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Database: PDB
Entry: 4M86
LinkDB: 4M86
Original site: 4M86 
HEADER    OXIDOREDUCTASE                          13-AUG-13   4M86              
TITLE     CRYSTAL STRUCTURE OF ENOYL-ACYL CARRIER PROTEIN REDUCTASE (FABI) FROM 
TITLE    2 NEISSERIA MENINGITIDIS                                               
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, ROSSMANN FOLD,           
KEYWDS   2 REDUCTASE, OXIDOREDUCTASE                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.D.NANSON,J.K.FORWOOD                                                
REVDAT   1   02-OCT-13 4M86    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                           
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 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) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.65                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 29598                          
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) : 0.178                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
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) : 2258                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.63                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2020                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 152                          
REMARK   3   BIN FREE R VALUE                    : 0.2550                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3738                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 292                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.91                          
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) : -0.01000                                             
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): 0.216         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.168         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.102         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.337         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3794 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3694 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5113 ; 1.157 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8474 ; 0.858 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   495 ; 5.657 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   157 ;32.859 ;23.503       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   647 ;12.774 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;15.872 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   581 ; 0.063 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4333 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   855 ; 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):  1992 ; 1.189 ; 2.088       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1991 ; 1.188 ; 2.086       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2483 ; 2.042 ; 3.116       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2484 ; 2.042 ; 3.118       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1802 ; 1.458 ; 2.398       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1803 ; 1.457 ; 2.399       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2631 ; 2.536 ; 3.489       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  4544 ; 4.805 ;17.516       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  4429 ; 4.617 ;17.253       
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   259       B     2    259    14895  0.09  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   259                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.6092  32.1573  -1.4486              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0407 T22:   0.0680                                     
REMARK   3      T33:   0.0460 T12:  -0.0385                                     
REMARK   3      T13:   0.0250 T23:  -0.0434                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1252 L22:   0.1329                                     
REMARK   3      L33:   0.4911 L12:  -0.0877                                     
REMARK   3      L13:   0.0084 L23:   0.0780                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0571 S12:   0.0733 S13:  -0.0259                       
REMARK   3      S21:   0.0076 S22:  -0.0569 S23:   0.0192                       
REMARK   3      S31:   0.0087 S32:  -0.0630 S33:   0.1140                       
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   259                          
REMARK   3    ORIGIN FOR THE GROUP (A): -36.4498  56.4822  16.5791              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0521 T22:   0.0395                                     
REMARK   3      T33:   0.0701 T12:   0.0295                                     
REMARK   3      T13:  -0.0476 T23:  -0.0423                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2601 L22:   0.0714                                     
REMARK   3      L33:   0.3870 L12:  -0.0702                                     
REMARK   3      L13:   0.1200 L23:  -0.0529                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0778 S12:  -0.0160 S13:   0.0543                       
REMARK   3      S21:  -0.0069 S22:  -0.0303 S23:   0.0013                       
REMARK   3      S31:  -0.0960 S32:  -0.0255 S33:   0.1081                       
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 4M86 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 RCSB081587.                                      
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   : 33863                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 36.580                             
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) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.23                     
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   (%): 53.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0M 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       80.50000            
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      161.00000            
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      120.75000            
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      201.25000            
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       40.25000            
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       80.50000            
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      161.00000            
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      201.25000            
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      120.75000            
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       40.25000            
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: 15050 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 33340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -100.0 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      -45.80450            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000       79.33572            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       40.25000            
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   195                                                      
REMARK 465     LEU A   196                                                      
REMARK 465     ALA A   197                                                      
REMARK 465     ALA A   198                                                      
REMARK 465     SER A   199                                                      
REMARK 465     GLY A   200                                                      
REMARK 465     ILE A   201                                                      
REMARK 465     ALA A   202                                                      
REMARK 465     ASP A   203                                                      
REMARK 465     GLU A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     MET B     1                                                      
REMARK 465     THR B   195                                                      
REMARK 465     LEU B   196                                                      
REMARK 465     ALA B   197                                                      
REMARK 465     ALA B   198                                                      
REMARK 465     SER B   199                                                      
REMARK 465     GLY B   200                                                      
REMARK 465     ILE B   201                                                      
REMARK 465     ALA B   202                                                      
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      -14.94     75.38                                   
REMARK 500    ASN A 158     -121.93     51.11                                   
REMARK 500    VAL A 248       74.91   -104.67                                   
REMARK 500    ASN B 156      -18.19     78.00                                   
REMARK 500    ASN B 158     -122.81     52.73                                   
REMARK 500    VAL B 248       75.64   -105.44                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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+                                
REMARK 900 RELATED ID: 4M89   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH NAD+ AND TRICLOSAN                  
DBREF  4M86 A    1   261  UNP    A1KVU8   A1KVU8_NEIMF     1    261             
DBREF  4M86 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                                                          
FORMUL   3  HOH   *292(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 GLY A  205  ASN A  215  1                                  11    
HELIX   12  12 THR A  222  SER A  235  1                                  14    
HELIX   13  13 ASP A  236  SER A  239  5                                   4    
HELIX   14  14 GLY A  251  ASN A  255  5                                   5    
HELIX   15  15 SER B   19  GLN B   31  1                                  13    
HELIX   16  16 VAL B   41  LYS B   43  5                                   3    
HELIX   17  17 LEU B   44  LEU B   55  1                                  12    
HELIX   18  18 SER B   67  GLY B   79  1                                  13    
HELIX   19  19 PRO B   96  SER B  101  5                                   6    
HELIX   20  20 ASP B  103  ILE B  108  1                                   6    
HELIX   21  21 SER B  109  ALA B  121  1                                  13    
HELIX   22  22 TYR B  122  ARG B  136  1                                  15    
HELIX   23  23 TYR B  147  VAL B  151  5                                   5    
HELIX   24  24 ASN B  158  GLY B  179  1                                  22    
HELIX   25  25 PHE B  204  ASN B  215  1                                  12    
HELIX   26  26 THR B  222  SER B  235  1                                  14    
HELIX   27  27 ASP B  236  SER B  239  5                                   4    
HELIX   28  28 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   9   O  GLU A  34           
SHEET    4   A 7 GLY A  87  HIS A  90  1  O  VAL A  89   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           
CRYST1   91.609   91.609  241.500  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      0.010916  0.006302  0.000000        0.00000                         
SCALE2      0.000000  0.012605  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004141        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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