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Database: PDB
Entry: 4LWB
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HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 26-JUL-13   4LWB              
TITLE     STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX WITH  
TITLE    2 6-((((3R,5S)-5-(((6-AMINO-4-METHYLPYRIDIN-2-YL)METHOXY)METHYL)       
TITLE    3 PYRROLIDIN-3-YL)OXY)METHYL)-4-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 SUBSP. SUBTILIS;              
SOURCE   3 ORGANISM_TAXID: 224308;                                              
SOURCE   4 STRAIN: 168;                                                         
SOURCE   5 GENE: BSU07630, NOS, YFLM;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    NITRIC OXIDE SYNTHASE, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR        
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.K.HOLDEN,H.LI,T.L.POULOS                                            
REVDAT   5   15-NOV-17 4LWB    1       REMARK                                   
REVDAT   4   20-NOV-13 4LWB    1       JRNL                                     
REVDAT   3   06-NOV-13 4LWB    1       JRNL                                     
REVDAT   2   30-OCT-13 4LWB    1       JRNL                                     
REVDAT   1   23-OCT-13 4LWB    0                                                
JRNL        AUTH   J.K.HOLDEN,H.LI,Q.JING,S.KANG,J.RICHO,R.B.SILVERMAN,         
JRNL        AUTH 2 T.L.POULOS                                                   
JRNL        TITL   STRUCTURAL AND BIOLOGICAL STUDIES ON BACTERIAL NITRIC OXIDE  
JRNL        TITL 2 SYNTHASE INHIBITORS.                                         
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 110 18127 2013              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   24145412                                                     
JRNL        DOI    10.1073/PNAS.1314080110                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 26684                          
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) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.233                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1829                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.36                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3000                       
REMARK   3   BIN FREE R VALUE SET COUNT          : NULL                         
REMARK   3   BIN FREE R VALUE                    : 0.3323                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2941                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 105                                     
REMARK   3   SOLVENT ATOMS            : 187                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.94                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.43                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.23000                                              
REMARK   3    B22 (A**2) : -5.94000                                             
REMARK   3    B33 (A**2) : 5.71000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.208         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.182         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.144         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.968        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3137 ; 0.015 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2915 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4264 ; 2.185 ; 1.981       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6709 ; 0.818 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   362 ; 6.699 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   154 ;34.228 ;24.026       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   522 ;15.162 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;17.654 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   438 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3527 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   751 ; 0.005 ; 0.020       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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  : 1                                          
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     2        A   363                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.6370 -20.2600 -22.2820              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1060 T22:   0.1391                                     
REMARK   3      T33:   0.0085 T12:   0.0174                                     
REMARK   3      T13:  -0.0187 T23:  -0.0040                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9576 L22:   1.8791                                     
REMARK   3      L33:   0.8520 L12:  -0.1549                                     
REMARK   3      L13:  -0.1379 L23:  -0.4227                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0469 S12:  -0.1615 S13:  -0.0441                       
REMARK   3      S21:   0.2117 S22:   0.0423 S23:  -0.0803                       
REMARK   3      S31:   0.0955 S32:   0.0739 S33:   0.0046                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4LWB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-AUG-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000081166.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JUL-12                          
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                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97946                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26684                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.13300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.19                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.13300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2FBZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86                     
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       40.13500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.53900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.13500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.53900            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: MONOMERIC                         
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 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 A1174  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    LYS A  24       33.05    -99.67                                   
REMARK 500    GLU A 117      -75.81   -102.46                                   
REMARK 500    LYS A 118       40.95   -106.17                                   
REMARK 500    ASP A 139       72.90     35.13                                   
REMARK 500    ALA A 233       61.90   -159.95                                   
REMARK 500    ARG A 247      -63.28   -125.36                                   
REMARK 500    ARG A 254     -127.32   -114.06                                   
REMARK 500    ASN A 348       33.23    -83.10                                   
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  106.8                                              
REMARK 620 3 HEM A 901   NB   93.7  85.7                                        
REMARK 620 4 HEM A 901   NC  101.6 151.5  90.1                                  
REMARK 620 5 HEM A 901   ND  104.6  86.5 161.5  88.8                            
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 QJ8 A 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B A 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL 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 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 906                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 907                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4LUW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4LUX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4LWA   RELATED DB: PDB                                   
DBREF  4LWB A    1   363  UNP    O34453   NOSO_BACSU       1    363             
SEQADV 4LWB ALA A   25  UNP  O34453    GLU    25 ENGINEERED MUTATION            
SEQADV 4LWB ALA A   26  UNP  O34453    GLU    26 ENGINEERED MUTATION            
SEQADV 4LWB 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    QJ8  A 902      26                                                       
HET    H4B  A 903      17                                                       
HET     CL  A 904       1                                                       
HET    GOL  A 905       6                                                       
HET    GOL  A 906       6                                                       
HET    GOL  A 907       6                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     QJ8 6-({[(3R,5S)-5-{[(6-AMINO-4-METHYLPYRIDIN-2-YL)                  
HETNAM   2 QJ8  METHOXY]METHYL}PYRROLIDIN-3-YL]OXY}METHYL)-4-                   
HETNAM   3 QJ8  METHYLPYRIDIN-2-AMINE                                           
HETNAM     H4B 5,6,7,8-TETRAHYDROBIOPTERIN                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETSYN     HEM HEME                                                             
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  HEM    C34 H32 FE N4 O4                                             
FORMUL   3  QJ8    C19 H27 N5 O2                                                
FORMUL   4  H4B    C9 H15 N5 O3                                                 
FORMUL   5   CL    CL 1-                                                        
FORMUL   6  GOL    3(C3 H8 O3)                                                  
FORMUL   9  HOH   *187(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  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  GLN A  295  1                                  21    
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  ARG A  344  5                                  10    
SHEET    1   A 4 ASN A  76  ASP A  79  0                                        
SHEET    2   A 4 THR A 109  ILE A 112  1  O  ILE A 110   N  ILE A  78           
SHEET    3   A 4 PHE A 235  ASN A 236 -1  O  ASN A 236   N  THR A 109           
SHEET    4   A 4 ILE A 217  ILE A 218 -1  N  ILE A 218   O  PHE A 235           
SHEET    1   B 3 VAL A 123  ILE A 125  0                                        
SHEET    2   B 3 LEU A 172  MET A 176 -1  O  ARG A 175   N  GLU A 124           
SHEET    3   B 3 VAL A 183  TYR A 185 -1  O  VAL A 183   N  PHE A 174           
SHEET    1   C 2 GLY A 135  SER A 138  0                                        
SHEET    2   C 2 GLU A 141  GLY A 144 -1  O  ILE A 143   N  TYR A 136           
SHEET    1   D 2 GLU A 194  PRO A 196  0                                        
SHEET    2   D 2 LYS A 211  TYR A 213 -1  O  TRP A 212   N  VAL A 195           
SHEET    1   E 3 ILE A 228  TYR A 230  0                                        
SHEET    2   E 3 MET A 221  VAL A 225 -1  N  LEU A 223   O  TYR A 230           
SHEET    3   E 3 ASN A 354  TYR A 357 -1  O  ASN A 354   N  GLU A 224           
SHEET    1   F 2 TYR A 239  MET A 240  0                                        
SHEET    2   F 2 ILE A 299  VAL A 300  1  O  VAL A 300   N  TYR A 239           
LINK         SG  CYS A  66                FE   HEM A 901     1555   1555  2.30  
CISPEP   1 LYS A  352    PRO A  353          0         0.28                     
SITE     1 AC1 16 TRP A  60  ARG A  65  CYS A  66  PHE A 235                    
SITE     2 AC1 16 ASN A 236  GLY A 237  TRP A 238  GLU A 243                    
SITE     3 AC1 16 TRP A 329  TYR A 355  TYR A 357  QJ8 A 902                    
SITE     4 AC1 16 H4B A 903  HOH A1003  HOH A1094  HOH A1164                    
SITE     1 AC2  9 HIS A 128  ILE A 218  ASP A 220  PHE A 235                    
SITE     2 AC2  9 TRP A 238  GLU A 243  TYR A 357  HEM A 901                    
SITE     3 AC2  9 HOH A1181                                                     
SITE     1 AC3  9 ARG A 247  TRP A 327  THR A 328  TRP A 329                    
SITE     2 AC3  9 PHE A 342  HIS A 343  HEM A 901  HOH A1115                    
SITE     3 AC3  9 HOH A1138                                                     
SITE     1 AC4  5 GLN A 129  ARG A 132  TYR A 239  ASN A 248                    
SITE     2 AC4  5 HOH A1046                                                     
SITE     1 AC5  7 GLU A 156  TRP A 160  ARG A 161  TRP A 238                    
SITE     2 AC5  7 SER A 298  ILE A 299  HOH A1127                               
SITE     1 AC6  6 ARG A 142  GLY A 144  ARG A 254  TYR A 255                    
SITE     2 AC6  6 LYS A 257  HOH A1122                                          
SITE     1 AC7  5 VAL A 183  TRP A 184  ASP A 270  ASN A 272                    
SITE     2 AC7  5 HOH A1179                                                     
CRYST1   80.270   95.078   62.739  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      0.012458  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010518  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015939        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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