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LongText Report for: 1MNA-pdb

Name Class
1MNA-pdb
HEADER    TRANSFERASE                             05-SEP-02   1MNA              
TITLE     THIOESTERASE DOMAIN OF PICROMYCIN POLYKETIDE SYNTHASE (PICS           
TITLE    2 TE), PH 8.0                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POLYKETIDE SYNTHASE IV;                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: THIOESTERASE DOMAIN;                                       
COMPND   5 SYNONYM: PICROMYCIN POLYKETIDE SYNTHASE; PIKAIV; TYPE I              
COMPND   6 POLYKETIDE SYNTHASE PIKAIV;                                          
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES VENEZUELAE;                        
SOURCE   3 ORGANISM_COMMON: BACTERIA;                                           
SOURCE   4 GENE: PICAIV;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_COMMON: BACTERIA;                                  
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    THIOESTERASE, POLYKETIDE SYNTHASE, OPEN SUBSTRATE CHANNEL,            
KEYWDS   2 ALPHA-BETA HYDROLASE                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.-C.TSAI,H.LU,D.E.CANE,C.KHOSLA,R.M.STROUD                           
REVDAT   1   04-FEB-03 1MNA    0                                                
JRNL        AUTH   S.-C.TSAI,H.LU,D.E.CANE,C.KHOSLA,R.M.STROUD                  
JRNL        TITL   INSIGHTS INTO CHANNEL ARCHITECTURE AND SUBSTRATE             
JRNL        TITL 2 SPECIFICITY FROM CRYSTAL STRUCTURES OF TWO                   
JRNL        TITL 3 MACROCYCLE-FORMING THIOESTERASES OF MODULAR                  
JRNL        TITL 4 POLYKETIDE SYNTHASES                                         
JRNL        REF    BIOCHEMISTRY                  V.  41 12598 2002              
JRNL        REFN   ASTM BICHAW  US ISSN 0006-2960                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 1.80 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.28                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 70844                          
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 SET) : 0.236                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3608                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.91                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 83.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 9747                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3220                       
REMARK   3   BIN FREE R VALUE                    : 0.3430                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 509                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.015                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4193                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 313                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -7.02000                                             
REMARK   3    B22 (A**2) : -2.85000                                             
REMARK   3    B33 (A**2) : 9.87000                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.28                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.28                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.85                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.36                                                 
REMARK   3   BSOL        : 40.34                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1MNA COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PRAGUE ON 19-SEP-2002.              
REMARK 100 THE RCSB ID CODE IS RCSB017035.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-NOV-2001                        
REMARK 200  TEMPERATURE           (KELVIN) : 190.0                              
REMARK 200  PH                             : 8.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : 9-2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 75591                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 9.100                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 31.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.0                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M LITHIUM SULFATE, 100 MM TRIS, 2      
REMARK 280  MM DTT, PH 8.0, VAPOR DIFFUSION, SITTING DROP AT 298K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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   1/2-X,1/2+Y,-Z                                          
REMARK 290       4555   1/2+X,1/2-Y,-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        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       54.02900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       65.29650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       54.02900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       65.29650            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR                     
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).                
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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 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 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     SER A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ASP A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     THR A   109                                                      
REMARK 465     GLY A   110                                                      
REMARK 465     THR A   111                                                      
REMARK 465     GLY A   112                                                      
REMARK 465     THR A   113                                                      
REMARK 465     ILE A   290                                                      
REMARK 465     GLU A   291                                                      
REMARK 465     GLY A   292                                                      
REMARK 465     ILE A   293                                                      
REMARK 465     GLU A   294                                                      
REMARK 465     GLY A   295                                                      
REMARK 465     ALA A   296                                                      
REMARK 465     GLY A   297                                                      
REMARK 465     LYS A   298                                                      
REMARK 465     SER B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     ASP B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     GLY B     6                                                      
REMARK 465     ALA B     7                                                      
REMARK 465     GLY B     8                                                      
REMARK 465     THR B   109                                                      
REMARK 465     GLY B   110                                                      
REMARK 465     THR B   111                                                      
REMARK 465     GLY B   112                                                      
REMARK 465     THR B   113                                                      
REMARK 465     GLY B   292                                                      
REMARK 465     ILE B   293                                                      
REMARK 465     GLU B   294                                                      
REMARK 465     GLY B   295                                                      
REMARK 465     ALA B   296                                                      
REMARK 465     GLY B   297                                                      
REMARK 465     LYS B   298                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)                  
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PRO A 179   CD    PRO A 179   CG     0.034                        
REMARK 500    PRO B 177   CD    PRO B 177   CG     0.035                        
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: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  98   N   -  CA  -  C   ANGL. DEV. = -8.3 DEGREES           
REMARK 500    ARG A 163   N   -  CA  -  C   ANGL. DEV. =  8.1 DEGREES           
REMARK 500    ALA A 199   N   -  CA  -  C   ANGL. DEV. = -7.8 DEGREES           
REMARK 500    GLY A 226   N   -  CA  -  C   ANGL. DEV. =  9.6 DEGREES           
REMARK 500    GLU B  85   N   -  CA  -  C   ANGL. DEV. =  9.4 DEGREES           
REMARK 500    ASP B  98   N   -  CA  -  C   ANGL. DEV. = -8.1 DEGREES           
REMARK 500    GLY B 108   N   -  CA  -  C   ANGL. DEV. =  7.2 DEGREES           
REMARK 500    VAL B 143   N   -  CA  -  C   ANGL. DEV. = -7.4 DEGREES           
REMARK 500    LEU B 233   N   -  CA  -  C   ANGL. DEV. = -7.5 DEGREES           
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  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 148     -118.31     54.87                                   
REMARK 500    THR B 115      -72.69     78.81                                   
REMARK 500    SER B 148     -117.66     56.31                                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1KEZ   RELATED DB: PDB                                   
REMARK 900 THIOESTERASE DOMAIN FROM 6-DEOXYERYTHRONOLIDE SYNTHASE               
REMARK 900 (DEBS TE), PH 7.2                                                    
REMARK 900 RELATED ID: 1MN6   RELATED DB: PDB                                   
REMARK 900 THIOESTERASE DOMAIN FROM PICROMYCIN POLYKETIDE SYNTHASE              
REMARK 900 (PICS TE), PH 7.6                                                    
REMARK 900 RELATED ID: MNQ   RELATED DB: PDB                                    
REMARK 900 THIOESTERASE DOMAIN FROM PICROMYCIN POLYKETIDE SYNTHASE              
REMARK 900 (PICS), PH 8.0                                                       
REMARK 900 RELATED ID: MO2   RELATED DB: PDB                                    
REMARK 900 THIOESTERASE DOMAIN FROM PICROMYCIN POLYKETIDE SYNTHASE              
REMARK 900 (PICS), PH 8.4                                                       
DBREF  1MNA A    1   298  PIR    T17412   T17412        1049   1346             
DBREF  1MNA B    1   298  PIR    T17412   T17412        1049   1346             
SEQRES   1 A  298  SER GLY ALA ASP THR GLY ALA GLY ALA GLY MET PHE ARG          
SEQRES   2 A  298  ALA LEU PHE ARG GLN ALA VAL GLU ASP ASP ARG TYR GLY          
SEQRES   3 A  298  GLU PHE LEU ASP VAL LEU ALA GLU ALA SER ALA PHE ARG          
SEQRES   4 A  298  PRO GLN PHE ALA SER PRO GLU ALA CYS SER GLU ARG LEU          
SEQRES   5 A  298  ASP PRO VAL LEU LEU ALA GLY GLY PRO THR ASP ARG ALA          
SEQRES   6 A  298  GLU GLY ARG ALA VAL LEU VAL GLY CYS THR GLY THR ALA          
SEQRES   7 A  298  ALA ASN GLY GLY PRO HIS GLU PHE LEU ARG LEU SER THR          
SEQRES   8 A  298  SER PHE GLN GLU GLU ARG ASP PHE LEU ALA VAL PRO LEU          
SEQRES   9 A  298  PRO GLY TYR GLY THR GLY THR GLY THR GLY THR ALA LEU          
SEQRES  10 A  298  LEU PRO ALA ASP LEU ASP THR ALA LEU ASP ALA GLN ALA          
SEQRES  11 A  298  ARG ALA ILE LEU ARG ALA ALA GLY ASP ALA PRO VAL VAL          
SEQRES  12 A  298  LEU LEU GLY HIS SER GLY GLY ALA LEU LEU ALA HIS GLU          
SEQRES  13 A  298  LEU ALA PHE ARG LEU GLU ARG ALA HIS GLY ALA PRO PRO          
SEQRES  14 A  298  ALA GLY ILE VAL LEU VAL ASP PRO TYR PRO PRO GLY HIS          
SEQRES  15 A  298  GLN GLU PRO ILE GLU VAL TRP SER ARG GLN LEU GLY GLU          
SEQRES  16 A  298  GLY LEU PHE ALA GLY GLU LEU GLU PRO MET SER ASP ALA          
SEQRES  17 A  298  ARG LEU LEU ALA MET GLY ARG TYR ALA ARG PHE LEU ALA          
SEQRES  18 A  298  GLY PRO ARG PRO GLY ARG SER SER ALA PRO VAL LEU LEU          
SEQRES  19 A  298  VAL ARG ALA SER GLU PRO LEU GLY ASP TRP GLN GLU GLU          
SEQRES  20 A  298  ARG GLY ASP TRP ARG ALA HIS TRP ASP LEU PRO HIS THR          
SEQRES  21 A  298  VAL ALA ASP VAL PRO GLY ASP HIS PHE THR MET MET ARG          
SEQRES  22 A  298  ASP HIS ALA PRO ALA VAL ALA GLU ALA VAL LEU SER TRP          
SEQRES  23 A  298  LEU ASP ALA ILE GLU GLY ILE GLU GLY ALA GLY LYS              
SEQRES   1 B  298  SER GLY ALA ASP THR GLY ALA GLY ALA GLY MET PHE ARG          
SEQRES   2 B  298  ALA LEU PHE ARG GLN ALA VAL GLU ASP ASP ARG TYR GLY          
SEQRES   3 B  298  GLU PHE LEU ASP VAL LEU ALA GLU ALA SER ALA PHE ARG          
SEQRES   4 B  298  PRO GLN PHE ALA SER PRO GLU ALA CYS SER GLU ARG LEU          
SEQRES   5 B  298  ASP PRO VAL LEU LEU ALA GLY GLY PRO THR ASP ARG ALA          
SEQRES   6 B  298  GLU GLY ARG ALA VAL LEU VAL GLY CYS THR GLY THR ALA          
SEQRES   7 B  298  ALA ASN GLY GLY PRO HIS GLU PHE LEU ARG LEU SER THR          
SEQRES   8 B  298  SER PHE GLN GLU GLU ARG ASP PHE LEU ALA VAL PRO LEU          
SEQRES   9 B  298  PRO GLY TYR GLY THR GLY THR GLY THR GLY THR ALA LEU          
SEQRES  10 B  298  LEU PRO ALA ASP LEU ASP THR ALA LEU ASP ALA GLN ALA          
SEQRES  11 B  298  ARG ALA ILE LEU ARG ALA ALA GLY ASP ALA PRO VAL VAL          
SEQRES  12 B  298  LEU LEU GLY HIS SER GLY GLY ALA LEU LEU ALA HIS GLU          
SEQRES  13 B  298  LEU ALA PHE ARG LEU GLU ARG ALA HIS GLY ALA PRO PRO          
SEQRES  14 B  298  ALA GLY ILE VAL LEU VAL ASP PRO TYR PRO PRO GLY HIS          
SEQRES  15 B  298  GLN GLU PRO ILE GLU VAL TRP SER ARG GLN LEU GLY GLU          
SEQRES  16 B  298  GLY LEU PHE ALA GLY GLU LEU GLU PRO MET SER ASP ALA          
SEQRES  17 B  298  ARG LEU LEU ALA MET GLY ARG TYR ALA ARG PHE LEU ALA          
SEQRES  18 B  298  GLY PRO ARG PRO GLY ARG SER SER ALA PRO VAL LEU LEU          
SEQRES  19 B  298  VAL ARG ALA SER GLU PRO LEU GLY ASP TRP GLN GLU GLU          
SEQRES  20 B  298  ARG GLY ASP TRP ARG ALA HIS TRP ASP LEU PRO HIS THR          
SEQRES  21 B  298  VAL ALA ASP VAL PRO GLY ASP HIS PHE THR MET MET ARG          
SEQRES  22 B  298  ASP HIS ALA PRO ALA VAL ALA GLU ALA VAL LEU SER TRP          
SEQRES  23 B  298  LEU ASP ALA ILE GLU GLY ILE GLU GLY ALA GLY LYS              
FORMUL   3  HOH   *313(H2 O1)                                                   
HELIX    1   1 GLY A   10  ASP A   22  1                                  13    
HELIX    2   2 ARG A   24  ALA A   37  1                                  14    
HELIX    3   3 SER A   44  CYS A   48  5                                   5    
HELIX    4   4 PHE A   86  SER A   92  1                                   7    
HELIX    5   5 ASP A  121  GLY A  138  1                                  18    
HELIX    6   6 SER A  148  HIS A  165  1                                  18    
HELIX    7   7 GLN A  183  TRP A  189  1                                   7    
HELIX    8   8 TRP A  189  ALA A  199  1                                  11    
HELIX    9   9 SER A  206  GLY A  222  1                                  17    
HELIX   10  10 GLN A  245  GLY A  249  5                                   5    
HELIX   11  11 PHE A  269  ASP A  274  1                                   6    
HELIX   12  12 HIS A  275  ALA A  289  1                                  15    
HELIX   13  13 GLY B   10  ASP B   22  1                                  13    
HELIX   14  14 ARG B   24  ALA B   37  1                                  14    
HELIX   15  15 SER B   44  CYS B   48  5                                   5    
HELIX   16  16 PHE B   86  SER B   92  1                                   7    
HELIX   17  17 ASP B  121  GLY B  138  1                                  18    
HELIX   18  18 SER B  148  HIS B  165  1                                  18    
HELIX   19  19 GLN B  183  TRP B  189  1                                   7    
HELIX   20  20 TRP B  189  ALA B  199  1                                  11    
HELIX   21  21 SER B  206  GLY B  222  1                                  17    
HELIX   22  22 GLN B  245  GLY B  249  5                                   5    
HELIX   23  23 PHE B  269  ARG B  273  5                                   5    
HELIX   24  24 HIS B  275  GLU B  291  1                                  17    
SHEET    1   A 2 GLN A  41  PHE A  42  0                                        
SHEET    2   A 2 LEU A 118  PRO A 119  1  O  LEU A 118   N  PHE A  42           
SHEET    1   B 7 VAL A  55  ALA A  58  0                                        
SHEET    2   B 7 PHE A  99  VAL A 102 -1  O  ALA A 101   N  VAL A  55           
SHEET    3   B 7 VAL A  70  CYS A  74  1  N  LEU A  71   O  LEU A 100           
SHEET    4   B 7 VAL A 142  HIS A 147  1  O  LEU A 145   N  VAL A  72           
SHEET    5   B 7 GLY A 171  VAL A 175  1  O  VAL A 173   N  LEU A 144           
SHEET    6   B 7 VAL A 232  ALA A 237  1  O  LEU A 233   N  ILE A 172           
SHEET    7   B 7 THR A 260  VAL A 264  1  O  ALA A 262   N  LEU A 234           
SHEET    1   C 2 GLN B  41  PHE B  42  0                                        
SHEET    2   C 2 LEU B 118  PRO B 119  1  O  LEU B 118   N  PHE B  42           
SHEET    1   D 7 VAL B  55  ALA B  58  0                                        
SHEET    2   D 7 PHE B  99  VAL B 102 -1  O  ALA B 101   N  VAL B  55           
SHEET    3   D 7 VAL B  70  CYS B  74  1  N  GLY B  73   O  LEU B 100           
SHEET    4   D 7 VAL B 142  HIS B 147  1  O  VAL B 143   N  VAL B  72           
SHEET    5   D 7 GLY B 171  VAL B 175  1  O  VAL B 173   N  LEU B 144           
SHEET    6   D 7 VAL B 232  ALA B 237  1  O  LEU B 233   N  LEU B 174           
SHEET    7   D 7 THR B 260  VAL B 264  1  O  THR B 260   N  LEU B 234           
CRYST1  108.058  130.593   56.750  90.00  90.00  90.00 P 21 21 2     8          
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      0.009254  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007657  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017621        0.00000                         
TER    2088      ALA A 289                                                      
TER    4193      GLU B 291                                                      
MASTER      329    0    0   24   18    0    0    6 4504    2    0   46          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
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