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Database: PDB
Entry: 5G6K
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Original site: 5G6K 
HEADER    OXIDOREDUCTASE                          18-JUN-16   5G6K              
TITLE     STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE I218V IN COMPLEX 
TITLE    2 WITH 7-((3-(2-(METHYLAMINO)ETHYL)PHENOXY)METHYL)QUINOLIN-2- AMINE    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NITRIC OXIDE SYNTHASE OXYGENASE;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: NOSOXY-LIKE PROTEIN, NITRIC OXIDE SYNTHASE;                 
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: 224308;                                              
SOURCE   4 STRAIN: 168;                                                         
SOURCE   5 ATCC: 23857;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PET28A                                     
KEYWDS    NITRIC OXIDE SYNTHASE, OXIDOREDUCTASE, INHIBITOR                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.K.HOLDEN,M.C.LEWIS,T.L.POULOS                                       
REVDAT   4   06-FEB-19 5G6K    1       JRNL   REMARK                            
REVDAT   3   30-JAN-19 5G6K    1       REMARK                                   
REVDAT   2   19-OCT-16 5G6K    1       JRNL                                     
REVDAT   1   21-SEP-16 5G6K    0                                                
JRNL        AUTH   J.K.HOLDEN,M.C.LEWIS,M.A.CINELLI,Z.ABDULLATIF,A.V.PENSA,     
JRNL        AUTH 2 R.B.SILVERMAN,T.L.POULOS                                     
JRNL        TITL   TARGETING BACTERIAL NITRIC OXIDE SYNTHASE WITH               
JRNL        TITL 2 AMINOQUINOLINE-BASED INHIBITORS.                             
JRNL        REF    BIOCHEMISTRY                  V.  55  5587 2016              
JRNL        REFN                   ISSN 1520-4995                               
JRNL        PMID   27607918                                                     
JRNL        DOI    10.1021/ACS.BIOCHEM.6B00786                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 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) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.77                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 74.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 26521                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.216                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1351                            
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 37.7775 -  4.2008    0.99     3533   205  0.1354 0.1738        
REMARK   3     2  4.2008 -  3.3350    1.00     3430   167  0.1460 0.1974        
REMARK   3     3  3.3350 -  2.9136    1.00     3386   172  0.1795 0.2504        
REMARK   3     4  2.9136 -  2.6473    1.00     3387   160  0.2097 0.2629        
REMARK   3     5  2.6473 -  2.4576    0.92     3102   179  0.1992 0.2383        
REMARK   3     6  2.4576 -  2.3127    0.78     2543   155  0.2052 0.2501        
REMARK   3     7  2.3127 -  2.1969    0.63     2114   140  0.2301 0.2680        
REMARK   3     8  2.1969 -  2.1013    0.52     1726    70  0.2209 0.2423        
REMARK   3     9  2.1013 -  2.0204    0.38     1245    67  0.2354 0.2746        
REMARK   3    10  2.0204 -  1.9507    0.21      704    36  0.2183 0.2885        
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)     : 0.200            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.160           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.19                          
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      :  0.014           3114                                  
REMARK   3   ANGLE     :  1.578           4235                                  
REMARK   3   CHIRALITY :  0.099            435                                  
REMARK   3   PLANARITY :  0.006            540                                  
REMARK   3   DIHEDRAL  : 14.518           1153                                  
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):   5.6328  19.7238  22.5678              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1596 T22:   0.1530                                     
REMARK   3      T33:   0.1402 T12:  -0.0087                                     
REMARK   3      T13:   0.0216 T23:  -0.0385                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4572 L22:   2.0211                                     
REMARK   3      L33:   1.2042 L12:   0.0489                                     
REMARK   3      L13:   0.1518 L23:  -0.6455                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0244 S12:   0.2012 S13:   0.1438                       
REMARK   3      S21:  -0.2211 S22:   0.0728 S23:  -0.0249                       
REMARK   3      S31:  -0.1007 S32:   0.0856 S33:  -0.0387                       
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 5G6K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-JUN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1290066968.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-15                          
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                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.18076                            
REMARK 200  MONOCHROMATOR                  : NULL                               
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   : 35577                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.770                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.6000                             
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) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.43000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.800                              
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 HIGH RESOLUTION SHELL AT 0.515. DATASET      
REMARK 200  HAD STRONG ANISOTROPY AND WAS FURTHER SCALED USING THE              
REMARK 200  DIFFRACTION ANISOTROPY SERVER.                                      
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85                     
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       40.29500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.53000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.29500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.53000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6990 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.4 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 A2225  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    ARG A  80       40.43   -109.74                                   
REMARK 500    GLU A 117      -81.08    -91.45                                   
REMARK 500    ASP A 201       -2.04   -144.72                                   
REMARK 500    ALA A 233       69.44   -158.23                                   
REMARK 500    ARG A 247      -66.06   -126.47                                   
REMARK 500    ARG A 254     -125.14   -113.79                                   
REMARK 500    ALA A 269       50.21   -118.57                                   
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   99.0                                              
REMARK 620 3 HEM A 901   NB   92.4  87.6                                        
REMARK 620 4 HEM A 901   NC   93.4 166.7  87.2                                  
REMARK 620 5 HEM A 901   ND  101.7  89.3 165.9  92.8                            
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 H4B A 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 903                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE M94 A 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 905                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5G65   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX      
REMARK 900 WITH QUINOLIN-2-AMINE                                                
REMARK 900 RELATED ID: 5G66   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX      
REMARK 900 WITH 4-METHYLQUINOLIN-2-AMINE                                        
REMARK 900 RELATED ID: 5G67   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX      
REMARK 900 WITH 7-((3-FLUOROPHENETHYLAMINO)METHYL)QUINOLIN -2-AMINE             
REMARK 900 RELATED ID: 5G68   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX      
REMARK 900 WITH 7-(2-(3-(3-FLUOROPHENYL(PROPYLAMINO) METHYL))QUINOLIN-2- AMINE  
REMARK 900 RELATED ID: 5G69   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX      
REMARK 900 WITH 7-(2-(3-FLUOROBENZYLAMINO)ETHYL)QUINOLIN -2-AMINE               
REMARK 900 RELATED ID: 5G6A   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX      
REMARK 900 WITH 7-((3-FLUOROPHENETHYLAMINO)ETHYL)QUINOLIN- 2-AMINE              
REMARK 900 RELATED ID: 5G6B   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX      
REMARK 900 WITH TWO MOLECULES OF 7-((3- FLUOROPHENETHYLAMINO)ETHYL)QUINOLIN-2-  
REMARK 900 AMINE                                                                
REMARK 900 RELATED ID: 5G6C   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE I218V IN        
REMARK 900 COMPLEX WITH 7-((3-FLUOROPHENETHYLAMINO)ETHYL) QUINOLIN-2-AMINE      
REMARK 900 RELATED ID: 5G6D   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX      
REMARK 900 WITH 7-(((3-(DIMETHYLAMINO)BENZYL)AMINO)METHYL )QUINOLIN-2-AMINE     
REMARK 900 RELATED ID: 5G6E   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX      
REMARK 900 WITH 7-(((3-(PYRIDIN-3-YL)PROPYL)AMINO) METHYL)QUINOLIN-2-AMINE      
REMARK 900 RELATED ID: 5G6F   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX      
REMARK 900 WITH 7-(((3-((DIMETHYLAMINO)METHYL)PHENYL) AMINO)METHYL) QUINOLIN-2- 
REMARK 900 AMINE                                                                
REMARK 900 RELATED ID: 5G6G   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX      
REMARK 900 WITH 7-((2-((METHYLAMINO)METHYL)PHENOXY)METHYL )QUINOLIN-2-AMINE     
REMARK 900 RELATED ID: 5G6H   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX      
REMARK 900 WITH 7-((3-(METHYLAMINO)METHYL)PHENOXY)METHYL )QUINOLIN-2-AMINE      
REMARK 900 RELATED ID: 5G6I   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE I218V IN        
REMARK 900 COMPLEX WITH 7-((3-(METHYLAMINO)METHYL) PHENOXY)METHYL)QUINOLIN-2-   
REMARK 900 AMINE                                                                
REMARK 900 RELATED ID: 5G6J   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX      
REMARK 900 WITH 7-((3-(2-(METHYLAMINO)ETHYL)PHENOXY) METHYL)QUINOLIN-2- AMINE   
REMARK 900 RELATED ID: 5G6L   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX      
REMARK 900 WITH 7-((4-CHLORO-3-((METHYLAMINO)METHYL) PHENOXY)METHYL) QUINOLIN-  
REMARK 900 2-AMINE                                                              
REMARK 900 RELATED ID: 5G6M   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX      
REMARK 900 WITH 7-((3-AMINOMETHYL)PHENOXY)METHYL)QUINOLIN -2-AMINE              
REMARK 900 RELATED ID: 5G6N   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX      
REMARK 900 WITH 7-((4-(DIMETHYLAMINO)METHYL)PHENOXY) METHYL)QUINOLIN-2- AMINE   
REMARK 900 RELATED ID: 5G6O   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX      
REMARK 900 WITH TWO MOLECULES OF 7-((4-(DIMETHYLAMINO) METHYL)PHENOXY)METHYL)   
REMARK 900 QUINOLIN-2- AMINE                                                    
REMARK 900 RELATED ID: 5G6P   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE I218V IN        
REMARK 900 COMPLEX WITH 7-((4-(DIMETHYLAMINO)METHYL) PHENOXY)METHYL)QUINOLIN-2- 
REMARK 900 AMINE                                                                
REMARK 900 RELATED ID: 5G6Q   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX      
REMARK 900 WITH 7-(((5-((METHYLAMINO)METHYL)PYRIDIN-3- YL)OXY)METHYL) QUINOLIN- 
REMARK 900 2-AMINE                                                              
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 MUTANT I218V INTRODUCED. SURFACE ENTROPY MUTATIONS E25A,             
REMARK 999 E26A AND E316A.                                                      
DBREF  5G6K A    1   363  UNP    O34453   NOSO_BACSU       1    363             
SEQADV 5G6K ALA A   25  UNP  O34453    GLU    25 ENGINEERED MUTATION            
SEQADV 5G6K ALA A   26  UNP  O34453    GLU    26 ENGINEERED MUTATION            
SEQADV 5G6K VAL A  218  UNP  O34453    ILE   218 ENGINEERED MUTATION            
SEQADV 5G6K 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 VAL 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    H4B  A 902      17                                                       
HET     CL  A 903       1                                                       
HET    M94  A 904      23                                                       
HET    GOL  A 905       6                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     H4B 5,6,7,8-TETRAHYDROBIOPTERIN                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     M94 7-[[3-[2-(METHYLAMINO)ETHYL]PHENOXY]METHYL]QUINOLIN-2-           
HETNAM   2 M94  AMINE                                                           
HETNAM     GOL GLYCEROL                                                         
HETSYN     HEM HEME                                                             
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  HEM    C34 H32 FE N4 O4                                             
FORMUL   3  H4B    C9 H15 N5 O3                                                 
FORMUL   4   CL    CL 1-                                                        
FORMUL   5  M94    C19 H21 N3 O                                                 
FORMUL   6  GOL    C3 H8 O3                                                     
FORMUL   7  HOH   *241(H2 O)                                                    
HELIX    1   1 GLU A    3  LEU A   22  1                                  20    
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  LEU A  158  1                                  11    
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  ALA A  319  1                                  19    
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  VAL A 218 -1  O  VAL 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  2.49  
CISPEP   1 LYS A  352    PRO A  353          0         2.15                     
SITE     1 AC1 18 TRP A  60  SER A  63  ARG A  65  CYS A  66                    
SITE     2 AC1 18 ILE A  67  PHE A 235  ASN A 236  GLY A 237                    
SITE     3 AC1 18 TRP A 238  GLU A 243  TRP A 329  TYR A 355                    
SITE     4 AC1 18 TYR A 357  H4B A 902  M94 A 904  HOH A2223                    
SITE     5 AC1 18 HOH A2239  HOH A2240                                          
SITE     1 AC2 12 ARG A 247  TRP A 327  THR A 328  PHE A 342                    
SITE     2 AC2 12 HIS A 343  ARG A 344  SER A 345  HEM A 901                    
SITE     3 AC2 12 M94 A 904  HOH A2034  HOH A2223  HOH A2241                    
SITE     1 AC3  4 GLN A 129  ARG A 132  TYR A 239  ASN A 248                    
SITE     1 AC4  9 HIS A 128  VAL A 218  PHE A 235  TRP A 238                    
SITE     2 AC4  9 GLU A 243  TRP A 329  HEM A 901  H4B A 902                    
SITE     3 AC4  9 HOH A2045                                                     
SITE     1 AC5  7 GLY A 159  TRP A 160  ARG A 161  TRP A 238                    
SITE     2 AC5  7 SER A 298  ILE A 299  GLN A 308                               
CRYST1   80.590   95.060   62.220  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      0.012408  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010520  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016072        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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