GenomeNet

Database: PDB
Entry: 4M89
LinkDB: 4M89
Original site: 4M89 
HEADER    OXIDOREDUCTASE/ANTIBIOTIC               13-AUG-13   4M89              
TITLE     CRYSTAL STRUCTURE OF ENOYL-ACYL CARRIER PROTEIN REDUCTASE (FABI) FROM 
TITLE    2 NEISSERIA MENINGITIDIS IN COMPLEX WITH NAD+ AND TRICLOSAN            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH];             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.3.1.9;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS;                         
SOURCE   3 ORGANISM_TAXID: 272831;                                              
SOURCE   4 STRAIN: FAM18;                                                       
SOURCE   5 GENE: FABI, NMC1834;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ENOYL, ACYL CARRIER PROTEIN, ACP, NEISSERIA, INHIBITOR, ROSSMANN      
KEYWDS   2 FOLD, REDUCTASE, NAD, TRICLOSAN, OXIDOREDUCTASE-ANTIBIOTIC COMPLEX   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.D.NANSON,J.K.FORWOOD                                                
REVDAT   1   02-OCT-13 4M89    0                                                
JRNL        AUTH   J.D.NANSON,J.K.FORWOOD                                       
JRNL        TITL   CRYSTAL STRUCTURE OF ENOYL-ACYL CARRIER PROTEIN REDUCTASE    
JRNL        TITL 2 (FABI) FROM NEISSERIA MENINGITIDIS IN COMPLEX WITH NAD+ AND  
JRNL        TITL 3 TRICLOSAN                                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.06                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 44797                          
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) : 0.168                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.186                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2383                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3203                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.91                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1930                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 195                          
REMARK   3   BIN FREE R VALUE                    : 0.2000                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3828                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 122                                     
REMARK   3   SOLVENT ATOMS            : 314                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.93                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : -0.00000                                             
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): 0.128         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.112         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.064         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.784         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4060 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3882 ; 0.004 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5500 ; 1.498 ; 2.000       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8906 ; 1.008 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   520 ; 5.683 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   162 ;30.283 ;23.333       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   666 ;12.871 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;16.560 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   618 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4610 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   934 ; 0.002 ; 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):  2068 ; 0.641 ; 1.174       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2067 ; 0.639 ; 1.173       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2586 ; 1.133 ; 1.758       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2587 ; 1.133 ; 1.759       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1990 ; 0.895 ; 1.349       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1989 ; 0.894 ; 1.349       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2913 ; 1.570 ; 1.957       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  4892 ; 3.378 ;10.152       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  4766 ; 3.213 ; 9.914       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 1                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1      A     2   258       B     2    258    15286  0.08  0.05    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A   258                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.2861 -31.5227  -1.4763              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0323 T22:   0.0408                                     
REMARK   3      T33:   0.0364 T12:  -0.0285                                     
REMARK   3      T13:  -0.0119 T23:   0.0128                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1187 L22:   0.1619                                     
REMARK   3      L33:   0.3520 L12:  -0.0945                                     
REMARK   3      L13:  -0.0036 L23:  -0.1354                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0360 S12:   0.0441 S13:   0.0177                       
REMARK   3      S21:   0.0018 S22:  -0.0448 S23:  -0.0256                       
REMARK   3      S31:   0.0238 S32:   0.0183 S33:   0.0808                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     2        B   258                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.6333 -56.4855  16.6043              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0618 T22:   0.0222                                     
REMARK   3      T33:   0.0439 T12:   0.0128                                     
REMARK   3      T13:   0.0321 T23:   0.0138                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2461 L22:   0.0327                                     
REMARK   3      L33:   0.3295 L12:  -0.0357                                     
REMARK   3      L13:   0.0116 L23:  -0.0239                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0468 S12:  -0.0331 S13:  -0.0126                       
REMARK   3      S21:  -0.0198 S22:  -0.0053 S23:   0.0004                       
REMARK   3      S31:   0.1021 S32:   0.0143 S33:   0.0521                       
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4M89 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-AUG-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB081590.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-MAR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
REMARK 200  MONOCHROMATOR                  : SILICON DOUBLE CRYSTAL             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : DIFFRACTOMETER                     
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47336                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.470                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M AMMONIUM SULFATE, VAPOR             
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 296.15K                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       80.42333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      160.84667            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      120.63500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      201.05833            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       40.21167            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       80.42333            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      160.84667            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      201.05833            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      120.63500            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       40.21167            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14360 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 32800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -90.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.500000  0.866025  0.000000       45.38500            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000      -78.60913            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       40.21167            
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 A 512  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 465     THR A   259                                                      
REMARK 465     GLU A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     MET B     1                                                      
REMARK 465     THR B   259                                                      
REMARK 465     GLU B   260                                                      
REMARK 465     GLY B   261                                                      
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    ASN A 156      -23.64     77.06                                   
REMARK 500    ASN A 158     -125.80     53.41                                   
REMARK 500    VAL A 248       70.81   -118.09                                   
REMARK 500    ASN B 156      -22.42     76.43                                   
REMARK 500    ASN B 158     -126.70     53.18                                   
REMARK 500    VAL B 248       71.81   -117.65                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TCL A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TCL B 302                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4M86   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN IN UNBOUND FORM                                     
REMARK 900 RELATED ID: 4M87   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH NAD+                                
DBREF  4M89 A    1   261  UNP    A1KVU8   A1KVU8_NEIMF     1    261             
DBREF  4M89 B    1   261  UNP    A1KVU8   A1KVU8_NEIMF     1    261             
SEQRES   1 A  261  MET GLY PHE LEU GLN GLY LYS LYS ILE LEU ILE THR GLY          
SEQRES   2 A  261  MET ILE SER GLU ARG SER ILE ALA TYR GLY ILE ALA LYS          
SEQRES   3 A  261  ALA CYS ARG GLU GLN GLY ALA GLU LEU ALA PHE THR TYR          
SEQRES   4 A  261  VAL VAL ASP LYS LEU GLU GLU ARG VAL ARG LYS MET ALA          
SEQRES   5 A  261  ALA GLU LEU ASP SER GLU LEU VAL PHE ARG CYS ASP VAL          
SEQRES   6 A  261  ALA SER ASP ASP GLU ILE ASN GLN VAL PHE ALA ASP LEU          
SEQRES   7 A  261  GLY LYS HIS TRP ASP GLY LEU ASP GLY LEU VAL HIS SER          
SEQRES   8 A  261  ILE GLY PHE ALA PRO LYS GLU ALA LEU SER GLY ASP PHE          
SEQRES   9 A  261  LEU ASP SER ILE SER ARG GLU ALA PHE ASN THR ALA HIS          
SEQRES  10 A  261  GLU ILE SER ALA TYR SER LEU PRO ALA LEU ALA LYS ALA          
SEQRES  11 A  261  ALA ARG PRO MET MET ARG GLY ARG ASN SER ALA ILE VAL          
SEQRES  12 A  261  ALA LEU SER TYR LEU GLY ALA VAL ARG ALA ILE PRO ASN          
SEQRES  13 A  261  TYR ASN VAL MET GLY MET ALA LYS ALA SER LEU GLU ALA          
SEQRES  14 A  261  GLY ILE ARG PHE THR ALA ALA CYS LEU GLY LYS GLU GLY          
SEQRES  15 A  261  ILE ARG CYS ASN GLY ILE SER ALA GLY PRO ILE LYS THR          
SEQRES  16 A  261  LEU ALA ALA SER GLY ILE ALA ASP PHE GLY LYS LEU LEU          
SEQRES  17 A  261  GLY HIS VAL ALA ALA HIS ASN PRO LEU ARG ARG ASN VAL          
SEQRES  18 A  261  THR ILE GLU GLU VAL GLY ASN THR ALA ALA PHE LEU LEU          
SEQRES  19 A  261  SER ASP LEU SER SER GLY ILE THR GLY GLU ILE THR TYR          
SEQRES  20 A  261  VAL ASP GLY GLY TYR SER ILE ASN ALA LEU SER THR GLU          
SEQRES  21 A  261  GLY                                                          
SEQRES   1 B  261  MET GLY PHE LEU GLN GLY LYS LYS ILE LEU ILE THR GLY          
SEQRES   2 B  261  MET ILE SER GLU ARG SER ILE ALA TYR GLY ILE ALA LYS          
SEQRES   3 B  261  ALA CYS ARG GLU GLN GLY ALA GLU LEU ALA PHE THR TYR          
SEQRES   4 B  261  VAL VAL ASP LYS LEU GLU GLU ARG VAL ARG LYS MET ALA          
SEQRES   5 B  261  ALA GLU LEU ASP SER GLU LEU VAL PHE ARG CYS ASP VAL          
SEQRES   6 B  261  ALA SER ASP ASP GLU ILE ASN GLN VAL PHE ALA ASP LEU          
SEQRES   7 B  261  GLY LYS HIS TRP ASP GLY LEU ASP GLY LEU VAL HIS SER          
SEQRES   8 B  261  ILE GLY PHE ALA PRO LYS GLU ALA LEU SER GLY ASP PHE          
SEQRES   9 B  261  LEU ASP SER ILE SER ARG GLU ALA PHE ASN THR ALA HIS          
SEQRES  10 B  261  GLU ILE SER ALA TYR SER LEU PRO ALA LEU ALA LYS ALA          
SEQRES  11 B  261  ALA ARG PRO MET MET ARG GLY ARG ASN SER ALA ILE VAL          
SEQRES  12 B  261  ALA LEU SER TYR LEU GLY ALA VAL ARG ALA ILE PRO ASN          
SEQRES  13 B  261  TYR ASN VAL MET GLY MET ALA LYS ALA SER LEU GLU ALA          
SEQRES  14 B  261  GLY ILE ARG PHE THR ALA ALA CYS LEU GLY LYS GLU GLY          
SEQRES  15 B  261  ILE ARG CYS ASN GLY ILE SER ALA GLY PRO ILE LYS THR          
SEQRES  16 B  261  LEU ALA ALA SER GLY ILE ALA ASP PHE GLY LYS LEU LEU          
SEQRES  17 B  261  GLY HIS VAL ALA ALA HIS ASN PRO LEU ARG ARG ASN VAL          
SEQRES  18 B  261  THR ILE GLU GLU VAL GLY ASN THR ALA ALA PHE LEU LEU          
SEQRES  19 B  261  SER ASP LEU SER SER GLY ILE THR GLY GLU ILE THR TYR          
SEQRES  20 B  261  VAL ASP GLY GLY TYR SER ILE ASN ALA LEU SER THR GLU          
SEQRES  21 B  261  GLY                                                          
HET    NAD  A 301      44                                                       
HET    TCL  A 302      17                                                       
HET    NAD  B 301      44                                                       
HET    TCL  B 302      17                                                       
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
HETNAM     TCL TRICLOSAN                                                        
FORMUL   3  NAD    2(C21 H27 N7 O14 P2)                                         
FORMUL   4  TCL    2(C12 H7 CL3 O2)                                             
FORMUL   7  HOH   *314(H2 O)                                                    
HELIX    1   1 SER A   19  GLN A   31  1                                  13    
HELIX    2   2 VAL A   41  LYS A   43  5                                   3    
HELIX    3   3 LEU A   44  LEU A   55  1                                  12    
HELIX    4   4 SER A   67  GLY A   79  1                                  13    
HELIX    5   5 PRO A   96  SER A  101  5                                   6    
HELIX    6   6 ASP A  103  ILE A  108  1                                   6    
HELIX    7   7 SER A  109  ALA A  121  1                                  13    
HELIX    8   8 TYR A  122  ARG A  136  1                                  15    
HELIX    9   9 TYR A  147  VAL A  151  5                                   5    
HELIX   10  10 ASN A  158  GLY A  179  1                                  22    
HELIX   11  11 LEU A  196  ILE A  201  5                                   6    
HELIX   12  12 ASP A  203  ASN A  215  1                                  13    
HELIX   13  13 THR A  222  SER A  235  1                                  14    
HELIX   14  14 ASP A  236  SER A  239  5                                   4    
HELIX   15  15 GLY A  251  ASN A  255  5                                   5    
HELIX   16  16 SER B   19  GLN B   31  1                                  13    
HELIX   17  17 VAL B   41  LYS B   43  5                                   3    
HELIX   18  18 LEU B   44  LEU B   55  1                                  12    
HELIX   19  19 SER B   67  GLY B   79  1                                  13    
HELIX   20  20 PRO B   96  SER B  101  5                                   6    
HELIX   21  21 ASP B  103  ILE B  108  1                                   6    
HELIX   22  22 SER B  109  ALA B  121  1                                  13    
HELIX   23  23 TYR B  122  ARG B  136  1                                  15    
HELIX   24  24 TYR B  147  VAL B  151  5                                   5    
HELIX   25  25 ASN B  158  GLY B  179  1                                  22    
HELIX   26  26 LEU B  196  ILE B  201  5                                   6    
HELIX   27  27 ASP B  203  ASN B  215  1                                  13    
HELIX   28  28 THR B  222  SER B  235  1                                  14    
HELIX   29  29 ASP B  236  SER B  239  5                                   4    
HELIX   30  30 GLY B  251  ASN B  255  5                                   5    
SHEET    1   A 7 VAL A  60  ARG A  62  0                                        
SHEET    2   A 7 GLU A  34  TYR A  39  1  N  PHE A  37   O  PHE A  61           
SHEET    3   A 7 LYS A   8  ILE A  11  1  N  ILE A  11   O  ALA A  36           
SHEET    4   A 7 GLY A  87  HIS A  90  1  O  GLY A  87   N  LEU A  10           
SHEET    5   A 7 SER A 140  SER A 146  1  O  VAL A 143   N  HIS A  90           
SHEET    6   A 7 ILE A 183  ALA A 190  1  O  ILE A 188   N  SER A 146           
SHEET    7   A 7 ILE A 245  VAL A 248  1  O  THR A 246   N  GLY A 187           
SHEET    1   B 7 VAL B  60  ARG B  62  0                                        
SHEET    2   B 7 GLU B  34  TYR B  39  1  N  PHE B  37   O  PHE B  61           
SHEET    3   B 7 LYS B   8  ILE B  11  1  N  ILE B  11   O  ALA B  36           
SHEET    4   B 7 GLY B  87  HIS B  90  1  O  VAL B  89   N  LEU B  10           
SHEET    5   B 7 SER B 140  SER B 146  1  O  VAL B 143   N  HIS B  90           
SHEET    6   B 7 ILE B 183  ALA B 190  1  O  ILE B 188   N  SER B 146           
SHEET    7   B 7 ILE B 245  VAL B 248  1  O  THR B 246   N  GLY B 187           
SITE     1 AC1 30 GLY A  13  ILE A  15  SER A  19  ILE A  20                    
SITE     2 AC1 30 VAL A  40  CYS A  63  ASP A  64  VAL A  65                    
SITE     3 AC1 30 SER A  91  ILE A  92  GLY A  93  ILE A 119                    
SITE     4 AC1 30 LEU A 145  SER A 146  LYS A 164  ALA A 190                    
SITE     5 AC1 30 GLY A 191  PRO A 192  ILE A 193  THR A 195                    
SITE     6 AC1 30 LEU A 196  ALA A 197  TCL A 302  HOH A 401                    
SITE     7 AC1 30 HOH A 402  HOH A 412  HOH A 423  HOH A 433                    
SITE     8 AC1 30 HOH A 449  HOH A 451                                          
SITE     1 AC2  9 GLY A  93  ALA A  95  LEU A 100  TYR A 147                    
SITE     2 AC2  9 TYR A 157  LYS A 164  ALA A 197  ILE A 201                    
SITE     3 AC2  9 NAD A 301                                                     
SITE     1 AC3 31 GLY B  13  ILE B  15  SER B  19  ILE B  20                    
SITE     2 AC3 31 VAL B  40  CYS B  63  ASP B  64  VAL B  65                    
SITE     3 AC3 31 SER B  91  ILE B  92  GLY B  93  ILE B 119                    
SITE     4 AC3 31 LEU B 145  SER B 146  TYR B 147  LYS B 164                    
SITE     5 AC3 31 ALA B 190  GLY B 191  PRO B 192  ILE B 193                    
SITE     6 AC3 31 THR B 195  LEU B 196  ALA B 197  TCL B 302                    
SITE     7 AC3 31 HOH B 410  HOH B 414  HOH B 431  HOH B 448                    
SITE     8 AC3 31 HOH B 472  HOH B 488  HOH B 538                               
SITE     1 AC4 10 GLY B  93  ALA B  95  LEU B 100  TYR B 147                    
SITE     2 AC4 10 TYR B 157  LYS B 164  ALA B 197  ALA B 198                    
SITE     3 AC4 10 ILE B 201  NAD B 301                                          
CRYST1   90.770   90.770  241.270  90.00  90.00 120.00 P 61 2 2     24          
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      0.011017  0.006361  0.000000        0.00000                         
SCALE2      0.000000  0.012721  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004145        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system