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Database: PDB
Entry: 5CFZ
LinkDB: 5CFZ
Original site: 5CFZ 
HEADER    OXIDOREDUCTASE                          08-JUL-15   5CFZ              
TITLE     CRYSTAL STRUCTURE OF E. COLI FABI IN APO FORM                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH] FABI;        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ENR,NADH-DEPENDENT ENOYL-ACP REDUCTASE;                     
COMPND   5 EC: 1.3.1.9;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);                  
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: FABI, ENVM, B1288, JW1281;                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET30                                     
KEYWDS    ANTIBIOTICS, NAD, ENOYL-ACP REDUCTASE, OXIDOREDUCATASE,               
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.A.JORDAN,J.L.VEY                                                    
REVDAT   1   09-DEC-15 5CFZ    0                                                
JRNL        AUTH   C.A.JORDAN,B.A.SANDOVAL,M.V.SEROBYAN,D.H.GILLING,            
JRNL        AUTH 2 M.P.GROZIAK,H.H.XU,J.L.VEY                                   
JRNL        TITL   CRYSTALLOGRAPHIC INSIGHTS INTO THE STRUCTURE-ACTIVITY        
JRNL        TITL 2 RELATIONSHIPS OF DIAZABORINE ENOYL-ACP REDUCTASE INHIBITORS. 
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  71  1521 2015              
JRNL        REFN                   ESSN 2053-230X                               
JRNL        PMID   26625295                                                     
JRNL        DOI    10.1107/S2053230X15022098                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.97 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.97                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 42431                          
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) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2255                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.97                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.02                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2548                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.44                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2200                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 124                          
REMARK   3   BIN FREE R VALUE                    : 0.2880                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3653                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 226                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.27                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.24000                                             
REMARK   3    B22 (A**2) : -0.24000                                             
REMARK   3    B33 (A**2) : 0.35000                                              
REMARK   3    B12 (A**2) : -0.12000                                             
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): 0.145         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.137         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.092         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.219         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3713 ; 0.020 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5020 ; 2.011 ; 1.954       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   491 ; 6.709 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   152 ;34.205 ;23.947       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   593 ;13.050 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;15.074 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   572 ; 0.147 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2804 ; 0.010 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   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    257       B     2    257     329 0.120 0.050     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 USED IF PRESENT IN    
REMARK   3  THE INPUT U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 5CFZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUL-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000210859.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-APR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL12-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95370                            
REMARK 200  MONOCHROMATOR                  : SI(111) DOUBLE CRYSTAL             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.20                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44807                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.969                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.903                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 11.70                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.97                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.16200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.16200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 10.10                              
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: 1QSG.PDB (MODEL'S RESIDUES WERE TRUNCATED TO         
REMARK 200  POLYALANINE AND LIGANDS WERE REMOVED)                               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M CITRATE PH 7.0, 0.1M AMMONIUM       
REMARK 280  SULFATE, 22%W/V PEG 2000, VAPOR DIFFUSION, HANGING DROP,            
REMARK 280  TEMPERATURE 298K                                                    
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      107.98000            
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      215.96000            
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      161.97000            
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      269.95000            
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       53.99000            
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      107.98000            
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      215.96000            
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      269.95000            
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      161.97000            
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       53.99000            
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: 14330 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 31200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 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        0.00000            
REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -53.99000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 346  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 330  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -42                                                      
REMARK 465     HIS A   -41                                                      
REMARK 465     HIS A   -40                                                      
REMARK 465     HIS A   -39                                                      
REMARK 465     HIS A   -38                                                      
REMARK 465     HIS A   -37                                                      
REMARK 465     HIS A   -36                                                      
REMARK 465     SER A   -35                                                      
REMARK 465     SER A   -34                                                      
REMARK 465     GLY A   -33                                                      
REMARK 465     LEU A   -32                                                      
REMARK 465     VAL A   -31                                                      
REMARK 465     PRO A   -30                                                      
REMARK 465     ARG A   -29                                                      
REMARK 465     GLY A   -28                                                      
REMARK 465     SER A   -27                                                      
REMARK 465     GLY A   -26                                                      
REMARK 465     MET A   -25                                                      
REMARK 465     LYS A   -24                                                      
REMARK 465     GLU A   -23                                                      
REMARK 465     THR A   -22                                                      
REMARK 465     ALA A   -21                                                      
REMARK 465     ALA A   -20                                                      
REMARK 465     ALA A   -19                                                      
REMARK 465     LYS A   -18                                                      
REMARK 465     PHE A   -17                                                      
REMARK 465     GLU A   -16                                                      
REMARK 465     ARG A   -15                                                      
REMARK 465     GLN A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     MET A   -12                                                      
REMARK 465     ASP A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     PRO A    -9                                                      
REMARK 465     ASP A    -8                                                      
REMARK 465     LEU A    -7                                                      
REMARK 465     GLY A    -6                                                      
REMARK 465     THR A    -5                                                      
REMARK 465     ASP A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     ASP A    -2                                                      
REMARK 465     ASP A    -1                                                      
REMARK 465     LYS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     LEU A   195                                                      
REMARK 465     ALA A   196                                                      
REMARK 465     ALA A   197                                                      
REMARK 465     SER A   198                                                      
REMARK 465     GLY A   199                                                      
REMARK 465     ILE A   200                                                      
REMARK 465     LYS A   201                                                      
REMARK 465     GLU A   258                                                      
REMARK 465     LEU A   259                                                      
REMARK 465     GLU A   260                                                      
REMARK 465     LEU A   261                                                      
REMARK 465     LYS A   262                                                      
REMARK 465     MET B   -42                                                      
REMARK 465     HIS B   -41                                                      
REMARK 465     HIS B   -40                                                      
REMARK 465     HIS B   -39                                                      
REMARK 465     HIS B   -38                                                      
REMARK 465     HIS B   -37                                                      
REMARK 465     HIS B   -36                                                      
REMARK 465     SER B   -35                                                      
REMARK 465     SER B   -34                                                      
REMARK 465     GLY B   -33                                                      
REMARK 465     LEU B   -32                                                      
REMARK 465     VAL B   -31                                                      
REMARK 465     PRO B   -30                                                      
REMARK 465     ARG B   -29                                                      
REMARK 465     GLY B   -28                                                      
REMARK 465     SER B   -27                                                      
REMARK 465     GLY B   -26                                                      
REMARK 465     MET B   -25                                                      
REMARK 465     LYS B   -24                                                      
REMARK 465     GLU B   -23                                                      
REMARK 465     THR B   -22                                                      
REMARK 465     ALA B   -21                                                      
REMARK 465     ALA B   -20                                                      
REMARK 465     ALA B   -19                                                      
REMARK 465     LYS B   -18                                                      
REMARK 465     PHE B   -17                                                      
REMARK 465     GLU B   -16                                                      
REMARK 465     ARG B   -15                                                      
REMARK 465     GLN B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     MET B   -12                                                      
REMARK 465     ASP B   -11                                                      
REMARK 465     SER B   -10                                                      
REMARK 465     PRO B    -9                                                      
REMARK 465     ASP B    -8                                                      
REMARK 465     LEU B    -7                                                      
REMARK 465     GLY B    -6                                                      
REMARK 465     THR B    -5                                                      
REMARK 465     ASP B    -4                                                      
REMARK 465     ASP B    -3                                                      
REMARK 465     ASP B    -2                                                      
REMARK 465     ASP B    -1                                                      
REMARK 465     LYS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     THR B   194                                                      
REMARK 465     LEU B   195                                                      
REMARK 465     ALA B   196                                                      
REMARK 465     ALA B   197                                                      
REMARK 465     SER B   198                                                      
REMARK 465     GLY B   199                                                      
REMARK 465     ILE B   200                                                      
REMARK 465     LYS B   201                                                      
REMARK 465     ASP B   202                                                      
REMARK 465     PHE B   203                                                      
REMARK 465     GLU B   258                                                      
REMARK 465     LEU B   259                                                      
REMARK 465     GLU B   260                                                      
REMARK 465     LEU B   261                                                      
REMARK 465     LYS B   262                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP A 202    CG   OD1  OD2                                       
REMARK 470     PHE A 203    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A 204    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 205    CG   CD   CE   NZ                                   
REMARK 470     LYS B  43    CG   CD   CE   NZ                                   
REMARK 470     ARG B 204    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 205    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   306     O    HOH A   406              1.12            
REMARK 500   O    HOH A   304     O    HOH A   317              1.27            
REMARK 500   O    HOH A   303     O    HOH A   337              1.33            
REMARK 500   O    HOH B   302     O    HOH B   352              1.44            
REMARK 500   O    HOH A   394     O    HOH A   412              1.59            
REMARK 500   NZ   LYS B    17     OE1  GLN B    54              1.85            
REMARK 500   O    HOH A   415     O    HOH A   430              1.87            
REMARK 500   N    GLY A     2     O    HOH A   301              1.91            
REMARK 500   O    HOH A   373     O    HOH A   412              1.97            
REMARK 500   O    SER A   252     O    HOH A   302              2.01            
REMARK 500   NH1  ARG B     8     O    HOH B   301              2.06            
REMARK 500   O    GLU B   150     O    HOH B   302              2.10            
REMARK 500   O    HOH A   428     O    HOH A   434              2.19            
REMARK 500   O    ASP A   101     O    HOH A   303              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   326     O    HOH A   344     8565     1.60            
REMARK 500   O    HOH B   312     O    HOH B   324    10554     1.67            
REMARK 500   O    HOH A   427     O    HOH A   429    10554     1.78            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A  90   CG    HIS A  90   CD2     0.073                       
REMARK 500    GLU A 180   CD    GLU A 180   OE1     0.074                       
REMARK 500    HIS B 209   CG    HIS B 209   CD2     0.062                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  47   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ASP A 235   CB  -  CG  -  OD1 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ASP B  98   CB  -  CG  -  OD1 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    LEU B 161   CB  -  CG  -  CD2 ANGL. DEV. = -10.7 DEGREES          
REMARK 500    GLU B 180   CB  -  CA  -  C   ANGL. DEV. = -13.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    SER A 121      -50.52   -120.61                                   
REMARK 500    ASN A 155      -24.59     79.99                                   
REMARK 500    ASN A 157     -129.00     53.65                                   
REMARK 500    VAL A 247       70.17   -115.56                                   
REMARK 500    GLN B  40      -63.06    -91.40                                   
REMARK 500    SER B 145     -167.23   -126.55                                   
REMARK 500    ASN B 155      -25.25     70.64                                   
REMARK 500    ASN B 157     -125.36     47.62                                   
REMARK 500    VAL B 247       72.77   -114.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5CG1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5CG2   RELATED DB: PDB                                   
DBREF  5CFZ A    1   262  UNP    P0AEK4   FABI_ECOLI       1    262             
DBREF  5CFZ B    1   262  UNP    P0AEK4   FABI_ECOLI       1    262             
SEQADV 5CFZ MET A  -42  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ HIS A  -41  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ HIS A  -40  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ HIS A  -39  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ HIS A  -38  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ HIS A  -37  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ HIS A  -36  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ SER A  -35  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ SER A  -34  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ GLY A  -33  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ LEU A  -32  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ VAL A  -31  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ PRO A  -30  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ ARG A  -29  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ GLY A  -28  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ SER A  -27  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ GLY A  -26  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ MET A  -25  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ LYS A  -24  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ GLU A  -23  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ THR A  -22  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ ALA A  -21  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ ALA A  -20  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ ALA A  -19  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ LYS A  -18  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ PHE A  -17  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ GLU A  -16  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ ARG A  -15  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ GLN A  -14  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ HIS A  -13  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ MET A  -12  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ ASP A  -11  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ SER A  -10  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ PRO A   -9  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ ASP A   -8  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ LEU A   -7  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ GLY A   -6  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ THR A   -5  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ ASP A   -4  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ ASP A   -3  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ ASP A   -2  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ ASP A   -1  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ LYS A    0  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ MET B  -42  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ HIS B  -41  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ HIS B  -40  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ HIS B  -39  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ HIS B  -38  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ HIS B  -37  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ HIS B  -36  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ SER B  -35  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ SER B  -34  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ GLY B  -33  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ LEU B  -32  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ VAL B  -31  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ PRO B  -30  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ ARG B  -29  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ GLY B  -28  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ SER B  -27  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ GLY B  -26  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ MET B  -25  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ LYS B  -24  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ GLU B  -23  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ THR B  -22  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ ALA B  -21  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ ALA B  -20  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ ALA B  -19  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ LYS B  -18  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ PHE B  -17  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ GLU B  -16  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ ARG B  -15  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ GLN B  -14  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ HIS B  -13  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ MET B  -12  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ ASP B  -11  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ SER B  -10  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ PRO B   -9  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ ASP B   -8  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ LEU B   -7  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ GLY B   -6  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ THR B   -5  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ ASP B   -4  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ ASP B   -3  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ ASP B   -2  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ ASP B   -1  UNP  P0AEK4              EXPRESSION TAG                 
SEQADV 5CFZ LYS B    0  UNP  P0AEK4              EXPRESSION TAG                 
SEQRES   1 A  305  MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO          
SEQRES   2 A  305  ARG GLY SER GLY MET LYS GLU THR ALA ALA ALA LYS PHE          
SEQRES   3 A  305  GLU ARG GLN HIS MET ASP SER PRO ASP LEU GLY THR ASP          
SEQRES   4 A  305  ASP ASP ASP LYS MET GLY PHE LEU SER GLY LYS ARG ILE          
SEQRES   5 A  305  LEU VAL THR GLY VAL ALA SER LYS LEU SER ILE ALA TYR          
SEQRES   6 A  305  GLY ILE ALA GLN ALA MET HIS ARG GLU GLY ALA GLU LEU          
SEQRES   7 A  305  ALA PHE THR TYR GLN ASN ASP LYS LEU LYS GLY ARG VAL          
SEQRES   8 A  305  GLU GLU PHE ALA ALA GLN LEU GLY SER ASP ILE VAL LEU          
SEQRES   9 A  305  GLN CYS ASP VAL ALA GLU ASP ALA SER ILE ASP THR MET          
SEQRES  10 A  305  PHE ALA GLU LEU GLY LYS VAL TRP PRO LYS PHE ASP GLY          
SEQRES  11 A  305  PHE VAL HIS SER ILE GLY PHE ALA PRO GLY ASP GLN LEU          
SEQRES  12 A  305  ASP GLY ASP TYR VAL ASN ALA VAL THR ARG GLU GLY PHE          
SEQRES  13 A  305  LYS ILE ALA HIS ASP ILE SER SER TYR SER PHE VAL ALA          
SEQRES  14 A  305  MET ALA LYS ALA CYS ARG SER MET LEU ASN PRO GLY SER          
SEQRES  15 A  305  ALA LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG ALA          
SEQRES  16 A  305  ILE PRO ASN TYR ASN VAL MET GLY LEU ALA LYS ALA SER          
SEQRES  17 A  305  LEU GLU ALA ASN VAL ARG TYR MET ALA ASN ALA MET GLY          
SEQRES  18 A  305  PRO GLU GLY VAL ARG VAL ASN ALA ILE SER ALA GLY PRO          
SEQRES  19 A  305  ILE ARG THR LEU ALA ALA SER GLY ILE LYS ASP PHE ARG          
SEQRES  20 A  305  LYS MET LEU ALA HIS CYS GLU ALA VAL THR PRO ILE ARG          
SEQRES  21 A  305  ARG THR VAL THR ILE GLU ASP VAL GLY ASN SER ALA ALA          
SEQRES  22 A  305  PHE LEU CYS SER ASP LEU SER ALA GLY ILE SER GLY GLU          
SEQRES  23 A  305  VAL VAL HIS VAL ASP GLY GLY PHE SER ILE ALA ALA MET          
SEQRES  24 A  305  ASN GLU LEU GLU LEU LYS                                      
SEQRES   1 B  305  MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO          
SEQRES   2 B  305  ARG GLY SER GLY MET LYS GLU THR ALA ALA ALA LYS PHE          
SEQRES   3 B  305  GLU ARG GLN HIS MET ASP SER PRO ASP LEU GLY THR ASP          
SEQRES   4 B  305  ASP ASP ASP LYS MET GLY PHE LEU SER GLY LYS ARG ILE          
SEQRES   5 B  305  LEU VAL THR GLY VAL ALA SER LYS LEU SER ILE ALA TYR          
SEQRES   6 B  305  GLY ILE ALA GLN ALA MET HIS ARG GLU GLY ALA GLU LEU          
SEQRES   7 B  305  ALA PHE THR TYR GLN ASN ASP LYS LEU LYS GLY ARG VAL          
SEQRES   8 B  305  GLU GLU PHE ALA ALA GLN LEU GLY SER ASP ILE VAL LEU          
SEQRES   9 B  305  GLN CYS ASP VAL ALA GLU ASP ALA SER ILE ASP THR MET          
SEQRES  10 B  305  PHE ALA GLU LEU GLY LYS VAL TRP PRO LYS PHE ASP GLY          
SEQRES  11 B  305  PHE VAL HIS SER ILE GLY PHE ALA PRO GLY ASP GLN LEU          
SEQRES  12 B  305  ASP GLY ASP TYR VAL ASN ALA VAL THR ARG GLU GLY PHE          
SEQRES  13 B  305  LYS ILE ALA HIS ASP ILE SER SER TYR SER PHE VAL ALA          
SEQRES  14 B  305  MET ALA LYS ALA CYS ARG SER MET LEU ASN PRO GLY SER          
SEQRES  15 B  305  ALA LEU LEU THR LEU SER TYR LEU GLY ALA GLU ARG ALA          
SEQRES  16 B  305  ILE PRO ASN TYR ASN VAL MET GLY LEU ALA LYS ALA SER          
SEQRES  17 B  305  LEU GLU ALA ASN VAL ARG TYR MET ALA ASN ALA MET GLY          
SEQRES  18 B  305  PRO GLU GLY VAL ARG VAL ASN ALA ILE SER ALA GLY PRO          
SEQRES  19 B  305  ILE ARG THR LEU ALA ALA SER GLY ILE LYS ASP PHE ARG          
SEQRES  20 B  305  LYS MET LEU ALA HIS CYS GLU ALA VAL THR PRO ILE ARG          
SEQRES  21 B  305  ARG THR VAL THR ILE GLU ASP VAL GLY ASN SER ALA ALA          
SEQRES  22 B  305  PHE LEU CYS SER ASP LEU SER ALA GLY ILE SER GLY GLU          
SEQRES  23 B  305  VAL VAL HIS VAL ASP GLY GLY PHE SER ILE ALA ALA MET          
SEQRES  24 B  305  ASN GLU LEU GLU LEU LYS                                      
FORMUL   3  HOH   *226(H2 O)                                                    
HELIX    1 AA1 SER A   19  GLU A   31  1                                  13    
HELIX    2 AA2 LEU A   44  LEU A   55  1                                  12    
HELIX    3 AA3 GLU A   67  TRP A   82  1                                  16    
HELIX    4 AA4 PRO A   96  ASP A  101  5                                   6    
HELIX    5 AA5 ASP A  103  VAL A  108  1                                   6    
HELIX    6 AA6 THR A  109  SER A  121  1                                  13    
HELIX    7 AA7 SER A  121  ARG A  132  1                                  12    
HELIX    8 AA8 TYR A  146  GLU A  150  5                                   5    
HELIX    9 AA9 ASN A  157  GLY A  178  1                                  22    
HELIX   10 AB1 PHE A  203  THR A  214  1                                  12    
HELIX   11 AB2 THR A  221  SER A  234  1                                  14    
HELIX   12 AB3 ASP A  235  ALA A  238  5                                   4    
HELIX   13 AB4 GLY A  250  ALA A  254  5                                   5    
HELIX   14 AB5 SER B   19  GLU B   31  1                                  13    
HELIX   15 AB6 ASN B   41  LYS B   43  5                                   3    
HELIX   16 AB7 LEU B   44  LEU B   55  1                                  12    
HELIX   17 AB8 GLU B   67  LYS B   80  1                                  14    
HELIX   18 AB9 PRO B   96  LEU B  100  5                                   5    
HELIX   19 AC1 ASP B  103  VAL B  108  1                                   6    
HELIX   20 AC2 THR B  109  SER B  121  1                                  13    
HELIX   21 AC3 SER B  121  ARG B  132  1                                  12    
HELIX   22 AC4 TYR B  146  GLU B  150  5                                   5    
HELIX   23 AC5 ASN B  157  GLY B  178  1                                  22    
HELIX   24 AC6 LYS B  205  THR B  214  1                                  10    
HELIX   25 AC7 THR B  221  SER B  234  1                                  14    
HELIX   26 AC8 ASP B  235  ALA B  238  5                                   4    
HELIX   27 AC9 GLY B  250  ALA B  254  5                                   5    
SHEET    1 AA1 7 VAL A  60  GLN A  62  0                                        
SHEET    2 AA1 7 GLU A  34  TYR A  39  1  N  PHE A  37   O  LEU A  61           
SHEET    3 AA1 7 ARG A   8  VAL A  11  1  N  VAL A  11   O  ALA A  36           
SHEET    4 AA1 7 PHE A  85  HIS A  90  1  O  ASP A  86   N  ARG A   8           
SHEET    5 AA1 7 LEU A 135  SER A 145  1  O  LEU A 142   N  HIS A  90           
SHEET    6 AA1 7 VAL A 182  ALA A 189  1  O  ILE A 187   N  SER A 145           
SHEET    7 AA1 7 VAL A 244  VAL A 247  1  O  VAL A 245   N  ALA A 186           
SHEET    1 AA2 7 VAL B  60  GLN B  62  0                                        
SHEET    2 AA2 7 GLU B  34  TYR B  39  1  N  PHE B  37   O  LEU B  61           
SHEET    3 AA2 7 ARG B   8  VAL B  11  1  N  VAL B  11   O  ALA B  36           
SHEET    4 AA2 7 PHE B  85  HIS B  90  1  O  ASP B  86   N  ARG B   8           
SHEET    5 AA2 7 LEU B 135  SER B 145  1  O  LEU B 142   N  HIS B  90           
SHEET    6 AA2 7 VAL B 182  ALA B 189  1  O  ILE B 187   N  SER B 145           
SHEET    7 AA2 7 VAL B 244  VAL B 247  1  O  VAL B 245   N  ALA B 186           
CRYST1   80.152   80.152  323.940  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      0.012476  0.007203  0.000000        0.00000                         
SCALE2      0.000000  0.014406  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003087        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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