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Database: PDB
Entry: 5CWA
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HEADER    LYASE/LYASE INHIBITOR                   28-JUL-15   5CWA              
TITLE     STRUCTURE OF ANTHRANILATE SYNTHASE COMPONENT I (TRPE) FROM            
TITLE    2 MYCOBACTERIUM TUBERCULOSIS WITH INHIBITOR BOUND                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANTHRANILATE SYNTHASE COMPONENT 1;                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ASI;                                                        
COMPND   5 EC: 4.1.3.27;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 OTHER_DETAILS: D TO H MUTATION FROM PUBLISHED SEQUENCE AT POSITION 2 
COMPND   9 DUE TO CLONING ARTEFACT, ALSO AFTER RTEV CLEAVAGE AN ADDITIONAL GA   
COMPND  10 REMAINS ON CONSTRUCT USED PRIOR TO START M (NOT SHOWN IN SEQUENCE    
COMPND  11 ABOVE)                                                               
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS (STRAIN CDC 1551 /   
SOURCE   3 OSHKOSH);                                                            
SOURCE   4 ORGANISM_TAXID: 83331;                                               
SOURCE   5 STRAIN: CDC 1551 / OSHKOSH;                                          
SOURCE   6 GENE: TRPE, MT1644;                                                  
SOURCE   7 EXPRESSION_SYSTEM: MYCOBACTERIUM SMEGMATIS;                          
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 1772                                        
KEYWDS    LYASE, INHIBITOR, LYASE-LYASE INHIBITOR COMPLEX                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.JOHNSTON,G.BASHIRI,G.L.EVANS,J.S.LOTT,E.N.BAKER                   
REVDAT   3   01-NOV-17 5CWA    1       REMARK                                   
REVDAT   2   18-NOV-15 5CWA    1       JRNL                                     
REVDAT   1   12-AUG-15 5CWA    0                                                
SPRSDE     12-AUG-15 5CWA      4PEN                                             
JRNL        AUTH   G.BASHIRI,J.M.JOHNSTON,G.L.EVANS,E.M.BULLOCH,D.C.GOLDSTONE,  
JRNL        AUTH 2 E.N.JIRGIS,S.KLEINBOELTING,A.CASTELL,R.J.RAMSAY,             
JRNL        AUTH 3 A.MANOS-TURVEY,R.J.PAYNE,J.S.LOTT,E.N.BAKER                  
JRNL        TITL   STRUCTURE AND INHIBITION OF SUBUNIT I OF THE ANTHRANILATE    
JRNL        TITL 2 SYNTHASE COMPLEX OF MYCOBACTERIUM TUBERCULOSIS AND           
JRNL        TITL 3 EXPRESSION OF THE ACTIVE COMPLEX.                            
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  71  2297 2015              
JRNL        REFN                   ESSN 1399-0047                               
JRNL        PMID   26527146                                                     
JRNL        DOI    10.1107/S1399004715017216                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0069                                      
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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 135.45                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 54282                          
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) : 0.209                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2767                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.16                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3748                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.57                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3610                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 187                          
REMARK   3   BIN FREE R VALUE                    : 0.3660                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3825                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 48                                      
REMARK   3   SOLVENT ATOMS            : 205                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.53                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.79000                                              
REMARK   3    B22 (A**2) : 0.79000                                              
REMARK   3    B33 (A**2) : -2.57000                                             
REMARK   3    B12 (A**2) : 0.40000                                              
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): 0.152         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.153         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.143         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.884         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3992 ; 0.012 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3761 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5448 ; 1.527 ; 1.975       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8614 ; 0.820 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   513 ; 6.789 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   178 ;33.997 ;23.146       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   607 ;16.515 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    39 ;17.422 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   623 ; 0.089 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4583 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   898 ; 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):  2031 ; 3.771 ; 5.479       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2030 ; 3.770 ; 5.477       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2539 ; 5.354 ; 8.201       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   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   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   4                                                                      
REMARK   4 5CWA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUL-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000212294.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-MAR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8983                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.20                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54312                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 135.452                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 21.90                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.15800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 22.40                              
REMARK 200  R MERGE FOR SHELL          (I) : 3.79400                            
REMARK 200  R SYM FOR SHELL            (I) : 3.79400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP 11.0.02                                        
REMARK 200 STARTING MODEL: 1QDL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.6-1.0 M AMMONIUM SULFATE, 0.1 M BIS    
REMARK 280  -TRIS PROPANE, PH 7, "SILVER BULLET" ADDITIVE G6, VAPOR             
REMARK 280  DIFFUSION, TEMPERATURE 291K, VAPOR DIFFUSION, HANGING DROP          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+1/3                                            
REMARK 290       6555   X-Y,X,Z+2/3                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+1/3                                            
REMARK 290      11555   -X+Y,Y,-Z                                               
REMARK 290      12555   X,X-Y,-Z+2/3                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.79467            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       85.58933            
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  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       42.79467            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       85.58933            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       42.79467            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       85.58933            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       42.79467            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       85.58933            
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 300 REMARK: BIOLOGICAL ASSEMBLY OF TRPE IS A DIMER. IN THE STRUCTURE     
REMARK 300 THIS DIMER IS GENERATED BY APPLICATION OF CRYSTAL SYMMETRY. THIS IS  
REMARK 300 SUPPORTED BY PISA ANALYSIS. ALSO FURTHER SUPPORTED BY EXPERIMENTAL   
REMARK 300 WORK - SEC AND SEC-MALS ANALYSIS.                                    
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13940 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 73510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -154.0 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 -1.000000  0.000000  0.000000       78.20300            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000     -135.45157            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000      -42.79467            
REMARK 350   BIOMT1   4  0.500000  0.866025  0.000000       78.20300            
REMARK 350   BIOMT2   4  0.866025 -0.500000  0.000000     -135.45157            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000      -42.79467            
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     GLY A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     ARG A   116                                                      
REMARK 465     GLN A   117                                                      
REMARK 465     SER A   118                                                      
REMARK 465     GLU A   119                                                      
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 226    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 330    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 340    CG   CD   CE   NZ                                   
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    ALA A  32       59.02   -145.56                                   
REMARK 500    SER A  62      112.29     80.37                                   
REMARK 500    SER A  62      112.29     81.09                                   
REMARK 500    ALA A  71       44.15    -96.98                                   
REMARK 500    THR A  78     -158.31   -145.27                                   
REMARK 500    GLU A 314       52.72     38.51                                   
REMARK 500    ARG A 330       73.40   -117.90                                   
REMARK 500    THR A 331     -138.79   -147.13                                   
REMARK 500    ASP A 332      -36.03    -35.74                                   
REMARK 500    SER A 417      -80.65   -147.23                                   
REMARK 500    ASN A 465       58.46     35.55                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR A  331     ASP A  332                 -140.03                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 905        DISTANCE =  6.48 ANGSTROMS                       
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 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 0GA A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 605                 
DBREF  5CWA A    1   511  UNP    P9WFX2   TRPE_MYCTO       1    511             
SEQADV 5CWA GLY A   -1  UNP  P9WFX2              EXPRESSION TAG                 
SEQADV 5CWA ALA A    0  UNP  P9WFX2              EXPRESSION TAG                 
SEQADV 5CWA ASP A    2  UNP  P9WFX2    HIS     2 ENGINEERED MUTATION            
SEQRES   1 A  513  GLY ALA MET ASP ALA ASP LEU ALA ALA THR THR SER ARG          
SEQRES   2 A  513  GLU ASP PHE ARG LEU LEU ALA ALA GLU HIS ARG VAL VAL          
SEQRES   3 A  513  PRO VAL THR ARG LYS VAL LEU ALA ASP SER GLU THR PRO          
SEQRES   4 A  513  LEU SER ALA TYR ARG LYS LEU ALA ALA ASN ARG PRO GLY          
SEQRES   5 A  513  THR PHE LEU LEU GLU SER ALA GLU ASN GLY ARG SER TRP          
SEQRES   6 A  513  SER ARG TRP SER PHE ILE GLY ALA GLY ALA PRO THR ALA          
SEQRES   7 A  513  LEU THR VAL ARG GLU GLY GLN ALA VAL TRP LEU GLY ALA          
SEQRES   8 A  513  VAL PRO LYS ASP ALA PRO THR GLY GLY ASP PRO LEU ARG          
SEQRES   9 A  513  ALA LEU GLN VAL THR LEU GLU LEU LEU ALA THR ALA ASP          
SEQRES  10 A  513  ARG GLN SER GLU PRO GLY LEU PRO PRO LEU SER GLY GLY          
SEQRES  11 A  513  MET VAL GLY PHE PHE ALA TYR ASP MET VAL ARG ARG LEU          
SEQRES  12 A  513  GLU ARG LEU PRO GLU ARG ALA VAL ASP ASP LEU CYS LEU          
SEQRES  13 A  513  PRO ASP MET LEU LEU LEU LEU ALA THR ASP VAL ALA ALA          
SEQRES  14 A  513  VAL ASP HIS HIS GLU GLY THR ILE THR LEU ILE ALA ASN          
SEQRES  15 A  513  ALA VAL ASN TRP ASN GLY THR ASP GLU ARG VAL ASP TRP          
SEQRES  16 A  513  ALA TYR ASP ASP ALA VAL ALA ARG LEU ASP VAL MET THR          
SEQRES  17 A  513  ALA ALA LEU GLY GLN PRO LEU PRO SER THR VAL ALA THR          
SEQRES  18 A  513  PHE SER ARG PRO GLU PRO ARG HIS ARG ALA GLN ARG THR          
SEQRES  19 A  513  VAL GLU GLU TYR GLY ALA ILE VAL GLU TYR LEU VAL ASP          
SEQRES  20 A  513  GLN ILE ALA ALA GLY GLU ALA PHE GLN VAL VAL PRO SER          
SEQRES  21 A  513  GLN ARG PHE GLU MET ASP THR ASP VAL ASP PRO ILE ASP          
SEQRES  22 A  513  VAL TYR ARG ILE LEU ARG VAL THR ASN PRO SER PRO TYR          
SEQRES  23 A  513  MET TYR LEU LEU GLN VAL PRO ASN SER ASP GLY ALA VAL          
SEQRES  24 A  513  ASP PHE SER ILE VAL GLY SER SER PRO GLU ALA LEU VAL          
SEQRES  25 A  513  THR VAL HIS GLU GLY TRP ALA THR THR HIS PRO ILE ALA          
SEQRES  26 A  513  GLY THR ARG TRP ARG GLY ARG THR ASP ASP GLU ASP VAL          
SEQRES  27 A  513  LEU LEU GLU LYS GLU LEU LEU ALA ASP ASP LYS GLU ARG          
SEQRES  28 A  513  ALA GLU HIS LEU MET LEU VAL ASP LEU GLY ARG ASN ASP          
SEQRES  29 A  513  LEU GLY ARG VAL CYS THR PRO GLY THR VAL ARG VAL GLU          
SEQRES  30 A  513  ASP TYR SER HIS ILE GLU ARG TYR SER HIS VAL MET HIS          
SEQRES  31 A  513  LEU VAL SER THR VAL THR GLY LYS LEU GLY GLU GLY ARG          
SEQRES  32 A  513  THR ALA LEU ASP ALA VAL THR ALA CYS PHE PRO ALA GLY          
SEQRES  33 A  513  THR LEU SER GLY ALA PRO LYS VAL ARG ALA MET GLU LEU          
SEQRES  34 A  513  ILE GLU GLU VAL GLU LYS THR ARG ARG GLY LEU TYR GLY          
SEQRES  35 A  513  GLY VAL VAL GLY TYR LEU ASP PHE ALA GLY ASN ALA ASP          
SEQRES  36 A  513  PHE ALA ILE ALA ILE ARG THR ALA LEU MET ARG ASN GLY          
SEQRES  37 A  513  THR ALA TYR VAL GLN ALA GLY GLY GLY VAL VAL ALA ASP          
SEQRES  38 A  513  SER ASN GLY SER TYR GLU TYR ASN GLU ALA ARG ASN LYS          
SEQRES  39 A  513  ALA ARG ALA VAL LEU ASN ALA ILE ALA ALA ALA GLU THR          
SEQRES  40 A  513  LEU ALA ALA PRO GLY ALA                                      
HET    SO4  A 601       5                                                       
HET    SO4  A 602       5                                                       
HET    GOL  A 603       6                                                       
HET    0GA  A 604      17                                                       
HET    GOL  A 605       6                                                       
HET    UNL  A 606       9                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM     0GA 3-{[(1Z)-1-CARBOXYPROP-1-EN-1-YL]OXY}-2-HYDROXYBENZOIC           
HETNAM   2 0GA  ACID                                                            
HETNAM     UNL UNKNOWN LIGAND                                                   
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  SO4    2(O4 S 2-)                                                   
FORMUL   4  GOL    2(C3 H8 O3)                                                  
FORMUL   5  0GA    C11 H10 O6                                                   
FORMUL   8  HOH   *205(H2 O)                                                    
HELIX    1 AA1 SER A   10  HIS A   21  1                                  12    
HELIX    2 AA2 THR A   36  ALA A   45  1                                  10    
HELIX    3 AA3 ALA A   57  ARG A   61  5                                   5    
HELIX    4 AA4 ASP A   99  LEU A  111  1                                  13    
HELIX    5 AA5 TYR A  135  LEU A  141  5                                   7    
HELIX    6 AA6 ARG A  190  GLN A  211  1                                  22    
HELIX    7 AA7 THR A  232  ALA A  249  1                                  18    
HELIX    8 AA8 ASP A  268  ASN A  280  1                                  13    
HELIX    9 AA9 ASP A  332  ASP A  345  1                                  14    
HELIX   10 AB1 ASP A  345  ARG A  365  1                                  21    
HELIX   11 AB2 THR A  402  PHE A  411  1                                  10    
HELIX   12 AB3 ALA A  413  LEU A  416  5                                   4    
HELIX   13 AB4 PRO A  420  GLU A  432  1                                  13    
HELIX   14 AB5 ASN A  481  GLU A  504  1                                  24    
SHEET    1 AA111 VAL A  23  LEU A  31  0                                        
SHEET    2 AA111 THR A 174  VAL A 182 -1  O  ALA A 181   N  VAL A  24           
SHEET    3 AA111 ASP A 164  ASP A 169 -1  N  VAL A 165   O  ILE A 178           
SHEET    4 AA111 TRP A  66  ALA A  71 -1  N  SER A  67   O  VAL A 168           
SHEET    5 AA111 THR A  51  GLU A  55 -1  N  PHE A  52   O  GLY A  70           
SHEET    6 AA111 TYR A 284  PRO A 291 -1  O  MET A 285   N  GLU A  55           
SHEET    7 AA111 VAL A 297  SER A 305 -1  O  PHE A 299   N  VAL A 290           
SHEET    8 AA111 THR A 460  ARG A 464 -1  O  MET A 463   N  SER A 300           
SHEET    9 AA111 THR A 467  GLY A 473 -1  O  THR A 467   N  ARG A 464           
SHEET   10 AA111 SER A 258  ASP A 264 -1  N  MET A 263   O  ALA A 468           
SHEET   11 AA111 ARG A 228  ALA A 229 -1  N  ARG A 228   O  GLU A 262           
SHEET    1 AA210 GLN A  83  LEU A  87  0                                        
SHEET    2 AA210 ALA A  76  ARG A  80 -1  N  THR A  78   O  VAL A  85           
SHEET    3 AA210 MET A 157  ALA A 162 -1  O  LEU A 159   N  LEU A  77           
SHEET    4 AA210 GLY A 128  PHE A 133 -1  N  VAL A 130   O  LEU A 160           
SHEET    5 AA210 VAL A 442  ASP A 447 -1  O  LEU A 446   N  MET A 129           
SHEET    6 AA210 ALA A 452  ILE A 456 -1  O  ALA A 455   N  VAL A 443           
SHEET    7 AA210 ALA A 308  HIS A 313 -1  N  LEU A 309   O  PHE A 454           
SHEET    8 AA210 TRP A 316  THR A 319 -1  O  THR A 318   N  THR A 311           
SHEET    9 AA210 VAL A 386  LYS A 396 -1  O  VAL A 393   N  THR A 319           
SHEET   10 AA210 ILE A 322  TRP A 327 -1  N  ARG A 326   O  MET A 387           
SHEET    1 AA310 GLN A  83  LEU A  87  0                                        
SHEET    2 AA310 ALA A  76  ARG A  80 -1  N  THR A  78   O  VAL A  85           
SHEET    3 AA310 MET A 157  ALA A 162 -1  O  LEU A 159   N  LEU A  77           
SHEET    4 AA310 GLY A 128  PHE A 133 -1  N  VAL A 130   O  LEU A 160           
SHEET    5 AA310 VAL A 442  ASP A 447 -1  O  LEU A 446   N  MET A 129           
SHEET    6 AA310 ALA A 452  ILE A 456 -1  O  ALA A 455   N  VAL A 443           
SHEET    7 AA310 ALA A 308  HIS A 313 -1  N  LEU A 309   O  PHE A 454           
SHEET    8 AA310 TRP A 316  THR A 319 -1  O  THR A 318   N  THR A 311           
SHEET    9 AA310 VAL A 386  LYS A 396 -1  O  VAL A 393   N  THR A 319           
SHEET   10 AA310 ARG A 373  ARG A 382 -1  N  HIS A 379   O  VAL A 390           
SHEET    1 AA4 2 GLN A 254  VAL A 255  0                                        
SHEET    2 AA4 2 GLY A 418  ALA A 419 -1  O  ALA A 419   N  GLN A 254           
CISPEP   1 ARG A  330    THR A  331          0        -3.81                     
CISPEP   2 PHE A  411    PRO A  412          0        -8.79                     
CISPEP   3 ALA A  419    PRO A  420          0        -7.43                     
SITE     1 AC1  5 TYR A 383  SER A 384  HIS A 385  VAL A 386                    
SITE     2 AC1  5 ARG A 459                                                     
SITE     1 AC2  4 ARG A 147  ARG A 231  LYS A 433  HOH A 701                    
SITE     1 AC3 10 LYS A  92  ASP A  93  PRO A  95  THR A  96                    
SITE     2 AC3 10 ARG A 365  CYS A 367  PRO A 369  ARG A 401                    
SITE     3 AC3 10 HOH A 750  HOH A 778                                          
SITE     1 AC4  7 THR A 415  TYR A 439  ALA A 472  GLY A 473                    
SITE     2 AC4  7 LYS A 492  HOH A 721  HOH A 831                               
SITE     1 AC5  8 LEU A 152  ARG A 436  LEU A 438  TYR A 439                    
SITE     2 AC5  8 THR A 460  TYR A 469  VAL A 470  GLN A 471                    
CRYST1  156.406  156.406  128.384  90.00  90.00 120.00 P 64 2 2     12          
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      0.006394  0.003691  0.000000        0.00000                         
SCALE2      0.000000  0.007383  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007789        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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