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Database: PDB
Entry: 4D3J
LinkDB: 4D3J
Original site: 4D3J 
HEADER    OXIDOREDUCTASE                          22-OCT-14   4D3J              
TITLE     STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX WITH  
TITLE    2 6,6'-(2,2'-(5-AMINO-1,3-PHENYLENE)BIS(ETHANE-2,1-DIYL))BIS(4-        
TITLE    3 METHYLPYRIDIN-2-AMINE)                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NITRIC OXIDE SYNTHASE OXYGENASE;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: NOSOXY-LIKE PROTEIN;                                        
COMPND   5 EC: 1.14.13.165;                                                     
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PET28A                                     
KEYWDS    NITRIC OXIDE SYNTHASE, OXIDOREDUCTASE, INHIBITOR                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.K.HOLDEN,T.L.POULOS                                                 
REVDAT   4   06-FEB-19 4D3J    1       REMARK                                   
REVDAT   3   30-JAN-19 4D3J    1       REMARK                                   
REVDAT   2   04-FEB-15 4D3J    1       JRNL                                     
REVDAT   1   14-JAN-15 4D3J    0                                                
JRNL        AUTH   J.K.HOLDEN,S.KANG,S.A.HOLLINGSWORTH,H.LI,N.LIM,S.CHEN,       
JRNL        AUTH 2 H.HUANG,F.XUE,W.TANG,R.B.SILVERMAN,T.L.POULOS                
JRNL        TITL   STRUCTURE-BASED DESIGN OF BACTERIAL NITRIC OXIDE SYNTHASE    
JRNL        TITL 2 INHIBITORS.                                                  
JRNL        REF    J.MED.CHEM.                   V.  58   994 2015              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   25522110                                                     
JRNL        DOI    10.1021/JM501723P                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.67 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.67                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.11                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 56494                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.166                           
REMARK   3   R VALUE            (WORKING SET) : 0.165                           
REMARK   3   FREE R VALUE                     : 0.188                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2880                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 37.1185 -  4.6047    0.99     2736   145  0.1572 0.1829        
REMARK   3     2  4.6047 -  3.6559    1.00     2600   149  0.1302 0.1489        
REMARK   3     3  3.6559 -  3.1940    1.00     2626   135  0.1486 0.1670        
REMARK   3     4  3.1940 -  2.9021    1.00     2595   121  0.1513 0.1685        
REMARK   3     5  2.9021 -  2.6942    1.00     2577   137  0.1613 0.2055        
REMARK   3     6  2.6942 -  2.5354    1.00     2574   120  0.1516 0.1904        
REMARK   3     7  2.5354 -  2.4084    1.00     2529   162  0.1555 0.1795        
REMARK   3     8  2.4084 -  2.3036    1.00     2545   156  0.1561 0.1820        
REMARK   3     9  2.3036 -  2.2149    1.00     2523   153  0.1520 0.1671        
REMARK   3    10  2.2149 -  2.1385    1.00     2561   114  0.1587 0.1925        
REMARK   3    11  2.1385 -  2.0717    1.00     2523   128  0.1706 0.1908        
REMARK   3    12  2.0717 -  2.0124    1.00     2544   125  0.1737 0.1796        
REMARK   3    13  2.0124 -  1.9595    1.00     2537   138  0.1840 0.1930        
REMARK   3    14  1.9595 -  1.9117    1.00     2512   152  0.1976 0.2268        
REMARK   3    15  1.9117 -  1.8682    1.00     2527   143  0.2084 0.2642        
REMARK   3    16  1.8682 -  1.8284    1.00     2521   142  0.2450 0.2650        
REMARK   3    17  1.8284 -  1.7919    1.00     2484   145  0.2561 0.2900        
REMARK   3    18  1.7919 -  1.7581    1.00     2536   129  0.2893 0.2988        
REMARK   3    19  1.7581 -  1.7267    1.00     2548   115  0.3166 0.3083        
REMARK   3    20  1.7267 -  1.6974    1.00     2489   140  0.3452 0.3768        
REMARK   3    21  1.6974 -  1.6700    0.99     2527   131  0.3783 0.4416        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.400           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           3137                                  
REMARK   3   ANGLE     :  1.169           4257                                  
REMARK   3   CHIRALITY :  0.073            437                                  
REMARK   3   PLANARITY :  0.004            542                                  
REMARK   3   DIHEDRAL  : 14.820           1167                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   5.8666  19.5919  23.0208              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1373 T22:   0.1462                                     
REMARK   3      T33:   0.2115 T12:   0.0035                                     
REMARK   3      T13:   0.0066 T23:  -0.0479                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1352 L22:   1.5785                                     
REMARK   3      L33:   1.0513 L12:   0.1970                                     
REMARK   3      L13:   0.2000 L23:  -0.3596                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0332 S12:   0.1662 S13:  -0.0045                       
REMARK   3      S21:  -0.1760 S22:   0.0407 S23:   0.0043                       
REMARK   3      S31:  -0.0488 S32:   0.0365 S33:  -0.0075                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4D3J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-OCT-14.                  
REMARK 100 THE DEPOSITION ID IS D_1290062011.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-DEC-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56580                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.670                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.110                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.04000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.7400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.67                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 37.11                    
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.12000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 4LWA                                       
REMARK 200                                                                      
REMARK 200 REMARK: CC ONE HALF FOR FULL DATA SET AT 0.999 CC ONE HALF FOR       
REMARK 200  HIGH RESOLUTION SHELL AT 0.591                                      
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 60 MM BIS-TRIS METHANE, 40 MM CITRIC     
REMARK 280  ACID, 20% PEG3350, 1.9% 1-PROPANOL, PH 7.6, VAPOR DIFFUSION,        
REMARK 280  HANGING DROP, TEMPERATURE 298K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       40.31150            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.50400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.31150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.50400            
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: 8570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.1 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A2314  LIES ON A SPECIAL POSITION.                          
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     MET A     1                                                      
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    ALA A 233       70.88   -160.86                                   
REMARK 500    ARG A 247      -68.61   -121.71                                   
REMARK 500    ARG A 254     -128.28   -118.79                                   
REMARK 500    ASN A 348       31.82    -88.77                                   
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                             HEM A 901  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  66   SG                                                     
REMARK 620 2 HEM A 901   NA   99.5                                              
REMARK 620 3 HEM A 901   NB   94.6  87.1                                        
REMARK 620 4 HEM A 901   NC   93.9 166.4  89.1                                  
REMARK 620 5 HEM A 901   ND  101.2  88.2 164.1  92.0                            
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 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 903                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XFN A 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 907                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 908                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 909                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 910                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 912                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE POL A 913                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4D3I   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX      
REMARK 900 WITH 6,6'-((5-(AMINOMETHYL)-1,3-PHENYLENE) BIS(ETHANE-2,1-DIYL))     
REMARK 900 BIS(4-METHYLPYRIDIN-2-AMINE)                                         
REMARK 900 RELATED ID: 4D3K   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX      
REMARK 900 WITH 6,6'-((5-(3-AMINOPROPYL)-1,3- PHENYLENE)BIS(ETHANE-2,1-DIYL))   
REMARK 900 BIS(4-METHYLPYRIDIN-2 -AMINE)                                        
REMARK 900 RELATED ID: 4D3M   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX      
REMARK 900 WITH 3-(2-(6-AMINO-4-METHYLPYRIDIN-2-YL) ETHYL)-5-(2-(4-METHYL-6-    
REMARK 900 (METHYLAMINO)PYRIDIN-2-YL) ETHYL)BENZONITRILE                        
REMARK 900 RELATED ID: 4D3N   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX      
REMARK 900 WITH 3-(2-(6-AMINO-4-METHYLPYRIDIN-2-YL) ETHYL)-5-((2-(PYRIDIN-2-YL) 
REMARK 900 ETHYL)AMINO)BENZONITRILE                                             
REMARK 900 RELATED ID: 4D3O   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX      
REMARK 900 WITH 6-(3-(2-(1H-PYRROLO(2,3-B)PYRIDIN- 6-YL)ETHYL)-5-(AMINOMETHYL)  
REMARK 900 PHENETHYL)-4-METHYLPYRIDIN- 2-AMINE                                  
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 MUTATIONS E25A, E26A AND E316A INTRODUCED                            
DBREF  4D3J A    1   363  UNP    O34453   NOSO_BACSU       1    363             
SEQADV 4D3J ALA A   25  UNP  O34453    GLU    25 ENGINEERED MUTATION            
SEQADV 4D3J ALA A   26  UNP  O34453    GLU    26 ENGINEERED MUTATION            
SEQADV 4D3J ALA A  316  UNP  O34453    GLU   316 ENGINEERED MUTATION            
SEQRES   1 A  363  MET GLU GLU LYS GLU ILE LEU TRP ASN GLU ALA LYS ALA          
SEQRES   2 A  363  PHE ILE ALA ALA CYS TYR GLN GLU LEU GLY LYS ALA ALA          
SEQRES   3 A  363  GLU VAL LYS ASP ARG LEU ALA ASP ILE LYS SER GLU ILE          
SEQRES   4 A  363  ASP LEU THR GLY SER TYR VAL HIS THR LYS GLU GLU LEU          
SEQRES   5 A  363  GLU HIS GLY ALA LYS MET ALA TRP ARG ASN SER ASN ARG          
SEQRES   6 A  363  CYS ILE GLY ARG LEU PHE TRP ASN SER LEU ASN VAL ILE          
SEQRES   7 A  363  ASP ARG ARG ASP VAL ARG THR LYS GLU GLU VAL ARG ASP          
SEQRES   8 A  363  ALA LEU PHE HIS HIS ILE GLU THR ALA THR ASN ASN GLY          
SEQRES   9 A  363  LYS ILE ARG PRO THR ILE THR ILE PHE PRO PRO GLU GLU          
SEQRES  10 A  363  LYS GLY GLU LYS GLN VAL GLU ILE TRP ASN HIS GLN LEU          
SEQRES  11 A  363  ILE ARG TYR ALA GLY TYR GLU SER ASP GLY GLU ARG ILE          
SEQRES  12 A  363  GLY ASP PRO ALA SER CYS SER LEU THR ALA ALA CYS GLU          
SEQRES  13 A  363  GLU LEU GLY TRP ARG GLY GLU ARG THR ASP PHE ASP LEU          
SEQRES  14 A  363  LEU PRO LEU ILE PHE ARG MET LYS GLY ASP GLU GLN PRO          
SEQRES  15 A  363  VAL TRP TYR GLU LEU PRO ARG SER LEU VAL ILE GLU VAL          
SEQRES  16 A  363  PRO ILE THR HIS PRO ASP ILE GLU ALA PHE SER ASP LEU          
SEQRES  17 A  363  GLU LEU LYS TRP TYR GLY VAL PRO ILE ILE SER ASP MET          
SEQRES  18 A  363  LYS LEU GLU VAL GLY GLY ILE HIS TYR ASN ALA ALA PRO          
SEQRES  19 A  363  PHE ASN GLY TRP TYR MET GLY THR GLU ILE GLY ALA ARG          
SEQRES  20 A  363  ASN LEU ALA ASP GLU LYS ARG TYR ASP LYS LEU LYS LYS          
SEQRES  21 A  363  VAL ALA SER VAL ILE GLY ILE ALA ALA ASP TYR ASN THR          
SEQRES  22 A  363  ASP LEU TRP LYS ASP GLN ALA LEU VAL GLU LEU ASN LYS          
SEQRES  23 A  363  ALA VAL LEU HIS SER TYR LYS LYS GLN GLY VAL SER ILE          
SEQRES  24 A  363  VAL ASP HIS HIS THR ALA ALA SER GLN PHE LYS ARG PHE          
SEQRES  25 A  363  GLU GLU GLN ALA GLU GLU ALA GLY ARG LYS LEU THR GLY          
SEQRES  26 A  363  ASP TRP THR TRP LEU ILE PRO PRO ILE SER PRO ALA ALA          
SEQRES  27 A  363  THR HIS ILE PHE HIS ARG SER TYR ASP ASN SER ILE VAL          
SEQRES  28 A  363  LYS PRO ASN TYR PHE TYR GLN ASP LYS PRO TYR GLU              
HET    HEM  A 901      43                                                       
HET     CL  A 903       1                                                       
HET    XFN  A 904      27                                                       
HET    GOL  A 907       6                                                       
HET    GOL  A 908       6                                                       
HET    GOL  A 909       6                                                       
HET    GOL  A 910       6                                                       
HET    PEG  A 912       7                                                       
HET    POL  A 913       4                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM      CL CHLORIDE ION                                                     
HETNAM     XFN 6,6'-[(5-AMINOBENZENE-1,3-DIYL)DIETHANE-2,1-DIYL]BIS(4-          
HETNAM   2 XFN  METHYLPYRIDIN-2-AMINE)                                          
HETNAM     GOL GLYCEROL                                                         
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     POL N-PROPANOL                                                       
HETSYN     HEM HEME                                                             
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     POL 1-PROPONOL                                                       
FORMUL   2  HEM    C34 H32 FE N4 O4                                             
FORMUL   3   CL    CL 1-                                                        
FORMUL   4  XFN    C22 H27 N5                                                   
FORMUL   5  GOL    4(C3 H8 O3)                                                  
FORMUL   9  PEG    C4 H10 O3                                                    
FORMUL  10  POL    C3 H8 O                                                      
FORMUL  11  HOH   *342(H2 O)                                                    
HELIX    1   1 GLU A    2  LEU A   22  1                                  21    
HELIX    2   2 LYS A   24  ALA A   26  5                                   3    
HELIX    3   3 GLU A   27  GLY A   43  1                                  17    
HELIX    4   4 THR A   48  ASN A   62  1                                  15    
HELIX    5   5 GLY A   68  LEU A   75  5                                   8    
HELIX    6   6 THR A   85  ASN A  102  1                                  18    
HELIX    7   7 ASN A  103  LYS A  105  5                                   3    
HELIX    8   8 SER A  148  GLU A  157  1                                  10    
HELIX    9   9 PRO A  188  VAL A  192  5                                   5    
HELIX   10  10 ILE A  202  GLU A  209  5                                   8    
HELIX   11  11 GLY A  241  ALA A  246  1                                   6    
HELIX   12  12 LYS A  257  ILE A  265  1                                   9    
HELIX   13  13 TYR A  271  ASP A  274  5                                   4    
HELIX   14  14 LEU A  275  GLY A  296  1                                  22    
HELIX   15  15 ASP A  301  GLY A  320  1                                  20    
HELIX   16  16 ASP A  326  ILE A  331  1                                   6    
HELIX   17  17 SER A  335  THR A  339  5                                   5    
HELIX   18  18 HIS A  340  ARG A  344  5                                   5    
SHEET    1  AA 4 ASN A  76  ASP A  79  0                                        
SHEET    2  AA 4 THR A 109  ILE A 112  1  O  ILE A 110   N  ILE A  78           
SHEET    3  AA 4 PHE A 235  ASN A 236 -1  O  ASN A 236   N  THR A 109           
SHEET    4  AA 4 ILE A 217  ILE A 218 -1  O  ILE A 218   N  PHE A 235           
SHEET    1  AB 3 VAL A 123  ILE A 125  0                                        
SHEET    2  AB 3 LEU A 172  MET A 176 -1  O  ARG A 175   N  GLU A 124           
SHEET    3  AB 3 VAL A 183  TYR A 185 -1  O  VAL A 183   N  PHE A 174           
SHEET    1  AC 2 GLY A 135  SER A 138  0                                        
SHEET    2  AC 2 GLU A 141  GLY A 144 -1  O  GLU A 141   N  SER A 138           
SHEET    1  AD 2 GLU A 194  PRO A 196  0                                        
SHEET    2  AD 2 LYS A 211  TYR A 213 -1  O  TRP A 212   N  VAL A 195           
SHEET    1  AE 3 ILE A 228  TYR A 230  0                                        
SHEET    2  AE 3 LYS A 222  VAL A 225 -1  O  LEU A 223   N  TYR A 230           
SHEET    3  AE 3 ASN A 354  PHE A 356 -1  O  ASN A 354   N  GLU A 224           
SHEET    1  AF 2 TYR A 239  MET A 240  0                                        
SHEET    2  AF 2 ILE A 299  VAL A 300  1  N  VAL A 300   O  TYR A 239           
LINK         SG  CYS A  66                FE   HEM A 901     1555   1555  2.48  
CISPEP   1 LYS A  352    PRO A  353          0        -1.60                     
SITE     1 AC1 15 TRP A  60  ARG A  65  CYS A  66  PHE A 235                    
SITE     2 AC1 15 ASN A 236  TRP A 238  GLU A 243  ARG A 247                    
SITE     3 AC1 15 TRP A 329  TYR A 355  TYR A 357  XFN A 904                    
SITE     4 AC1 15 HOH A2048  HOH A2339  HOH A2340                               
SITE     1 AC2  5 GLN A 129  TYR A 239  ARG A 247  ASN A 248                    
SITE     2 AC2  5 HOH A2136                                                     
SITE     1 AC3 11 HIS A 128  ARG A 132  PHE A 235  TRP A 238                    
SITE     2 AC3 11 GLU A 243  ARG A 247  TRP A 329  HEM A 901                    
SITE     3 AC3 11 GOL A 909  POL A 913  HOH A2136                               
SITE     1 AC4  9 GLU A 156  TRP A 160  ARG A 161  TRP A 238                    
SITE     2 AC4  9 SER A 298  ILE A 299  HOH A2161  HOH A2165                    
SITE     3 AC4  9 HOH A2284                                                     
SITE     1 AC5  6 VAL A 183  TRP A 184  TYR A 271  ASN A 272                    
SITE     2 AC5  6 HOH A2261  HOH A2341                                          
SITE     1 AC6  6 TRP A 327  THR A 328  PHE A 342  ARG A 344                    
SITE     2 AC6  6 XFN A 904  HOH A2051                                          
SITE     1 AC7  6 ARG A 142  ASP A 166  ARG A 254  TYR A 255                    
SITE     2 AC7  6 LYS A 257  HOH A2149                                          
SITE     1 AC8  8 ALA A 250  ASP A 251  GLU A 252  ALA A 337                    
SITE     2 AC8  8 ALA A 338  HOH A2237  HOH A2316  HOH A2318                    
SITE     1 AC9  5 ARG A 132  ALA A 147  XFN A 904  HOH A2338                    
SITE     2 AC9  5 HOH A2342                                                     
CRYST1   80.623   95.008   62.766  90.00  90.00  90.00 P 21 21 2     4          
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      0.012403  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010525  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015932        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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