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Database: PDB
Entry: 4M87
LinkDB: 4M87
Original site: 4M87 
HEADER    OXIDOREDUCTASE                          13-AUG-13   4M87              
TITLE     CRYSTAL STRUCTURE OF ENOYL-ACYL CARRIER PROTEIN REDUCTASE (FABI) FROM 
TITLE    2 NEISSERIA MENINGITIDIS IN COMPLEX WITH NAD+                          
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, NAD, OXIDOREDUCTASE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.D.NANSON,J.K.FORWOOD                                                
REVDAT   1   02-OCT-13 4M87    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+      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 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) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.10                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 27446                          
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) : 0.170                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.189                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1468                            
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) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.31                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1943                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.71                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1740                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 121                          
REMARK   3   BIN FREE R VALUE                    : 0.1950                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3752                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 88                                      
REMARK   3   SOLVENT ATOMS            : 260                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.30                          
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): 0.236         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.168         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.101         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.474         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3904 ; 0.006 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3754 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5281 ; 1.249 ; 1.995       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8614 ; 0.901 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   500 ; 5.609 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   156 ;30.027 ;23.526       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   646 ;12.189 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;13.938 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   601 ; 0.066 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4415 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   883 ; 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):  2009 ; 0.908 ; 1.990       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2008 ; 0.905 ; 1.988       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2506 ; 1.543 ; 2.978       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2507 ; 1.544 ; 2.979       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1893 ; 1.324 ; 2.267       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1894 ; 1.324 ; 2.268       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2776 ; 2.267 ; 3.319       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  4593 ; 4.451 ;16.901       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  4501 ; 4.278 ;16.639       
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    14107  0.11  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):  30.2815 -31.6941  -1.4627              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0386 T22:   0.0291                                     
REMARK   3      T33:   0.0216 T12:  -0.0274                                     
REMARK   3      T13:  -0.0043 T23:   0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0958 L22:   0.1663                                     
REMARK   3      L33:   0.4929 L12:  -0.0541                                     
REMARK   3      L13:   0.0280 L23:  -0.1063                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0369 S12:   0.0311 S13:   0.0304                       
REMARK   3      S21:  -0.0157 S22:  -0.0225 S23:  -0.0111                       
REMARK   3      S31:   0.0180 S32:   0.0129 S33:   0.0594                       
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):  36.2438 -56.4422  16.3473              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0698 T22:   0.0033                                     
REMARK   3      T33:   0.0398 T12:   0.0027                                     
REMARK   3      T13:   0.0377 T23:   0.0007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3015 L22:   0.0818                                     
REMARK   3      L33:   0.4208 L12:  -0.0766                                     
REMARK   3      L13:  -0.0403 L23:   0.0384                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0349 S12:  -0.0241 S13:  -0.0288                       
REMARK   3      S21:  -0.0249 S22:  -0.0025 S23:  -0.0013                       
REMARK   3      S31:   0.1144 S32:  -0.0063 S33:   0.0375                       
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 4M87 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 RCSB081588.                                      
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   : 29052                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.400                             
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) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.33                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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   (%): 52.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.3M AMMONIUM SULFATE, 12.5% GLYCEROL,   
REMARK 280  VAPOR 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       80.28000            
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      160.56000            
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      120.42000            
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      200.70000            
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       40.14000            
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       80.28000            
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      160.56000            
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      200.70000            
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      120.42000            
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       40.14000            
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: 14420 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 32620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -93.0 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       45.55000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000      -78.89491            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       40.14000            
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     LYS B   194                                                      
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     ASP B   203                                                      
REMARK 465     PHE B   204                                                      
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      -27.52     77.98                                   
REMARK 500    ASN A 158     -122.32     52.28                                   
REMARK 500    VAL A 248       74.04   -111.76                                   
REMARK 500    ASN B 156      -27.87     79.87                                   
REMARK 500    ASN B 158     -123.79     52.73                                   
REMARK 500    VAL B 248       74.43   -111.04                                   
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 NAD B 301                 
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: 4M89   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH NAD+ AND TRICLOSAN                  
DBREF  4M87 A    1   261  UNP    A1KVU8   A1KVU8_NEIMF     1    261             
DBREF  4M87 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    NAD  B 301      44                                                       
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
FORMUL   3  NAD    2(C21 H27 N7 O14 P2)                                         
FORMUL   5  HOH   *260(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 ALA A  197  ILE A  201  5                                   5    
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 LYS B  206  ASN B  215  1                                  10    
HELIX   27  27 THR B  222  SER B  235  1                                  14    
HELIX   28  28 ASP B  236  SER B  239  5                                   4    
HELIX   29  29 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  GLY B  87   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  HOH A 401  HOH A 404                    
SITE     7 AC1 30 HOH A 413  HOH A 426  HOH A 433  HOH A 434                    
SITE     8 AC1 30 HOH A 504  HOH A 533                                          
SITE     1 AC2 26 GLY B  13  ILE B  15  SER B  19  ILE B  20                    
SITE     2 AC2 26 VAL B  40  CYS B  63  ASP B  64  VAL B  65                    
SITE     3 AC2 26 SER B  91  ILE B  92  GLY B  93  ILE B 119                    
SITE     4 AC2 26 LEU B 145  SER B 146  TYR B 147  LYS B 164                    
SITE     5 AC2 26 ALA B 190  GLY B 191  PRO B 192  ILE B 193                    
SITE     6 AC2 26 HOH B 411  HOH B 418  HOH B 422  HOH B 460                    
SITE     7 AC2 26 HOH B 475  HOH B 514                                          
CRYST1   91.100   91.100  240.840  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      0.010977  0.006338  0.000000        0.00000                         
SCALE2      0.000000  0.012675  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004152        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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