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Database: PDB
Entry: 3FMI
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Original site: 3FMI 
HEADER    LIGASE                                  22-DEC-08   3FMI              
TITLE     CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS DETHIOBIOTIN          
TITLE    2 SYNTHETASE COMPLEXED WITH 7-KETO 8-AMINOPELARGONIC ACID              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DETHIOBIOTIN SYNTHETASE;                                   
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: DTB SYNTHETASE, DTBS;                                       
COMPND   5 EC: 6.3.3.3;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 1773;                                                
SOURCE   4 STRAIN: H37RV;                                                       
SOURCE   5 GENE: BIOD, MT1621, MTCY336.33C, RV1570;                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28B                                    
KEYWDS    RV1570, BIOD, LIGASE, ATP-BINDING, BIOTIN BIOSYNTHESIS, MAGNESIUM,    
KEYWDS   2 NUCLEOTIDE-BINDING                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.DEY,J.C.SACCHETTINI                                                 
REVDAT   3   06-SEP-23 3FMI    1       REMARK SEQADV LINK                       
REVDAT   2   25-AUG-10 3FMI    1       JRNL                                     
REVDAT   1   30-JUN-09 3FMI    0                                                
JRNL        AUTH   S.DEY,J.M.LANE,R.E.LEE,E.J.RUBIN,J.C.SACCHETTINI             
JRNL        TITL   STRUCTURAL CHARACTERIZATION OF THE MYCOBACTERIUM             
JRNL        TITL 2 TUBERCULOSIS BIOTIN BIOSYNTHESIS ENZYMES                     
JRNL        TITL 3 7,8-DIAMINOPELARGONIC ACID SYNTHASE AND DETHIOBIOTIN         
JRNL        TITL 4 SYNTHETASE .                                                 
JRNL        REF    BIOCHEMISTRY                  V.  49  6746 2010              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   20565114                                                     
JRNL        DOI    10.1021/BI902097J                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.18 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.18                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 43644                          
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) : 0.216                           
REMARK   3   R VALUE            (WORKING SET) : 0.214                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2323                            
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) : 2.18                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.23                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3087                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.82                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2890                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 168                          
REMARK   3   BIN FREE R VALUE                    : 0.3700                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6328                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 59                                      
REMARK   3   SOLVENT ATOMS            : 210                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.93000                                              
REMARK   3    B22 (A**2) : 1.01000                                              
REMARK   3    B33 (A**2) : -1.94000                                             
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): 0.296         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.230         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.173         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.688         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6462 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8834 ; 1.471 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   902 ; 6.122 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   205 ;35.318 ;23.366       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   927 ;19.368 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    52 ;18.636 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1109 ; 0.093 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4795 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2858 ; 0.224 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4405 ; 0.315 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   544 ; 0.188 ; 0.500       
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):    61 ; 0.224 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.241 ; 0.500       
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):  4575 ; 2.811 ; 5.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7100 ; 4.046 ; 7.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2050 ; 5.563 ; 9.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1734 ; 7.052 ;11.000       
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   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
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   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3FMI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JAN-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000050772.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 120                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.541                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46066                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.180                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 13.90                              
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 38.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.18                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.50                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.39000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.330                              
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: PDB ENTRY 3FGN                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5, VAPOR DIFFUSION, HANGING DROP,   
REMARK 280  TEMPERATURE 291K                                                    
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       27.68600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.78450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.56850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       75.78450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.68600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.56850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3250 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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   -24                                                      
REMARK 465     GLY A   -23                                                      
REMARK 465     SER A   -22                                                      
REMARK 465     SER A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     SER A   -14                                                      
REMARK 465     SER A   -13                                                      
REMARK 465     GLY A   -12                                                      
REMARK 465     LEU A   -11                                                      
REMARK 465     GLN A   -10                                                      
REMARK 465     GLY A    -9                                                      
REMARK 465     THR A    -8                                                      
REMARK 465     GLU A    -7                                                      
REMARK 465     ASN A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     MET B   -24                                                      
REMARK 465     GLY B   -23                                                      
REMARK 465     SER B   -22                                                      
REMARK 465     SER B   -21                                                      
REMARK 465     HIS B   -20                                                      
REMARK 465     HIS B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     SER B   -14                                                      
REMARK 465     SER B   -13                                                      
REMARK 465     GLY B   -12                                                      
REMARK 465     LEU B   -11                                                      
REMARK 465     GLN B   -10                                                      
REMARK 465     GLY B    -9                                                      
REMARK 465     THR B    -8                                                      
REMARK 465     GLU B    -7                                                      
REMARK 465     ASN B    -6                                                      
REMARK 465     LEU B    -5                                                      
REMARK 465     TYR B    -4                                                      
REMARK 465     PHE B    -3                                                      
REMARK 465     GLN B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B   226                                                      
REMARK 465     MET C   -24                                                      
REMARK 465     GLY C   -23                                                      
REMARK 465     SER C   -22                                                      
REMARK 465     SER C   -21                                                      
REMARK 465     HIS C   -20                                                      
REMARK 465     HIS C   -19                                                      
REMARK 465     HIS C   -18                                                      
REMARK 465     HIS C   -17                                                      
REMARK 465     HIS C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     SER C   -14                                                      
REMARK 465     SER C   -13                                                      
REMARK 465     GLY C   -12                                                      
REMARK 465     LEU C   -11                                                      
REMARK 465     GLN C   -10                                                      
REMARK 465     GLY C    -9                                                      
REMARK 465     THR C    -8                                                      
REMARK 465     GLU C    -7                                                      
REMARK 465     ASN C    -6                                                      
REMARK 465     LEU C    -5                                                      
REMARK 465     TYR C    -4                                                      
REMARK 465     PHE C    -3                                                      
REMARK 465     GLN C    -2                                                      
REMARK 465     GLY C   226                                                      
REMARK 465     MET D   -24                                                      
REMARK 465     GLY D   -23                                                      
REMARK 465     SER D   -22                                                      
REMARK 465     SER D   -21                                                      
REMARK 465     HIS D   -20                                                      
REMARK 465     HIS D   -19                                                      
REMARK 465     HIS D   -18                                                      
REMARK 465     HIS D   -17                                                      
REMARK 465     HIS D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     SER D   -14                                                      
REMARK 465     SER D   -13                                                      
REMARK 465     GLY D   -12                                                      
REMARK 465     LEU D   -11                                                      
REMARK 465     GLN D   -10                                                      
REMARK 465     GLY D    -9                                                      
REMARK 465     THR D    -8                                                      
REMARK 465     GLU D    -7                                                      
REMARK 465     ASN D    -6                                                      
REMARK 465     LEU D    -5                                                      
REMARK 465     TYR D    -4                                                      
REMARK 465     PHE D    -3                                                      
REMARK 465     GLN D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLY D   226                                                      
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 193   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A 193   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG D 125   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 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    LEU A  65      -78.72   -146.18                                   
REMARK 500    ALA B  84      167.66    -48.03                                   
REMARK 500    PRO B  86      173.91    -58.29                                   
REMARK 500    MET C   1      128.24    -21.17                                   
REMARK 500    LEU C  65      -78.77   -140.93                                   
REMARK 500    LEU C 143      117.64    -31.61                                   
REMARK 500    PRO C 174     -103.31    -14.28                                   
REMARK 500    ALA D  84      168.01    -48.73                                   
REMARK 500    PRO D 101      126.39    -35.36                                   
REMARK 500    PRO D 175     -138.07    -55.54                                   
REMARK 500    ALA D 200      -56.41    -20.67                                   
REMARK 500    ALA D 201       -4.89    -52.31                                   
REMARK 500    ALA D 205      -66.21    169.71                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 250                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KAP A 430                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KAP B 430                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 251                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 253                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KAP C 430                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 252                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3FGN   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF DETHIOBIOTIN SYNTHETASE FROM MYCOBACTERIUM TUBERCULOSIS 
REMARK 900 RELATED ID: 3FMF   RELATED DB: PDB                                   
DBREF  3FMI A    1   226  UNP    O06620   BIOD_MYCTU       1    226             
DBREF  3FMI B    1   226  UNP    O06620   BIOD_MYCTU       1    226             
DBREF  3FMI C    1   226  UNP    O06620   BIOD_MYCTU       1    226             
DBREF  3FMI D    1   226  UNP    O06620   BIOD_MYCTU       1    226             
SEQADV 3FMI MET A  -24  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI GLY A  -23  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI SER A  -22  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI SER A  -21  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS A  -20  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS A  -19  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS A  -18  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS A  -17  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS A  -16  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS A  -15  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI SER A  -14  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI SER A  -13  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI GLY A  -12  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI LEU A  -11  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI GLN A  -10  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI GLY A   -9  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI THR A   -8  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI GLU A   -7  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI ASN A   -6  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI LEU A   -5  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI TYR A   -4  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI PHE A   -3  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI GLN A   -2  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI SER A   -1  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS A    0  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI MET B  -24  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI GLY B  -23  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI SER B  -22  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI SER B  -21  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS B  -20  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS B  -19  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS B  -18  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS B  -17  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS B  -16  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS B  -15  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI SER B  -14  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI SER B  -13  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI GLY B  -12  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI LEU B  -11  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI GLN B  -10  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI GLY B   -9  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI THR B   -8  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI GLU B   -7  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI ASN B   -6  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI LEU B   -5  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI TYR B   -4  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI PHE B   -3  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI GLN B   -2  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI SER B   -1  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS B    0  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI MET C  -24  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI GLY C  -23  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI SER C  -22  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI SER C  -21  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS C  -20  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS C  -19  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS C  -18  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS C  -17  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS C  -16  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS C  -15  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI SER C  -14  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI SER C  -13  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI GLY C  -12  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI LEU C  -11  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI GLN C  -10  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI GLY C   -9  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI THR C   -8  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI GLU C   -7  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI ASN C   -6  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI LEU C   -5  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI TYR C   -4  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI PHE C   -3  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI GLN C   -2  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI SER C   -1  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS C    0  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI MET D  -24  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI GLY D  -23  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI SER D  -22  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI SER D  -21  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS D  -20  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS D  -19  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS D  -18  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS D  -17  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS D  -16  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS D  -15  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI SER D  -14  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI SER D  -13  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI GLY D  -12  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI LEU D  -11  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI GLN D  -10  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI GLY D   -9  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI THR D   -8  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI GLU D   -7  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI ASN D   -6  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI LEU D   -5  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI TYR D   -4  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI PHE D   -3  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI GLN D   -2  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI SER D   -1  UNP  O06620              EXPRESSION TAG                 
SEQADV 3FMI HIS D    0  UNP  O06620              EXPRESSION TAG                 
SEQRES   1 A  251  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  251  LEU GLN GLY THR GLU ASN LEU TYR PHE GLN SER HIS MET          
SEQRES   3 A  251  THR ILE LEU VAL VAL THR GLY THR GLY THR GLY VAL GLY          
SEQRES   4 A  251  LYS THR VAL VAL CYS ALA ALA LEU ALA SER ALA ALA ARG          
SEQRES   5 A  251  GLN ALA GLY ILE ASP VAL ALA VAL CYS LYS PRO VAL GLN          
SEQRES   6 A  251  THR GLY THR ALA ARG GLY ASP ASP ASP LEU ALA GLU VAL          
SEQRES   7 A  251  GLY ARG LEU ALA GLY VAL THR GLN LEU ALA GLY LEU ALA          
SEQRES   8 A  251  ARG TYR PRO GLN PRO MET ALA PRO ALA ALA ALA ALA GLU          
SEQRES   9 A  251  HIS ALA GLY MET ALA LEU PRO ALA ARG ASP GLN ILE VAL          
SEQRES  10 A  251  ARG LEU ILE ALA ASP LEU ASP ARG PRO GLY ARG LEU THR          
SEQRES  11 A  251  LEU VAL GLU GLY ALA GLY GLY LEU LEU VAL GLU LEU ALA          
SEQRES  12 A  251  GLU PRO GLY VAL THR LEU ARG ASP VAL ALA VAL ASP VAL          
SEQRES  13 A  251  ALA ALA ALA ALA LEU VAL VAL VAL THR ALA ASP LEU GLY          
SEQRES  14 A  251  THR LEU ASN HIS THR LYS LEU THR LEU GLU ALA LEU ALA          
SEQRES  15 A  251  ALA GLN GLN VAL SER CSX ALA GLY LEU VAL ILE GLY SER          
SEQRES  16 A  251  TRP PRO ASP PRO PRO GLY LEU VAL ALA ALA SER ASN ARG          
SEQRES  17 A  251  SER ALA LEU ALA ARG ILE ALA MET VAL ARG ALA ALA LEU          
SEQRES  18 A  251  PRO ALA GLY ALA ALA SER LEU ASP ALA GLY ASP PHE ALA          
SEQRES  19 A  251  ALA MET SER ALA ALA ALA PHE ASP ARG ASN TRP VAL ALA          
SEQRES  20 A  251  GLY LEU VAL GLY                                              
SEQRES   1 B  251  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  251  LEU GLN GLY THR GLU ASN LEU TYR PHE GLN SER HIS MET          
SEQRES   3 B  251  THR ILE LEU VAL VAL THR GLY THR GLY THR GLY VAL GLY          
SEQRES   4 B  251  LYS THR VAL VAL CYS ALA ALA LEU ALA SER ALA ALA ARG          
SEQRES   5 B  251  GLN ALA GLY ILE ASP VAL ALA VAL CYS LYS PRO VAL GLN          
SEQRES   6 B  251  THR GLY THR ALA ARG GLY ASP ASP ASP LEU ALA GLU VAL          
SEQRES   7 B  251  GLY ARG LEU ALA GLY VAL THR GLN LEU ALA GLY LEU ALA          
SEQRES   8 B  251  ARG TYR PRO GLN PRO MET ALA PRO ALA ALA ALA ALA GLU          
SEQRES   9 B  251  HIS ALA GLY MET ALA LEU PRO ALA ARG ASP GLN ILE VAL          
SEQRES  10 B  251  ARG LEU ILE ALA ASP LEU ASP ARG PRO GLY ARG LEU THR          
SEQRES  11 B  251  LEU VAL GLU GLY ALA GLY GLY LEU LEU VAL GLU LEU ALA          
SEQRES  12 B  251  GLU PRO GLY VAL THR LEU ARG ASP VAL ALA VAL ASP VAL          
SEQRES  13 B  251  ALA ALA ALA ALA LEU VAL VAL VAL THR ALA ASP LEU GLY          
SEQRES  14 B  251  THR LEU ASN HIS THR LYS LEU THR LEU GLU ALA LEU ALA          
SEQRES  15 B  251  ALA GLN GLN VAL SER CSX ALA GLY LEU VAL ILE GLY SER          
SEQRES  16 B  251  TRP PRO ASP PRO PRO GLY LEU VAL ALA ALA SER ASN ARG          
SEQRES  17 B  251  SER ALA LEU ALA ARG ILE ALA MET VAL ARG ALA ALA LEU          
SEQRES  18 B  251  PRO ALA GLY ALA ALA SER LEU ASP ALA GLY ASP PHE ALA          
SEQRES  19 B  251  ALA MET SER ALA ALA ALA PHE ASP ARG ASN TRP VAL ALA          
SEQRES  20 B  251  GLY LEU VAL GLY                                              
SEQRES   1 C  251  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  251  LEU GLN GLY THR GLU ASN LEU TYR PHE GLN SER HIS MET          
SEQRES   3 C  251  THR ILE LEU VAL VAL THR GLY THR GLY THR GLY VAL GLY          
SEQRES   4 C  251  LYS THR VAL VAL CYS ALA ALA LEU ALA SER ALA ALA ARG          
SEQRES   5 C  251  GLN ALA GLY ILE ASP VAL ALA VAL CYS LYS PRO VAL GLN          
SEQRES   6 C  251  THR GLY THR ALA ARG GLY ASP ASP ASP LEU ALA GLU VAL          
SEQRES   7 C  251  GLY ARG LEU ALA GLY VAL THR GLN LEU ALA GLY LEU ALA          
SEQRES   8 C  251  ARG TYR PRO GLN PRO MET ALA PRO ALA ALA ALA ALA GLU          
SEQRES   9 C  251  HIS ALA GLY MET ALA LEU PRO ALA ARG ASP GLN ILE VAL          
SEQRES  10 C  251  ARG LEU ILE ALA ASP LEU ASP ARG PRO GLY ARG LEU THR          
SEQRES  11 C  251  LEU VAL GLU GLY ALA GLY GLY LEU LEU VAL GLU LEU ALA          
SEQRES  12 C  251  GLU PRO GLY VAL THR LEU ARG ASP VAL ALA VAL ASP VAL          
SEQRES  13 C  251  ALA ALA ALA ALA LEU VAL VAL VAL THR ALA ASP LEU GLY          
SEQRES  14 C  251  THR LEU ASN HIS THR LYS LEU THR LEU GLU ALA LEU ALA          
SEQRES  15 C  251  ALA GLN GLN VAL SER CSX ALA GLY LEU VAL ILE GLY SER          
SEQRES  16 C  251  TRP PRO ASP PRO PRO GLY LEU VAL ALA ALA SER ASN ARG          
SEQRES  17 C  251  SER ALA LEU ALA ARG ILE ALA MET VAL ARG ALA ALA LEU          
SEQRES  18 C  251  PRO ALA GLY ALA ALA SER LEU ASP ALA GLY ASP PHE ALA          
SEQRES  19 C  251  ALA MET SER ALA ALA ALA PHE ASP ARG ASN TRP VAL ALA          
SEQRES  20 C  251  GLY LEU VAL GLY                                              
SEQRES   1 D  251  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  251  LEU GLN GLY THR GLU ASN LEU TYR PHE GLN SER HIS MET          
SEQRES   3 D  251  THR ILE LEU VAL VAL THR GLY THR GLY THR GLY VAL GLY          
SEQRES   4 D  251  LYS THR VAL VAL CYS ALA ALA LEU ALA SER ALA ALA ARG          
SEQRES   5 D  251  GLN ALA GLY ILE ASP VAL ALA VAL CYS LYS PRO VAL GLN          
SEQRES   6 D  251  THR GLY THR ALA ARG GLY ASP ASP ASP LEU ALA GLU VAL          
SEQRES   7 D  251  GLY ARG LEU ALA GLY VAL THR GLN LEU ALA GLY LEU ALA          
SEQRES   8 D  251  ARG TYR PRO GLN PRO MET ALA PRO ALA ALA ALA ALA GLU          
SEQRES   9 D  251  HIS ALA GLY MET ALA LEU PRO ALA ARG ASP GLN ILE VAL          
SEQRES  10 D  251  ARG LEU ILE ALA ASP LEU ASP ARG PRO GLY ARG LEU THR          
SEQRES  11 D  251  LEU VAL GLU GLY ALA GLY GLY LEU LEU VAL GLU LEU ALA          
SEQRES  12 D  251  GLU PRO GLY VAL THR LEU ARG ASP VAL ALA VAL ASP VAL          
SEQRES  13 D  251  ALA ALA ALA ALA LEU VAL VAL VAL THR ALA ASP LEU GLY          
SEQRES  14 D  251  THR LEU ASN HIS THR LYS LEU THR LEU GLU ALA LEU ALA          
SEQRES  15 D  251  ALA GLN GLN VAL SER CSX ALA GLY LEU VAL ILE GLY SER          
SEQRES  16 D  251  TRP PRO ASP PRO PRO GLY LEU VAL ALA ALA SER ASN ARG          
SEQRES  17 D  251  SER ALA LEU ALA ARG ILE ALA MET VAL ARG ALA ALA LEU          
SEQRES  18 D  251  PRO ALA GLY ALA ALA SER LEU ASP ALA GLY ASP PHE ALA          
SEQRES  19 D  251  ALA MET SER ALA ALA ALA PHE ASP ARG ASN TRP VAL ALA          
SEQRES  20 D  251  GLY LEU VAL GLY                                              
MODRES 3FMI CSX A  163  CYS  S-OXY CYSTEINE                                     
MODRES 3FMI CSX B  163  CYS  S-OXY CYSTEINE                                     
MODRES 3FMI CSX C  163  CYS  S-OXY CYSTEINE                                     
MODRES 3FMI CSX D  163  CYS  S-OXY CYSTEINE                                     
HET    CSX  A 163       7                                                       
HET    CSX  B 163       7                                                       
HET    CSX  C 163       7                                                       
HET    CSX  D 163       7                                                       
HET    SO4  A 250       5                                                       
HET    KAP  A 430      13                                                       
HET    KAP  B 430      13                                                       
HET    SO4  B 251       5                                                       
HET    SO4  C 253       5                                                       
HET    KAP  C 430      13                                                       
HET    SO4  D 252       5                                                       
HETNAM     CSX S-OXY CYSTEINE                                                   
HETNAM     SO4 SULFATE ION                                                      
HETNAM     KAP 7-KETO-8-AMINOPELARGONIC ACID                                    
FORMUL   1  CSX    4(C3 H7 N O3 S)                                              
FORMUL   5  SO4    4(O4 S 2-)                                                   
FORMUL   6  KAP    3(C9 H17 N O3)                                               
FORMUL  12  HOH   *210(H2 O)                                                    
HELIX    1   1 GLY A   14  ALA A   29  1                                  16    
HELIX    2   2 THR A   43  GLY A   46  5                                   4    
HELIX    3   3 ASP A   48  GLY A   58  1                                  11    
HELIX    4   4 ALA A   73  ALA A   81  1                                   9    
HELIX    5   5 ALA A   87  ASP A   97  1                                  11    
HELIX    6   6 LEU A  124  VAL A  131  1                                   8    
HELIX    7   7 GLY A  144  GLN A  159  1                                  16    
HELIX    8   8 GLY A  176  ALA A  190  1                                  15    
HELIX    9   9 GLY A  199  LEU A  203  5                                   5    
HELIX   10  10 ASP A  204  PHE A  216  1                                  13    
HELIX   11  11 ASP A  217  GLY A  223  1                                   7    
HELIX   12  12 LEU A  224  GLY A  226  5                                   3    
HELIX   13  13 GLY B   14  ALA B   29  1                                  16    
HELIX   14  14 ASP B   48  GLY B   58  1                                  11    
HELIX   15  15 ALA B   73  GLY B   82  1                                  10    
HELIX   16  16 ALA B   87  ASP B   99  1                                  13    
HELIX   17  17 LEU B  124  VAL B  131  1                                   8    
HELIX   18  18 GLY B  144  GLN B  159  1                                  16    
HELIX   19  19 GLY B  176  ALA B  190  1                                  15    
HELIX   20  20 GLY B  199  LEU B  203  5                                   5    
HELIX   21  21 ASP B  204  PHE B  216  1                                  13    
HELIX   22  22 ASP B  217  LEU B  224  1                                   8    
HELIX   23  23 GLY C   14  ALA C   29  1                                  16    
HELIX   24  24 GLY C   42  GLY C   46  5                                   5    
HELIX   25  25 ASP C   48  ALA C   57  1                                  10    
HELIX   26  26 ALA C   73  ALA C   81  1                                   9    
HELIX   27  27 ALA C   87  ASP C   97  1                                  11    
HELIX   28  28 THR C  123  VAL C  131  1                                   9    
HELIX   29  29 GLY C  144  ALA C  158  1                                  15    
HELIX   30  30 GLY C  176  ALA C  190  1                                  15    
HELIX   31  31 GLY C  199  LEU C  203  5                                   5    
HELIX   32  32 ASP C  204  PHE C  216  1                                  13    
HELIX   33  33 ASP C  217  GLY C  223  1                                   7    
HELIX   34  34 GLY D   14  ALA D   29  1                                  16    
HELIX   35  35 ASP D   48  GLY D   58  1                                  11    
HELIX   36  36 ALA D   73  GLY D   82  1                                  10    
HELIX   37  37 ALA D   87  LEU D   98  1                                  12    
HELIX   38  38 LEU D  124  ALA D  132  1                                   9    
HELIX   39  39 GLY D  144  GLN D  159  1                                  16    
HELIX   40  40 GLY D  176  ALA D  190  1                                  15    
HELIX   41  41 GLY D  199  LEU D  203  5                                   5    
HELIX   42  42 ALA D  205  PHE D  216  1                                  12    
HELIX   43  43 ASP D  217  GLY D  223  1                                   7    
SHEET    1   A 7 GLN A  61  TYR A  68  0                                        
SHEET    2   A 7 VAL A  33  THR A  41  1  N  VAL A  35   O  GLN A  61           
SHEET    3   A 7 LEU A 104  GLU A 108  1  O  LEU A 106   N  CYS A  36           
SHEET    4   A 7 THR A   2  GLY A   8  1  N  VAL A   6   O  VAL A 107           
SHEET    5   A 7 ALA A 134  VAL A 139  1  O  LEU A 136   N  VAL A   5           
SHEET    6   A 7 CSX A 163  TRP A 171  1  O  ALA A 164   N  ALA A 135           
SHEET    7   A 7 VAL A 192  PRO A 197  1  O  ARG A 193   N  LEU A 166           
SHEET    1   B 2 GLU A 116  ALA A 118  0                                        
SHEET    2   B 2 VAL A 122  THR A 123 -1  O  VAL A 122   N  LEU A 117           
SHEET    1   C 7 GLN B  61  ALA B  63  0                                        
SHEET    2   C 7 ASP B  32  CYS B  36  1  N  VAL B  35   O  GLN B  61           
SHEET    3   C 7 ARG B 103  GLY B 112  1  O  LEU B 106   N  CYS B  36           
SHEET    4   C 7 ILE B   3  GLY B   8  1  N  VAL B   6   O  VAL B 107           
SHEET    5   C 7 ALA B 134  VAL B 139  1  O  VAL B 138   N  THR B   7           
SHEET    6   C 7 CSX B 163  TRP B 171  1  O  VAL B 167   N  VAL B 139           
SHEET    7   C 7 VAL B 192  PRO B 197  1  O  LEU B 196   N  TRP B 171           
SHEET    1   D 2 VAL B  39  THR B  41  0                                        
SHEET    2   D 2 ALA B  66  TYR B  68  1  O  TYR B  68   N  GLN B  40           
SHEET    1   E 2 GLU B 116  ALA B 118  0                                        
SHEET    2   E 2 VAL B 122  THR B 123 -1  O  VAL B 122   N  LEU B 117           
SHEET    1   F 7 LEU C  62  ARG C  67  0                                        
SHEET    2   F 7 VAL C  33  GLN C  40  1  N  LYS C  37   O  ALA C  63           
SHEET    3   F 7 LEU C 104  GLU C 108  1  O  LEU C 106   N  CYS C  36           
SHEET    4   F 7 THR C   2  GLY C   8  1  N  THR C   2   O  THR C 105           
SHEET    5   F 7 ALA C 134  VAL C 139  1  O  LEU C 136   N  VAL C   5           
SHEET    6   F 7 CSX C 163  TRP C 171  1  O  ALA C 164   N  ALA C 135           
SHEET    7   F 7 VAL C 192  PRO C 197  1  O  LEU C 196   N  TRP C 171           
SHEET    1   G 7 GLN D  61  ALA D  63  0                                        
SHEET    2   G 7 ASP D  32  CYS D  36  1  N  VAL D  35   O  GLN D  61           
SHEET    3   G 7 ARG D 103  GLY D 112  1  O  LEU D 106   N  CYS D  36           
SHEET    4   G 7 ILE D   3  GLY D   8  1  N  VAL D   6   O  VAL D 107           
SHEET    5   G 7 ALA D 134  VAL D 139  1  O  VAL D 138   N  THR D   7           
SHEET    6   G 7 CSX D 163  TRP D 171  1  O  ALA D 164   N  ALA D 135           
SHEET    7   G 7 VAL D 192  PRO D 197  1  O  ARG D 193   N  LEU D 166           
SHEET    1   H 2 VAL D  39  THR D  41  0                                        
SHEET    2   H 2 ALA D  66  TYR D  68  1  O  TYR D  68   N  GLN D  40           
SHEET    1   I 2 GLU D 116  ALA D 118  0                                        
SHEET    2   I 2 VAL D 122  THR D 123 -1  O  VAL D 122   N  LEU D 117           
LINK         C   SER A 162                 N   CSX A 163     1555   1555  1.33  
LINK         C   CSX A 163                 N   ALA A 164     1555   1555  1.34  
LINK         C   SER B 162                 N   CSX B 163     1555   1555  1.32  
LINK         C   CSX B 163                 N   ALA B 164     1555   1555  1.33  
LINK         C   SER C 162                 N   CSX C 163     1555   1555  1.33  
LINK         C   CSX C 163                 N   ALA C 164     1555   1555  1.33  
LINK         C   SER D 162                 N   CSX D 163     1555   1555  1.33  
LINK         C   CSX D 163                 N   ALA D 164     1555   1555  1.33  
CISPEP   1 GLU A  119    PRO A  120          0         0.78                     
CISPEP   2 ASP A  173    PRO A  174          0        -5.80                     
CISPEP   3 ALA B  110    GLY B  111          0       -25.41                     
CISPEP   4 GLU B  119    PRO B  120          0       -11.82                     
CISPEP   5 ASP B  173    PRO B  174          0        -6.16                     
CISPEP   6 GLU C  119    PRO C  120          0        -7.20                     
CISPEP   7 ASP C  173    PRO C  174          0         7.50                     
CISPEP   8 PRO C  174    PRO C  175          0        20.89                     
CISPEP   9 GLU D  119    PRO D  120          0        -5.79                     
CISPEP  10 ASP D  173    PRO D  174          0        -3.73                     
SITE     1 AC1  6 GLY A  12  VAL A  13  GLY A  14  LYS A  15                    
SITE     2 AC1  6 THR A  16  HOH A 272                                          
SITE     1 AC2 10 LEU A 143  GLY A 144  THR A 145  LEU A 146                    
SITE     2 AC2 10 ASN A 147  THR B  11  THR B  41  PRO B  71                    
SITE     3 AC2 10 MET B  72  ALA B  73                                          
SITE     1 AC3 14 THR A  11  THR A  41  ASP A  47  PRO A  71                    
SITE     2 AC3 14 ALA A  73  VAL A 115  LEU B 143  GLY B 144                    
SITE     3 AC3 14 THR B 145  LEU B 146  ASN B 147  HOH B 227                    
SITE     4 AC3 14 HOH B 229  HOH B 230                                          
SITE     1 AC4  6 GLY B  12  VAL B  13  GLY B  14  LYS B  15                    
SITE     2 AC4  6 THR B  16  HOH B 234                                          
SITE     1 AC5  5 GLY C  12  VAL C  13  GLY C  14  LYS C  15                    
SITE     2 AC5  5 THR C  16                                                     
SITE     1 AC6 16 THR C  11  THR C  41  ARG C  45  ASP C  47                    
SITE     2 AC6 16 PRO C  71  MET C  72  ALA C  73  VAL C 115                    
SITE     3 AC6 16 HOH C 228  HOH C 247  HOH C 249  LEU D 143                    
SITE     4 AC6 16 GLY D 144  THR D 145  LEU D 146  ASN D 147                    
SITE     1 AC7  6 GLY D  12  VAL D  13  GLY D  14  LYS D  15                    
SITE     2 AC7  6 THR D  16  HOH D 241                                          
CRYST1   55.372  105.137  151.569  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      0.018060  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009511  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006598        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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