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LongText Report for: 1EXW-pdb

Name Class
1EXW-pdb
HEADER    HYDROLASE                               04-MAY-00   1EXW              
TITLE     CRYSTAL STRUCTURE OF PALMITOYL PROTEIN THIOESTERASE 1                 
TITLE    2 COMPLEXED WITH HEXADECYLSULFONYL FLUORIDE                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PALMITOYL PROTEIN THIOESTERASE 1;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.1.2.22;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: BOVINE;                                             
SOURCE   4 EXPRESSION_SYSTEM: BACULOVIRUS;                                      
SOURCE   5 EXPRESSION_SYSTEM_CELL: SF21 CELLS                                   
KEYWDS    ALPHA/BETA HYDROLASE, PALMITOYL PROTEIN THIOESTERASE, PMSF            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.J.BELLIZZI III,J.CLARDY                                             
REVDAT   1   02-AUG-00 1EXW    0                                                
JRNL        AUTH   A.K.DAS,J.J.BELLIZZI III,S.TANDEL,E.BIEHL,J.CLARDY,          
JRNL        AUTH 2 S.L.HOFMANN                                                  
JRNL        TITL   STRUCTURAL BASIS FOR THE INSENSITIVITY OF A SERINE           
JRNL        TITL 2 ENZYME (PALMITOYL-PROTEIN THIOESTERASE) TO                   
JRNL        TITL 3 PHENYLMETHANESULFONYL FLUORIDE                               
JRNL        REF    J.BIOL.CHEM.                  V. 275 23847 2000              
JRNL        REFN   ASTM JBCHA3  US ISSN 0021-9258                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.40 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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 : GENERATED PARAMETER/TOPOLOGY FILES              
REMARK   3                      FOR HDSF WITH XPLO2D                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.71                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 12638                          
REMARK   3                                                                      
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) : 0.243                           
REMARK   3   FREE R VALUE                     : 0.288                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 630                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.011                           
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.55                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1961                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3250                       
REMARK   3   BIN FREE R VALUE                    : 0.3790                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 100                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.038                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2210                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 75                                      
REMARK   3   SOLVENT ATOMS            : 40                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 54.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 7.13000                                              
REMARK   3    B22 (A**2) : 7.13000                                              
REMARK   3    B33 (A**2) : -14.27000                                            
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) : 0.36                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.340                           
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.48                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.49                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.70                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
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                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.33                                                 
REMARK   3   BSOL        : 51.33                                                
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  : PARAM                                          
REMARK   3  PARAMETER FILE  2  : PARAM                                          
REMARK   3  PARAMETER FILE  3  : PARAM                                          
REMARK   3  PARAMETER FILE  4  : HDS.PAR                                        
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  4   : HDS.TOP                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: USED SIMULATED ANNEALING,                 
REMARK   3  ENERGY MINIMIZATION, INDIVIDUAL B-FACTOR REFINEMENT. USED           
REMARK   3  ISOTROPIC B-FACTOR CORRECTION AND BULK SOLVENT CORRECTION           
REMARK   4                                                                      
REMARK   4 1EXW COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAY-2000.                
REMARK 100 THE RCSB ID CODE IS RCSB011005.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-FEB-1999                        
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9100                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM-4 CCD                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA, TRUNCATE                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 79642                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 36.270                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 7.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
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   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 55% PPG 400, 0.1 M BIS TRIS              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,1/2+Z                                             
REMARK 290       3555   -Y,X,1/4+Z                                              
REMARK 290       4555   Y,-X,3/4+Z                                              
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,1/2-Z                                              
REMARK 290       7555   Y,X,3/4-Z                                               
REMARK 290       8555   -Y,-X,1/4-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       64.01500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       32.00750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       96.02250            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       64.01500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       96.02250            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       32.00750            
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 1 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI                             
REMARK 500   OE2  GLU A   294     OH   TYR A   298              2.13            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH1  ARG A   191     OD2  ASP A    28     7545     2.15            
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    GLU A 286   CG    GLU A 286   CB    -0.119                        
REMARK 500    GLU A 286   CD    GLU A 286   CG     0.099                        
REMARK 500    HIS A 289   CG    HIS A 289   CB     0.059                        
REMARK 500    GLN A 291   CD    GLN A 291   CG    -0.067                        
REMARK 500    GLN A 291   OE1   GLN A 291   CD     0.080                        
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    HIS A  66   CB  -  CA  -  C   ANGL. DEV. =-11.9 DEGREES           
REMARK 500    PHE A  85   N   -  CA  -  C   ANGL. DEV. = 10.0 DEGREES           
REMARK 500    TRP A 186   N   -  CA  -  C   ANGL. DEV. = -9.4 DEGREES           
REMARK 500    GLU A 286   OE1 -  CD  -  OE2 ANGL. DEV. = -8.8 DEGREES           
REMARK 500    GLU A 286   CG  -  CD  -  OE2 ANGL. DEV. = 11.1 DEGREES           
REMARK 500    HIS A 289   CB  -  CA  -  C   ANGL. DEV. = -9.5 DEGREES           
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 BEFORE REACTION WITH THE PROTEIN, THE LIGAND                         
REMARK 600 HSF WAS 1-HEXADECYLSULFONYL FLUORIDE.  THE FLUORINE                  
REMARK 600 IS LOST DURING REACTION.  THE S1 OF HDR 430 IS                       
REMARK 600 COVALENTLY BOUND TO THE OG OF SER 115.                               
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1EI9   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PALMITOYL PROTEIN THIOESTERASE 1                
REMARK 900 RELATED ID: 1EH5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PALMITOYL PROTEIN THIOESTERASE 1                
REMARK 900 COMPLEXED WITH PALMITATE                                             
DBREF  1EXW A   28   306  SWS    P45478   PPT_BOVIN       28    306             
SEQRES   1 A  279  ASP PRO PRO ALA PRO LEU PRO LEU VAL ILE TRP HIS GLY          
SEQRES   2 A  279  MET GLY ASP SER CYS CYS ASN PRO LEU SER MET GLY ALA          
SEQRES   3 A  279  ILE LYS LYS MET VAL GLU LYS LYS ILE PRO GLY ILE HIS          
SEQRES   4 A  279  VAL LEU SER LEU GLU ILE GLY LYS THR LEU ARG GLU ASP          
SEQRES   5 A  279  VAL GLU ASN SER PHE PHE LEU ASN VAL ASN SER GLN VAL          
SEQRES   6 A  279  THR THR VAL CYS GLN ILE LEU ALA LYS ASP PRO LYS LEU          
SEQRES   7 A  279  GLN GLN GLY TYR ASN ALA MET GLY PHE SER GLN GLY GLY          
SEQRES   8 A  279  GLN PHE LEU ARG ALA VAL ALA GLN ARG CYS PRO SER PRO          
SEQRES   9 A  279  PRO MET VAL ASN LEU ILE SER VAL GLY GLY GLN HIS GLN          
SEQRES  10 A  279  GLY VAL PHE GLY LEU PRO ARG CYS PRO GLY GLU SER SER          
SEQRES  11 A  279  HIS ILE CYS ASP PHE ILE ARG LYS THR LEU ASN ALA GLY          
SEQRES  12 A  279  ALA TYR ASN LYS ALA ILE GLN GLU ARG LEU VAL GLN ALA          
SEQRES  13 A  279  GLU TYR TRP HIS ASP PRO ILE ARG GLU ASP ILE TYR ARG          
SEQRES  14 A  279  ASN HIS SER ILE PHE LEU ALA ASP ILE ASN GLN GLU ARG          
SEQRES  15 A  279  GLY VAL ASN GLU SER TYR LYS LYS ASN LEU MET ALA LEU          
SEQRES  16 A  279  LYS LYS PHE VAL MET VAL LYS PHE LEU ASN ASP THR ILE          
SEQRES  17 A  279  VAL ASP PRO VAL ASP SER GLU TRP PHE GLY PHE TYR ARG          
SEQRES  18 A  279  SER GLY GLN ALA LYS GLU THR ILE PRO LEU GLN GLU SER          
SEQRES  19 A  279  THR LEU TYR THR GLN ASP ARG LEU GLY LEU LYS ALA MET          
SEQRES  20 A  279  ASP LYS ALA GLY GLN LEU VAL PHE LEU ALA LEU GLU GLY          
SEQRES  21 A  279  ASP HIS LEU GLN LEU SER GLU GLU TRP PHE TYR ALA HIS          
SEQRES  22 A  279  ILE ILE PRO PHE LEU GLU                                      
MODRES 1EXW ASN A  197  ASN  GLYCOSYLATION SITE                                 
MODRES 1EXW ASN A  212  ASN  GLYCOSYLATION SITE                                 
MODRES 1EXW ASN A  232  ASN  GLYCOSYLATION SITE                                 
MODRES 1EXW SER A  115  SER  MODIFIED BY HSF                                    
HET    NAG  A 400      14                                                       
HET    NAG  A 410      14                                                       
HET    NAG  B 420      14                                                       
HET    NAG  B 421      14                                                       
HET    HSF  A 430      19                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     HSF 1-HEXADECYLSULFONYL FLUORIDE                                     
HETSYN     NAG NAG                                                              
FORMUL   2  NAG    4(C8 H15 N1 O6)                                              
FORMUL   5  HSF    C16 H33 O2 S1 F1                                             
FORMUL   6  HOH   *40(H2 O1)                                                    
HELIX    1   1 SER A   50  ILE A   62  1                                  13    
HELIX    2   2 THR A   75  LEU A   86  1                                  12    
HELIX    3   3 ASN A   87  LYS A  101  1                                  15    
HELIX    4   4 ASP A  102  GLN A  106  5                                   5    
HELIX    5   5 GLN A  116  CYS A  128  1                                  13    
HELIX    6   6 SER A  157  TYR A  172  1                                  16    
HELIX    7   7 ALA A  175  LEU A  180  1                                   6    
HELIX    8   8 VAL A  181  TYR A  185  5                                   5    
HELIX    9   9 ARG A  191  SER A  199  1                                   9    
HELIX   10  10 PHE A  201  ASN A  206  1                                   6    
HELIX   11  11 ASN A  212  ALA A  221  1                                  10    
HELIX   12  12 PRO A  238  PHE A  244  5                                   7    
HELIX   13  13 PRO A  257  GLU A  260  5                                   4    
HELIX   14  14 SER A  261  GLN A  266  1                                   6    
HELIX   15  15 GLY A  270  ALA A  277  1                                   8    
HELIX   16  16 SER A  293  ILE A  301  1                                   9    
HELIX   17  17 ILE A  302  GLU A  306  5                                   5    
SHEET    1   A 6 VAL A  67  SER A  69  0                                        
SHEET    2   A 6 LEU A  35  TRP A  38  1  O  LEU A  35   N  LEU A  68           
SHEET    3   A 6 TYR A 109  PHE A 114  1  O  ASN A 110   N  VAL A  36           
SHEET    4   A 6 MET A 133  VAL A 139  1  N  VAL A 134   O  TYR A 109           
SHEET    5   A 6 LYS A 224  PHE A 230  1  O  LYS A 224   N  LEU A 136           
SHEET    6   A 6 LEU A 280  LEU A 285  1  O  VAL A 281   N  MET A 227           
SHEET    1   B 2 PHE A 246  TYR A 247  0                                        
SHEET    2   B 2 THR A 255  ILE A 256 -1  N  ILE A 256   O  PHE A 246           
SSBOND   1 CYS A   45    CYS A   46                                             
SSBOND   2 CYS A   96    CYS A  128                                             
SSBOND   3 CYS A  152    CYS A  160                                             
LINK         ND2 ASN A 197                 C1  NAG A 400                        
LINK         ND2 ASN A 212                 C1  NAG A 410                        
LINK         ND2 ASN A 232                 C1  NAG B 420                        
LINK         O4  NAG B 420                 C1  NAG B 421                        
LINK         S1  HSF A 430                 OG  SER A 115                        
CISPEP   1 SER A  130    PRO A  131          0         0.09                     
CISPEP   2 ASP A  237    PRO A  238          0         1.70                     
CRYST1   69.060   69.060  128.030  90.00  90.00  90.00 P 41 2 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      0.014480  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014480  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007811        0.00000                               
END                                                                             

Send your questions or comments to :
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:
ESTHER Home Page and ACEDB Home Page
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