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Database: PDB
Entry: 4M8S
LinkDB: 4M8S
Original site: 4M8S 
HEADER    OXIDOREDUCTASE                          13-AUG-13   4M8S              
TITLE     CRYSTAL STRUCTURE OF 3-KETOACYL -(ACYL CARRIER PROTEIN) REDUCTASE     
TITLE    2 (FABG) FROM NEISSERIA MENINGITIDIS                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE 3-OXOACYL-[ACYL-CARRIER PROTEIN] REDUCTASE;       
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 1.1.1.100;                                                       
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: FABG, NMC0302;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    FABG, NEISSERIA, ACYL CARRIER PROTEIN, ROSSMANN FOLD, REDUCTASE,      
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.D.NANSON,J.K.FORWOOD                                                
REVDAT   1   28-JAN-15 4M8S    0                                                
JRNL        AUTH   J.D.NANSON,J.K.FORWOOD                                       
JRNL        TITL   THE CRYSTAL STRUCTURE OF 3-KETOACYL -(ACYL CARRIER PROTEIN)  
JRNL        TITL 2 REDUCTASE (FABG) FROM NEISSERIA MENINGITIDIS                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.54                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 56732                          
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) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.199                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3020                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4101                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.88                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2040                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 225                          
REMARK   3   BIN FREE R VALUE                    : 0.2340                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7167                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 677                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.57                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
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): 0.196         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.150         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.094         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.451         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.933                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7221 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  7146 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9735 ; 1.189 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 16349 ; 1.213 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   970 ; 5.020 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   287 ;34.231 ;24.564       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1269 ;12.418 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    54 ;17.695 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1153 ; 0.063 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8347 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1575 ; 0.003 ; 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):  3898 ; 1.176 ; 1.772       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3897 ; 1.175 ; 1.772       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4862 ; 2.054 ; 2.650       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  4863 ; 2.054 ; 2.650       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3323 ; 1.462 ; 2.096       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  3324 ; 1.461 ; 2.096       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  4874 ; 2.559 ; 3.034       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  8805 ; 5.693 ;15.708       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  8490 ; 5.454 ;15.175       
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  : 6                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1      A     3   247       B     3    247    13890  0.13  0.05    
REMARK   3    2      A     2   248       C     2    248    14094  0.13  0.05    
REMARK   3    3      A     2   248       D     2    248    13654  0.11  0.05    
REMARK   3    4      B     3   247       C     3    247    13672  0.13  0.05    
REMARK   3    5      B     3   248       D     3    248    13218  0.13  0.05    
REMARK   3    6      C     2   248       D     2    248    13630  0.11  0.05    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
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   248                          
REMARK   3    ORIGIN FOR THE GROUP (A): -57.1303 125.4734 129.0389              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0472 T22:   0.0277                                     
REMARK   3      T33:   0.0413 T12:   0.0082                                     
REMARK   3      T13:   0.0139 T23:  -0.0132                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2253 L22:   0.2017                                     
REMARK   3      L33:   0.1894 L12:   0.0527                                     
REMARK   3      L13:   0.1092 L23:   0.0187                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0283 S12:   0.0579 S13:  -0.0575                       
REMARK   3      S21:  -0.0158 S22:  -0.0058 S23:  -0.0103                       
REMARK   3      S31:  -0.0286 S32:   0.0130 S33:  -0.0225                       
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     3        B   248                          
REMARK   3    ORIGIN FOR THE GROUP (A): -67.3751 151.3392 142.5260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0466 T22:   0.0122                                     
REMARK   3      T33:   0.0475 T12:   0.0039                                     
REMARK   3      T13:   0.0034 T23:   0.0026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1650 L22:   0.0903                                     
REMARK   3      L33:   0.2214 L12:  -0.0470                                     
REMARK   3      L13:   0.0902 L23:   0.0703                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0327 S12:  -0.0172 S13:  -0.0214                       
REMARK   3      S21:  -0.0273 S22:  -0.0012 S23:   0.0208                       
REMARK   3      S31:  -0.0573 S32:  -0.0011 S33:   0.0339                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     2        C   248                          
REMARK   3    ORIGIN FOR THE GROUP (A): -32.1764 127.7794 146.4971              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0074 T22:   0.0648                                     
REMARK   3      T33:   0.0467 T12:   0.0087                                     
REMARK   3      T13:   0.0155 T23:   0.0069                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2604 L22:   0.1977                                     
REMARK   3      L33:   0.2525 L12:  -0.0132                                     
REMARK   3      L13:   0.1934 L23:   0.1359                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0228 S12:   0.0271 S13:  -0.0558                       
REMARK   3      S21:  -0.0014 S22:   0.0756 S23:  -0.0112                       
REMARK   3      S31:  -0.0225 S32:   0.0697 S33:  -0.0528                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     2        D   248                          
REMARK   3    ORIGIN FOR THE GROUP (A): -48.0736 146.0246 165.3661              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0443 T22:   0.0701                                     
REMARK   3      T33:   0.0062 T12:   0.0100                                     
REMARK   3      T13:   0.0104 T23:   0.0088                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1884 L22:   0.2682                                     
REMARK   3      L33:   0.1232 L12:  -0.2196                                     
REMARK   3      L13:   0.0007 L23:   0.0117                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0677 S12:  -0.0545 S13:  -0.0096                       
REMARK   3      S21:   0.0723 S22:   0.0485 S23:   0.0095                       
REMARK   3      S31:   0.0036 S32:   0.0289 S33:   0.0193                       
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 4M8S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-OCT-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB081609.                                      
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   : 59818                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.360                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
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) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
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   (%): 41.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 250MM AMMONIUM PHOSPHATE DIBASIC, 25%    
REMARK 280  PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 296.15K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       33.44500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.55000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.63500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.55000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.44500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.63500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13170 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 33650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D                            
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 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     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     MET C     1                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ASP D   191                                                      
REMARK 465     MET D   192                                                      
REMARK 465     THR D   193                                                      
REMARK 465     ARG D   194                                                      
REMARK 465     ALA D   195                                                      
REMARK 465     LEU D   196                                                      
REMARK 465     PRO D   197                                                      
REMARK 465     GLU D   198                                                      
REMARK 465     GLU D   199                                                      
REMARK 465     THR D   200                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C  SSEQI                                                     
REMARK 475     ARG B   133                                                      
DBREF  4M8S A    1   248  UNP    A1KRY4   A1KRY4_NEIMF     1    248             
DBREF  4M8S B    1   248  UNP    A1KRY4   A1KRY4_NEIMF     1    248             
DBREF  4M8S C    1   248  UNP    A1KRY4   A1KRY4_NEIMF     1    248             
DBREF  4M8S D    1   248  UNP    A1KRY4   A1KRY4_NEIMF     1    248             
SEQRES   1 A  248  MET SER THR GLN ASP LEU SER GLY LYS ILE ALA LEU VAL          
SEQRES   2 A  248  THR GLY ALA SER ARG GLY ILE GLY ALA ALA ILE ALA ASP          
SEQRES   3 A  248  THR LEU ALA ALA ALA GLY ALA LYS VAL ILE GLY THR ALA          
SEQRES   4 A  248  THR SER GLU SER GLY ALA ALA ALA ILE SER GLU ARG LEU          
SEQRES   5 A  248  ALA GLN TRP GLY GLY GLU GLY ARG VAL LEU ASN SER ALA          
SEQRES   6 A  248  GLU PRO GLU THR VAL GLU ASN LEU ILE ALA ASP ILE GLU          
SEQRES   7 A  248  LYS THR PHE GLY LYS LEU ASP ILE LEU VAL ASN ASN ALA          
SEQRES   8 A  248  GLY ILE THR ARG ASP ASN LEU LEU MET ARG MET LYS GLU          
SEQRES   9 A  248  GLU GLU TRP ASP ASP ILE MET GLN VAL ASN LEU LYS SER          
SEQRES  10 A  248  VAL PHE ARG ALA SER LYS ALA VAL LEU ARG GLY MET MET          
SEQRES  11 A  248  LYS GLN ARG ALA GLY ARG ILE ILE ASN ILE THR SER VAL          
SEQRES  12 A  248  VAL GLY VAL MET GLY ASN ALA GLY GLN THR ASN TYR ALA          
SEQRES  13 A  248  ALA ALA LYS ALA GLY LEU ILE GLY PHE SER LYS SER MET          
SEQRES  14 A  248  ALA ARG GLU VAL GLY SER ARG GLY ILE THR VAL ASN CYS          
SEQRES  15 A  248  VAL ALA PRO GLY PHE ILE ASP THR ASP MET THR ARG ALA          
SEQRES  16 A  248  LEU PRO GLU GLU THR ARG GLN THR PHE THR ALA GLN THR          
SEQRES  17 A  248  ALA LEU GLY ARG PHE GLY ASP ALA GLN ASP ILE ALA ASP          
SEQRES  18 A  248  ALA VAL LEU PHE LEU ALA SER ASP GLN ALA LYS TYR ILE          
SEQRES  19 A  248  THR GLY GLN THR LEU HIS VAL ASN GLY GLY MET LEU MET          
SEQRES  20 A  248  PRO                                                          
SEQRES   1 B  248  MET SER THR GLN ASP LEU SER GLY LYS ILE ALA LEU VAL          
SEQRES   2 B  248  THR GLY ALA SER ARG GLY ILE GLY ALA ALA ILE ALA ASP          
SEQRES   3 B  248  THR LEU ALA ALA ALA GLY ALA LYS VAL ILE GLY THR ALA          
SEQRES   4 B  248  THR SER GLU SER GLY ALA ALA ALA ILE SER GLU ARG LEU          
SEQRES   5 B  248  ALA GLN TRP GLY GLY GLU GLY ARG VAL LEU ASN SER ALA          
SEQRES   6 B  248  GLU PRO GLU THR VAL GLU ASN LEU ILE ALA ASP ILE GLU          
SEQRES   7 B  248  LYS THR PHE GLY LYS LEU ASP ILE LEU VAL ASN ASN ALA          
SEQRES   8 B  248  GLY ILE THR ARG ASP ASN LEU LEU MET ARG MET LYS GLU          
SEQRES   9 B  248  GLU GLU TRP ASP ASP ILE MET GLN VAL ASN LEU LYS SER          
SEQRES  10 B  248  VAL PHE ARG ALA SER LYS ALA VAL LEU ARG GLY MET MET          
SEQRES  11 B  248  LYS GLN ARG ALA GLY ARG ILE ILE ASN ILE THR SER VAL          
SEQRES  12 B  248  VAL GLY VAL MET GLY ASN ALA GLY GLN THR ASN TYR ALA          
SEQRES  13 B  248  ALA ALA LYS ALA GLY LEU ILE GLY PHE SER LYS SER MET          
SEQRES  14 B  248  ALA ARG GLU VAL GLY SER ARG GLY ILE THR VAL ASN CYS          
SEQRES  15 B  248  VAL ALA PRO GLY PHE ILE ASP THR ASP MET THR ARG ALA          
SEQRES  16 B  248  LEU PRO GLU GLU THR ARG GLN THR PHE THR ALA GLN THR          
SEQRES  17 B  248  ALA LEU GLY ARG PHE GLY ASP ALA GLN ASP ILE ALA ASP          
SEQRES  18 B  248  ALA VAL LEU PHE LEU ALA SER ASP GLN ALA LYS TYR ILE          
SEQRES  19 B  248  THR GLY GLN THR LEU HIS VAL ASN GLY GLY MET LEU MET          
SEQRES  20 B  248  PRO                                                          
SEQRES   1 C  248  MET SER THR GLN ASP LEU SER GLY LYS ILE ALA LEU VAL          
SEQRES   2 C  248  THR GLY ALA SER ARG GLY ILE GLY ALA ALA ILE ALA ASP          
SEQRES   3 C  248  THR LEU ALA ALA ALA GLY ALA LYS VAL ILE GLY THR ALA          
SEQRES   4 C  248  THR SER GLU SER GLY ALA ALA ALA ILE SER GLU ARG LEU          
SEQRES   5 C  248  ALA GLN TRP GLY GLY GLU GLY ARG VAL LEU ASN SER ALA          
SEQRES   6 C  248  GLU PRO GLU THR VAL GLU ASN LEU ILE ALA ASP ILE GLU          
SEQRES   7 C  248  LYS THR PHE GLY LYS LEU ASP ILE LEU VAL ASN ASN ALA          
SEQRES   8 C  248  GLY ILE THR ARG ASP ASN LEU LEU MET ARG MET LYS GLU          
SEQRES   9 C  248  GLU GLU TRP ASP ASP ILE MET GLN VAL ASN LEU LYS SER          
SEQRES  10 C  248  VAL PHE ARG ALA SER LYS ALA VAL LEU ARG GLY MET MET          
SEQRES  11 C  248  LYS GLN ARG ALA GLY ARG ILE ILE ASN ILE THR SER VAL          
SEQRES  12 C  248  VAL GLY VAL MET GLY ASN ALA GLY GLN THR ASN TYR ALA          
SEQRES  13 C  248  ALA ALA LYS ALA GLY LEU ILE GLY PHE SER LYS SER MET          
SEQRES  14 C  248  ALA ARG GLU VAL GLY SER ARG GLY ILE THR VAL ASN CYS          
SEQRES  15 C  248  VAL ALA PRO GLY PHE ILE ASP THR ASP MET THR ARG ALA          
SEQRES  16 C  248  LEU PRO GLU GLU THR ARG GLN THR PHE THR ALA GLN THR          
SEQRES  17 C  248  ALA LEU GLY ARG PHE GLY ASP ALA GLN ASP ILE ALA ASP          
SEQRES  18 C  248  ALA VAL LEU PHE LEU ALA SER ASP GLN ALA LYS TYR ILE          
SEQRES  19 C  248  THR GLY GLN THR LEU HIS VAL ASN GLY GLY MET LEU MET          
SEQRES  20 C  248  PRO                                                          
SEQRES   1 D  248  MET SER THR GLN ASP LEU SER GLY LYS ILE ALA LEU VAL          
SEQRES   2 D  248  THR GLY ALA SER ARG GLY ILE GLY ALA ALA ILE ALA ASP          
SEQRES   3 D  248  THR LEU ALA ALA ALA GLY ALA LYS VAL ILE GLY THR ALA          
SEQRES   4 D  248  THR SER GLU SER GLY ALA ALA ALA ILE SER GLU ARG LEU          
SEQRES   5 D  248  ALA GLN TRP GLY GLY GLU GLY ARG VAL LEU ASN SER ALA          
SEQRES   6 D  248  GLU PRO GLU THR VAL GLU ASN LEU ILE ALA ASP ILE GLU          
SEQRES   7 D  248  LYS THR PHE GLY LYS LEU ASP ILE LEU VAL ASN ASN ALA          
SEQRES   8 D  248  GLY ILE THR ARG ASP ASN LEU LEU MET ARG MET LYS GLU          
SEQRES   9 D  248  GLU GLU TRP ASP ASP ILE MET GLN VAL ASN LEU LYS SER          
SEQRES  10 D  248  VAL PHE ARG ALA SER LYS ALA VAL LEU ARG GLY MET MET          
SEQRES  11 D  248  LYS GLN ARG ALA GLY ARG ILE ILE ASN ILE THR SER VAL          
SEQRES  12 D  248  VAL GLY VAL MET GLY ASN ALA GLY GLN THR ASN TYR ALA          
SEQRES  13 D  248  ALA ALA LYS ALA GLY LEU ILE GLY PHE SER LYS SER MET          
SEQRES  14 D  248  ALA ARG GLU VAL GLY SER ARG GLY ILE THR VAL ASN CYS          
SEQRES  15 D  248  VAL ALA PRO GLY PHE ILE ASP THR ASP MET THR ARG ALA          
SEQRES  16 D  248  LEU PRO GLU GLU THR ARG GLN THR PHE THR ALA GLN THR          
SEQRES  17 D  248  ALA LEU GLY ARG PHE GLY ASP ALA GLN ASP ILE ALA ASP          
SEQRES  18 D  248  ALA VAL LEU PHE LEU ALA SER ASP GLN ALA LYS TYR ILE          
SEQRES  19 D  248  THR GLY GLN THR LEU HIS VAL ASN GLY GLY MET LEU MET          
SEQRES  20 D  248  PRO                                                          
FORMUL   5  HOH   *677(H2 O)                                                    
HELIX    1   1 ARG A   18  ALA A   31  1                                  14    
HELIX    2   2 SER A   41  ALA A   53  1                                  13    
HELIX    3   3 GLN A   54  GLY A   56  5                                   3    
HELIX    4   4 GLU A   68  GLY A   82  1                                  15    
HELIX    5   5 LEU A   98  MET A  102  5                                   5    
HELIX    6   6 LYS A  103  LEU A  115  1                                  13    
HELIX    7   7 LEU A  115  ARG A  133  1                                  19    
HELIX    8   8 VAL A  143  GLY A  148  1                                   6    
HELIX    9   9 GLN A  152  GLY A  174  1                                  23    
HELIX   10  10 THR A  190  ALA A  195  1                                   6    
HELIX   11  11 PRO A  197  ALA A  206  1                                  10    
HELIX   12  12 ASP A  215  SER A  228  1                                  14    
HELIX   13  13 ASP A  229  LYS A  232  5                                   4    
HELIX   14  14 ARG B   18  ALA B   31  1                                  14    
HELIX   15  15 SER B   41  ALA B   53  1                                  13    
HELIX   16  16 GLN B   54  GLY B   56  5                                   3    
HELIX   17  17 GLU B   68  PHE B   81  1                                  14    
HELIX   18  18 LEU B   98  MET B  102  5                                   5    
HELIX   19  19 LYS B  103  LEU B  115  1                                  13    
HELIX   20  20 LEU B  115  GLN B  132  1                                  18    
HELIX   21  21 VAL B  143  GLY B  148  1                                   6    
HELIX   22  22 GLN B  152  GLY B  174  1                                  23    
HELIX   23  23 SER B  175  GLY B  177  5                                   3    
HELIX   24  24 THR B  190  ALA B  195  1                                   6    
HELIX   25  25 PRO B  197  ALA B  206  1                                  10    
HELIX   26  26 ASP B  215  SER B  228  1                                  14    
HELIX   27  27 ASP B  229  LYS B  232  5                                   4    
HELIX   28  28 ARG C   18  ALA C   31  1                                  14    
HELIX   29  29 SER C   41  ALA C   53  1                                  13    
HELIX   30  30 GLN C   54  GLY C   56  5                                   3    
HELIX   31  31 GLU C   68  GLY C   82  1                                  15    
HELIX   32  32 LEU C   98  MET C  102  5                                   5    
HELIX   33  33 LYS C  103  LEU C  115  1                                  13    
HELIX   34  34 LEU C  115  ARG C  133  1                                  19    
HELIX   35  35 VAL C  143  GLY C  148  1                                   6    
HELIX   36  36 GLN C  152  GLY C  174  1                                  23    
HELIX   37  37 THR C  190  ALA C  195  1                                   6    
HELIX   38  38 PRO C  197  THR C  208  1                                  12    
HELIX   39  39 ASP C  215  SER C  228  1                                  14    
HELIX   40  40 ASP C  229  LYS C  232  5                                   4    
HELIX   41  41 ARG D   18  ALA D   31  1                                  14    
HELIX   42  42 SER D   41  ALA D   53  1                                  13    
HELIX   43  43 GLN D   54  GLY D   56  5                                   3    
HELIX   44  44 GLU D   68  GLY D   82  1                                  15    
HELIX   45  45 LEU D   98  MET D  102  5                                   5    
HELIX   46  46 LYS D  103  LEU D  115  1                                  13    
HELIX   47  47 LEU D  115  ARG D  133  1                                  19    
HELIX   48  48 VAL D  143  GLY D  148  1                                   6    
HELIX   49  49 GLN D  152  GLY D  174  1                                  23    
HELIX   50  50 GLN D  202  ALA D  206  1                                   5    
HELIX   51  51 ASP D  215  SER D  228  1                                  14    
HELIX   52  52 ASP D  229  LYS D  232  5                                   4    
SHEET    1   A 7 GLU A  58  VAL A  61  0                                        
SHEET    2   A 7 LYS A  34  ALA A  39  1  N  GLY A  37   O  GLU A  58           
SHEET    3   A 7 ILE A  10  VAL A  13  1  N  ALA A  11   O  LYS A  34           
SHEET    4   A 7 ILE A  86  ASN A  89  1  O  VAL A  88   N  LEU A  12           
SHEET    5   A 7 GLY A 135  ILE A 140  1  O  ILE A 138   N  LEU A  87           
SHEET    6   A 7 ILE A 178  PRO A 185  1  O  ASN A 181   N  ASN A 139           
SHEET    7   A 7 THR A 238  VAL A 241  1  O  LEU A 239   N  CYS A 182           
SHEET    1   B 7 GLU B  58  VAL B  61  0                                        
SHEET    2   B 7 LYS B  34  ALA B  39  1  N  GLY B  37   O  GLU B  58           
SHEET    3   B 7 ILE B  10  VAL B  13  1  N  ALA B  11   O  LYS B  34           
SHEET    4   B 7 ILE B  86  ASN B  89  1  O  VAL B  88   N  LEU B  12           
SHEET    5   B 7 ARG B 136  ILE B 140  1  O  ILE B 138   N  LEU B  87           
SHEET    6   B 7 THR B 179  PRO B 185  1  O  ASN B 181   N  ASN B 139           
SHEET    7   B 7 THR B 238  VAL B 241  1  O  LEU B 239   N  CYS B 182           
SHEET    1   C 7 GLU C  58  VAL C  61  0                                        
SHEET    2   C 7 LYS C  34  ALA C  39  1  N  GLY C  37   O  GLU C  58           
SHEET    3   C 7 ILE C  10  VAL C  13  1  N  ALA C  11   O  LYS C  34           
SHEET    4   C 7 ILE C  86  ASN C  89  1  O  VAL C  88   N  LEU C  12           
SHEET    5   C 7 GLY C 135  ILE C 140  1  O  ILE C 138   N  LEU C  87           
SHEET    6   C 7 ILE C 178  PRO C 185  1  O  ASN C 181   N  ASN C 139           
SHEET    7   C 7 THR C 238  VAL C 241  1  O  LEU C 239   N  CYS C 182           
SHEET    1   D 7 GLU D  58  VAL D  61  0                                        
SHEET    2   D 7 LYS D  34  ALA D  39  1  N  GLY D  37   O  GLU D  58           
SHEET    3   D 7 ILE D  10  VAL D  13  1  N  ALA D  11   O  LYS D  34           
SHEET    4   D 7 ILE D  86  ASN D  89  1  O  VAL D  88   N  LEU D  12           
SHEET    5   D 7 GLY D 135  ILE D 140  1  O  ILE D 138   N  LEU D  87           
SHEET    6   D 7 ILE D 178  PRO D 185  1  O  ASN D 181   N  ASN D 139           
SHEET    7   D 7 THR D 238  VAL D 241  1  O  LEU D 239   N  CYS D 182           
CRYST1   66.890  111.270  117.100  90.00  90.00  90.00 P 21 21 21   16          
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      0.014950  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008987  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008540        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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