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Database: PDB
Entry: 3L60
LinkDB: 3L60
Original site: 3L60 
HEADER    OXIDOREDUCTASE                          22-DEC-09   3L60              
TITLE     CRYSTAL STRUCTURE OF BRANCHED-CHAIN ALPHA-KETO ACID                   
TITLE    2 DEHYDROGENASE SUBUNIT E2 FROM MYCOBACTERIUM TUBERCULOSIS             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE;              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: C-TERMINAL FRAGMENT, RESIDUES 155-393;                     
COMPND   5 SYNONYM: PROBABLE DIHYDROLIPOAMIDE S-ACETYLTRANSFERASE E2            
COMPND   6 COMPONENT PDHC (LIPOATE ACETYLTRANSFERASE)                           
COMPND   7 (THIOLTRANSACETYLASE A);                                             
COMPND   8 EC: 2.3.1.12;                                                        
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 1773;                                                
SOURCE   4 GENE: PDHC, RV2495C;                                                 
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    STRUCTURAL GENOMICS, PSI-2, DEHYDROGENASE, PROTEIN STRUCTURE          
KEYWDS   2 INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL              
KEYWDS   3 GENOMICS, NYSGXRC                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.D.ZENCHECK,J.B.BONNANO,Y.PATSKOVSKY,R.TORO,J.FREEMAN,               
AUTHOR   2 J.M.SAUDER,S.K.BURLEY,S.C.ALMO,NEW YORK SGX RESEARCH CENTER          
AUTHOR   3 FOR STRUCTURAL GENOMICS (NYSGXRC)                                    
REVDAT   1   05-JAN-10 3L60    0                                                
JRNL        AUTH   W.D.ZENCHECK,J.B.BONNANO,Y.PATSKOVSKY,R.TORO,                
JRNL        AUTH 2 J.FREEMAN,J.M.SAUDER,S.K.BURLEY,S.C.ALMO                     
JRNL        TITL   CRYSTAL STRUCTURE OF BRANCHED-CHAIN ALPHA-KETO ACID          
JRNL        TITL 2 DEHYDROGENASE SUBUNIT E2 FROM MYCOBACTERIUM                  
JRNL        TITL 3 TUBERCULOSIS                                                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0089                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 17990                          
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) : 0.184                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 979                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1323                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1970                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 65                           
REMARK   3   BIN FREE R VALUE                    : 0.2050                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1703                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 9                                       
REMARK   3   SOLVENT ATOMS            : 140                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.68                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.155         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.145         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.093         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.247         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1744 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1144 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2380 ; 1.448 ; 1.975       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2803 ; 0.921 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   230 ; 6.088 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    66 ;32.842 ;23.182       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   275 ;13.900 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;25.315 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   292 ; 0.077 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1950 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   334 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1143 ; 0.921 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   465 ; 0.208 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1846 ; 1.633 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   601 ; 2.142 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   533 ; 3.545 ; 4.500       
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 : BABINET MODEL WITH 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: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3L60 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-DEC-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB056876.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-NOV-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18995                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -5.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 19.100                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 19.10                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.36000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELX                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 60% TASCIMATE, PH 7, 10% GLYCEROL,       
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z,-X,-Y                                                 
REMARK 290       7555   -Z,-X,Y                                                 
REMARK 290       8555   -Z,X,-Y                                                 
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z,-X                                                 
REMARK 290      11555   Y,-Z,-X                                                 
REMARK 290      12555   -Y,-Z,X                                                 
REMARK 290      13555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      14555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      15555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      16555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      17555   Z+1/2,X+1/2,Y+1/2                                       
REMARK 290      18555   Z+1/2,-X+1/2,-Y+1/2                                     
REMARK 290      19555   -Z+1/2,-X+1/2,Y+1/2                                     
REMARK 290      20555   -Z+1/2,X+1/2,-Y+1/2                                     
REMARK 290      21555   Y+1/2,Z+1/2,X+1/2                                       
REMARK 290      22555   -Y+1/2,Z+1/2,-X+1/2                                     
REMARK 290      23555   Y+1/2,-Z+1/2,-X+1/2                                     
REMARK 290      24555   -Y+1/2,-Z+1/2,X+1/2                                     
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000       59.38200            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       59.38200            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       59.38200            
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000       59.38200            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       59.38200            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       59.38200            
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       59.38200            
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000       59.38200            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       59.38200            
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000       59.38200            
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000       59.38200            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       59.38200            
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000       59.38200            
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       59.38200            
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       59.38200            
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000       59.38200            
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000       59.38200            
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       59.38200            
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000       59.38200            
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       59.38200            
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000       59.38200            
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000       59.38200            
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000       59.38200            
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000       59.38200            
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000       59.38200            
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       59.38200            
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       59.38200            
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000       59.38200            
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000       59.38200            
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000       59.38200            
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000       59.38200            
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000       59.38200            
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       59.38200            
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000       59.38200            
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       59.38200            
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000       59.38200            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT3   3  1.000000  0.000000  0.000000        0.00000            
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   8  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A  51  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   152                                                      
REMARK 465     SER A   153                                                      
REMARK 465     LEU A   154                                                      
REMARK 465     ALA A   155                                                      
REMARK 465     ALA A   156                                                      
REMARK 465     ALA A   157                                                      
REMARK 465     ARG A   158                                                      
REMARK 465     GLY A   159                                                      
REMARK 465     GLY A   160                                                      
REMARK 465     VAL A   161                                                      
REMARK 465     GLY A   162                                                      
REMARK 465     ALA A   163                                                      
REMARK 465     GLY A   164                                                      
REMARK 465     GLU A   394                                                      
REMARK 465     GLY A   395                                                      
REMARK 465     HIS A   396                                                      
REMARK 465     HIS A   397                                                      
REMARK 465     HIS A   398                                                      
REMARK 465     HIS A   399                                                      
REMARK 465     HIS A   400                                                      
REMARK 465     HIS A   401                                                      
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     ARG A 176    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 186    CG   CD   CE   NZ                                   
REMARK 470     SER A 243    OG                                                  
REMARK 470     GLU A 245    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 265    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 388    OG1  CG2                                            
REMARK 470     LEU A 391    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 237       79.53   -118.74                                   
REMARK 500    GLU A 245       39.44    -99.91                                   
REMARK 500    PRO A 329       30.93    -91.01                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: NYSGXRC-13665A   RELATED DB: TARGETDB                    
DBREF  3L60 A  154   393  UNP    O06159   O06159_MYCTU   154    393             
SEQADV 3L60 MET A  152  UNP  O06159              EXPRESSION TAG                 
SEQADV 3L60 SER A  153  UNP  O06159              EXPRESSION TAG                 
SEQADV 3L60 GLU A  394  UNP  O06159              EXPRESSION TAG                 
SEQADV 3L60 GLY A  395  UNP  O06159              EXPRESSION TAG                 
SEQADV 3L60 HIS A  396  UNP  O06159              EXPRESSION TAG                 
SEQADV 3L60 HIS A  397  UNP  O06159              EXPRESSION TAG                 
SEQADV 3L60 HIS A  398  UNP  O06159              EXPRESSION TAG                 
SEQADV 3L60 HIS A  399  UNP  O06159              EXPRESSION TAG                 
SEQADV 3L60 HIS A  400  UNP  O06159              EXPRESSION TAG                 
SEQADV 3L60 HIS A  401  UNP  O06159              EXPRESSION TAG                 
SEQRES   1 A  250  MET SER LEU ALA ALA ALA ARG GLY GLY VAL GLY ALA GLY          
SEQRES   2 A  250  PRO ASP VAL ARG PRO VAL HIS GLY VAL HIS ALA ARG MET          
SEQRES   3 A  250  ALA GLU LYS MET THR LEU SER HIS LYS GLU ILE PRO THR          
SEQRES   4 A  250  ALA LYS ALA SER VAL GLU VAL ILE CYS ALA GLU LEU LEU          
SEQRES   5 A  250  ARG LEU ARG ASP ARG PHE VAL SER ALA ALA PRO GLU ILE          
SEQRES   6 A  250  THR PRO PHE ALA LEU THR LEU ARG LEU LEU VAL ILE ALA          
SEQRES   7 A  250  LEU LYS HIS ASN VAL ILE LEU ASN SER THR TRP VAL ASP          
SEQRES   8 A  250  SER GLY GLU GLY PRO GLN VAL HIS VAL HIS ARG GLY VAL          
SEQRES   9 A  250  HIS LEU GLY PHE GLY ALA ALA THR GLU ARG GLY LEU LEU          
SEQRES  10 A  250  VAL PRO VAL VAL THR ASP ALA GLN ASP LYS ASN THR ARG          
SEQRES  11 A  250  GLU LEU ALA SER ARG VAL ALA GLU LEU ILE THR GLY ALA          
SEQRES  12 A  250  ARG GLU GLY THR LEU THR PRO ALA GLU LEU ARG GLY SER          
SEQRES  13 A  250  THR PHE THR VAL SER ASN PHE GLY ALA LEU GLY VAL ASP          
SEQRES  14 A  250  ASP GLY VAL PRO VAL ILE ASN HIS PRO GLU ALA ALA ILE          
SEQRES  15 A  250  LEU GLY LEU GLY ALA ILE LYS PRO ARG PRO VAL VAL VAL          
SEQRES  16 A  250  GLY GLY GLU VAL VAL ALA ARG PRO THR MET THR LEU THR          
SEQRES  17 A  250  CYS VAL PHE ASP HIS ARG VAL VAL ASP GLY ALA GLN VAL          
SEQRES  18 A  250  ALA GLN PHE MET CYS GLU LEU ARG ASP LEU ILE GLU SER          
SEQRES  19 A  250  PRO GLU THR ALA LEU LEU ASP LEU GLU GLY HIS HIS HIS          
SEQRES  20 A  250  HIS HIS HIS                                                  
HET    UNL  A   1       9                                                       
HETNAM     UNL UNKNOWN LIGAND                                                   
FORMUL   3  HOH   *140(H2 O)                                                    
HELIX    1   1 HIS A  171  ILE A  188  1                                  18    
HELIX    2   2 CYS A  199  VAL A  210  1                                  12    
HELIX    3   3 THR A  217  ASN A  233  1                                  17    
HELIX    4   4 VAL A  234  LEU A  236  5                                   3    
HELIX    5   5 ASP A  274  LYS A  278  5                                   5    
HELIX    6   6 ASN A  279  GLY A  297  1                                  19    
HELIX    7   7 THR A  300  ARG A  305  5                                   6    
HELIX    8   8 ASN A  313  GLY A  318  5                                   6    
HELIX    9   9 ASP A  368  SER A  385  1                                  18    
HELIX   10  10 SER A  385  LEU A  390  1                                   6    
SHEET    1   A 6 THR A 190  ILE A 198  0                                        
SHEET    2   A 6 GLU A 349  ASP A 363 -1  O  CYS A 360   N  ALA A 193           
SHEET    3   A 6 ALA A 332  LEU A 336 -1  N  GLY A 335   O  THR A 359           
SHEET    4   A 6 PHE A 309  SER A 312  1  N  SER A 312   O  LEU A 334           
SHEET    5   A 6 LEU A 257  PHE A 259  1  N  GLY A 258   O  PHE A 309           
SHEET    6   A 6 VAL A 271  VAL A 272 -1  O  VAL A 272   N  LEU A 257           
SHEET    1   B 3 THR A 190  ILE A 198  0                                        
SHEET    2   B 3 GLU A 349  ASP A 363 -1  O  CYS A 360   N  ALA A 193           
SHEET    3   B 3 LYS A 340  VAL A 346 -1  N  VAL A 344   O  VAL A 351           
SHEET    1   C 2 SER A 238  VAL A 241  0                                        
SHEET    2   C 2 GLN A 248  VAL A 251 -1  O  GLN A 248   N  VAL A 241           
SHEET    1   D 2 ALA A 261  THR A 263  0                                        
SHEET    2   D 2 GLY A 266  LEU A 268 -1  O  LEU A 268   N  ALA A 261           
CISPEP   1 HIS A  328    PRO A  329          0        -1.98                     
CRYST1  118.764  118.764  118.764  90.00  90.00  90.00 I 2 3        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      0.008420  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008420  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008420        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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