:  -0.0155 S22:  -0.0189 S23:   0.0258                       
REMARK   3      S31:  -0.0541 S32:  -0.2595 S33:   0.0817                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   299        B   860                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.3330   4.7620  59.9020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0792 T22:   0.0780                                     
REMARK   3      T33:   0.0237 T12:   0.0098                                     
REMARK   3      T13:   0.0147 T23:   0.0142                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6964 L22:   0.6708                                     
REMARK   3      L33:   2.1227 L12:  -0.1475                                     
REMARK   3      L13:  -0.1711 L23:   0.3140                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0392 S12:  -0.0265 S13:   0.0594                       
REMARK   3      S21:  -0.0431 S22:  -0.0332 S23:   0.0004                       
REMARK   3      S31:  -0.0176 S32:   0.0464 S33:   0.0724                       
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 3N62 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAY-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000059425.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-MAR-09                          
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) : 1.000                              
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69795                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
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     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.06900                            
REMARK 200  R SYM                      (I) : 0.06900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.98                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.57900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1OM4                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-24% PEG3350 100MM MES 100-140MM       
REMARK 280  AMMONIUM ACETATE 5MM GSH, 35UM SDS, PH 5.8, VAPOR DIFFUSION,        
REMARK 280  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       25.90300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       82.05950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.19300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       82.05950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.90300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.19300            
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: 11710 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 32510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -187.0 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       -4.71     56.29                                   
REMARK 500    THR A 321      -61.01   -130.23                                   
REMARK 500    LYS A 423       76.25   -108.73                                   
REMARK 500    THR A 466      -86.76   -109.92                                   
REMARK 500    PHE A 517       56.09   -140.57                                   
REMARK 500    CYS A 582       53.44   -153.83                                   
REMARK 500    ARG A 603     -135.37   -117.53                                   
REMARK 500    ASP B 309       -0.84     63.33                                   
REMARK 500    THR B 321      -59.72   -127.40                                   
REMARK 500    SER B 392       -1.17     74.67                                   
REMARK 500    THR B 466      -81.19   -111.86                                   
REMARK 500    CYS B 582       54.81   -150.66                                   
REMARK 500    VAL B 595      -61.06    -96.10                                   
REMARK 500    ARG B 603     -136.65   -115.24                                   
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 719  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 920   O                                                      
REMARK 620 2 ASP B 600   OD1 106.5                                              
REMARK 620 3 XFJ B 719   N11  11.5  96.7                                        
REMARK 620 4 HIS A 692   NE2 102.4  98.5 110.4                                  
REMARK 620 5 ASP B 600   OD2 160.0  53.5 149.7  82.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 901  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 XFJ B 805   N11                                                    
REMARK 620 2 ASP A 600   OD1 100.4                                              
REMARK 620 3 HOH A 920   O    14.8 102.8                                        
REMARK 620 4 HIS B 692   NE2 101.3 102.7 114.5                                  
REMARK 620 5 ASP A 600   OD2 154.3  54.3 155.3  82.6                            
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  104.7                                              
REMARK 620 3 HEM B 750   NB  100.6  85.1                                        
REMARK 620 4 HEM B 750   NC   97.3 157.9  91.2                                  
REMARK 620 5 HEM B 750   ND  100.7  89.6 158.7  86.0                            
REMARK 620 N                    1     2     3     4                             
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 B 326   SG                                                     
REMARK 620 2 CYS B 331   SG  115.3                                              
REMARK 620 3 CYS A 326   SG  120.4 102.9                                        
REMARK 620 4 CYS A 331   SG  103.3  98.4 114.6                                  
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  104.7                                              
REMARK 620 3 HEM A 750   NB  100.3  85.7                                        
REMARK 620 4 HEM A 750   NC   98.9 156.4  88.8                                  
REMARK 620 5 HEM A 750   ND  102.5  88.8 157.2  87.3                            
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 XFJ A 800                 
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 MTL A 870                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 910                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 900                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B A 760                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 719                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B B 760                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XFJ B 805                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 750                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XFJ B 800                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XFJ B 719                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 860                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTL B 870                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 910                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3N5P   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N5Q   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N5R   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N5S   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N5T   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N5V   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N5W   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N5X   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N5Y   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N5Z   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N60   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N61   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N63   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N64   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N65   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N66   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N67   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N68   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N69   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N6A   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N6B   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N6C   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N6D   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N6E   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N6F   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N6G   RELATED DB: PDB                                   
DBREF  3N62 A  297   718  UNP    P29476   NOS1_RAT       297    718             
DBREF  3N62 B  297   718  UNP    P29476   NOS1_RAT       297    718             
SEQADV 3N62 ASN A  597  UNP  P29476    ASP   597 ENGINEERED MUTATION            
SEQADV 3N62 ASN B  597  UNP  P29476    ASP   597 ENGINEERED MUTATION            
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 ASN 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 ASN 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      48                                                       
HET    XFJ  A 800      26                                                       
HET    ACT  A 860       4                                                       
HET    MTL  A 870      12                                                       
HET     CL  A 910       1                                                       
HET     ZN  A 900       1                                                       
HET     ZN  A 901       1                                                       
HET    H4B  A 760      17                                                       
HET     ZN  A 719       1                                                       
HET    H4B  B 760      17                                                       
HET    XFJ  B 805      26                                                       
HET    HEM  B 750      48                                                       
HET    XFJ  B 800      26                                                       
HET    XFJ  B 719      26                                                       
HET    ACT  B 860       4                                                       
HET    MTL  B 870      12                                                       
HET     CL  B 910       1                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     XFJ 6,6'-(PYRIDINE-3,5-DIYLDIETHANE-2,1-DIYL)BIS(4-                  
HETNAM   2 XFJ  METHYLPYRIDIN-2-AMINE)                                          
HETNAM     ACT ACETATE ION                                                      
HETNAM     MTL D-MANNITOL                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM      ZN ZINC ION                                                         
HETNAM     H4B 5,6,7,8-TETRAHYDROBIOPTERIN                                      
HETSYN     HEM HEME                                                             
FORMUL   3  HEM    2(C34 H32 FE N4 O4)                                          
FORMUL   4  XFJ    4(C21 H25 N5)                                                
FORMUL   5  ACT    2(C2 H3 O2 1-)                                               
FORMUL   6  MTL    2(C6 H14 O6)                                                 
FORMUL   7   CL    2(CL 1-)                                                     
FORMUL   8   ZN    3(ZN 2+)                                                     
FORMUL  10  H4B    2(C9 H15 N5 O3)                                              
FORMUL  20  HOH   *402(H2 O)                                                    
HELIX    1   1 THR A  315  SER A  320  5                                   6    
HELIX    2   2 THR A  350  ILE A  369  1                                  20    
HELIX    3   3 SER A  374  SER A  392  1                                  19    
HELIX    4   4 LYS A  397  ASN A  411  1                                  15    
HELIX    5   5 GLY A  417  TRP A  421  5                                   5    
HELIX    6   6 THR A  434  ASN A  451  1                                  18    
HELIX    7   7 LYS A  452  ASN A  454  5                                   3    
HELIX    8   8 ASN A  498  GLN A  508  1                                  11    
HELIX    9   9 PRO A  537  VAL A  541  5                                   5    
HELIX   10  10 PHE A  551  GLY A  558  5                                   8    
HELIX   11  11 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  THR A  688  5                                   5    
HELIX   19  19 ASP A  709  THR A  713  5                                   5    
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 TRP B  553  GLY B  558  5                                   6    
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  THR B  688  5                                   5    
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        ZN    ZN A 719                 O  BHOH B 920     1555   1555  1.85  
LINK        ZN    ZN A 901                 N11AXFJ B 805     1555   1555  1.94  
LINK         OD1 ASP A 600                ZN    ZN A 901     1555   1555  2.04  
LINK        ZN    ZN A 901                 O  BHOH A 920     1555   1555  2.04  
LINK         OD1 ASP B 600                ZN    ZN A 719     1555   1555  2.12  
LINK         NE2 HIS B 692                ZN    ZN A 901     1555   1555  2.20  
LINK        ZN    ZN A 719                 N11AXFJ B 719     1555   1555  2.21  
LINK         NE2 HIS A 692                ZN    ZN A 719     1555   1555  2.28  
LINK         SG  CYS B 415                FE   HEM B 750     1555   1555  2.35  
LINK         SG  CYS B 326                ZN    ZN A 900     1555   1555  2.37  
LINK         SG  CYS B 331                ZN    ZN A 900     1555   1555  2.38  
LINK         SG  CYS A 326                ZN    ZN A 900     1555   1555  2.39  
LINK         SG  CYS A 331                ZN    ZN A 900     1555   1555  2.39  
LINK         SG  CYS A 415                FE   HEM A 750     1555   1555  2.39  
LINK         OD2 ASP A 600                ZN    ZN A 901     1555   1555  2.66  
LINK         OD2 ASP B 600                ZN    ZN A 719     1555   1555  2.69  
CISPEP   1 THR A  701    PRO A  702          0        -4.70                     
CISPEP   2 THR A  701    PRO A  702          0        -4.18                     
CISPEP   3 THR B  701    PRO B  702          0        -2.20                     
SITE     1 AC1 18 TRP A 409  CYS A 415  SER A 457  PHE A 584                    
SITE     2 AC1 18 SER A 585  GLY A 586  TRP A 587  MET A 589                    
SITE     3 AC1 18 GLU A 592  ARG A 596  TRP A 678  PHE A 704                    
SITE     4 AC1 18 XFJ A 800  HOH A1015  HOH A1041  HOH A1107                    
SITE     5 AC1 18 H4B B 760  XFJ B 805                                          
SITE     1 AC2 12 LEU A 337  ARG A 414  GLN A 478  VAL A 567                    
SITE     2 AC2 12 PHE A 584  TRP A 587  GLU A 592  ARG A 596                    
SITE     3 AC2 12 TYR A 706  HEM A 750  HOH A1069  HOH A1122                    
SITE     1 AC3  4 TRP A 587  SER A 657  HOH A1092  HOH A1119                    
SITE     1 AC4 10 SER A 477  ARG A 481  ALA A 497  ASN A 498                    
SITE     2 AC4 10 GLN A 500  PHE A 501  ASN A 569  ASP A 709                    
SITE     3 AC4 10 HOH A1032  XFJ B 805                                          
SITE     1 AC5  6 ARG A 596  ASP A 600   ZN A 901  SER B 686                    
SITE     2 AC5  6 HIS B 692  XFJ B 805                                          
SITE     1 AC6  4 CYS A 326  CYS A 331  CYS B 326  CYS B 331                    
SITE     1 AC7  5 ASP A 600   CL A 910  HOH A 920  HIS B 692                    
SITE     2 AC7  5 XFJ B 805                                                     
SITE     1 AC8 13 TRP A 676  PHE A 691  HIS A 692  GLN A 693                    
SITE     2 AC8 13 GLU A 694  HOH A1077  SER B 334  MET B 336                    
SITE     3 AC8 13 VAL B 677  TRP B 678  XFJ B 719  HEM B 750                    
SITE     4 AC8 13 HOH B 921                                                     
SITE     1 AC9  5 HIS A 692  ASP B 600  XFJ B 719   CL B 910                    
SITE     2 AC9  5 HOH B 920                                                     
SITE     1 BC1 12 SER A 334  MET A 336  VAL A 677  TRP A 678                    
SITE     2 BC1 12 HEM A 750  HOH A 921  TRP B 676  PHE B 691                    
SITE     3 BC1 12 HIS B 692  GLN B 693  XFJ B 805  HOH B1250                    
SITE     1 BC2 15 ARG A 596  ASP A 600  VAL A 677  TRP A 678                    
SITE     2 BC2 15 HEM A 750  MTL A 870   ZN A 901   CL A 910                    
SITE     3 BC2 15 HOH A 920  HOH A 921  TRP B 306  ASP B 309                    
SITE     4 BC2 15 PHE B 691  HIS B 692  H4B B 760                               
SITE     1 BC3 15 H4B A 760  TRP B 409  CYS B 415  SER B 457                    
SITE     2 BC3 15 PHE B 584  SER B 585  TRP B 587  GLU B 592                    
SITE     3 BC3 15 ARG B 596  TRP B 678  PHE B 704  XFJ B 719                    
SITE     4 BC3 15 XFJ B 800  HOH B1212  HOH B1329                               
SITE     1 BC4 11 ARG B 414  GLN B 478  VAL B 567  PHE B 584                    
SITE     2 BC4 11 TRP B 587  GLU B 592  ARG B 596  HEM B 750                    
SITE     3 BC4 11 MTL B 870  HOH B1277  HOH B1334                               
SITE     1 BC5 16 TRP A 306  ASP A 309  PHE A 691  HIS A 692                    
SITE     2 BC5 16  ZN A 719  H4B A 760  ARG B 596  ASP B 600                    
SITE     3 BC5 16 VAL B 677  TRP B 678  HEM B 750  MTL B 870                    
SITE     4 BC5 16  CL B 910  HOH B 920  HOH B 921  HOH B1199                    
SITE     1 BC6  6 TRP B 587  VAL B 649  HOH B1262  HOH B1263                    
SITE     2 BC6  6 HOH B1289  HOH B1335                                          
SITE     1 BC7 13 SER B 477  ARG B 481  ALA B 497  ASN B 498                    
SITE     2 BC7 13 GLN B 500  PHE B 501  ASN B 569  ASP B 709                    
SITE     3 BC7 13 XFJ B 719  XFJ B 800  HOH B1274  HOH B1307                    
SITE     4 BC7 13 HOH B1388                                                     
SITE     1 BC8  5 SER A 686   ZN A 719  ARG B 596  ASP B 600                    
SITE     2 BC8  5 XFJ B 719                                                     
CRYST1   51.806  110.386  164.119  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      0.019303  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009059  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006093        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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